The Enzyme Database

Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (NC-IUBMB)

Proposed Changes to the Enzyme List

The entries below are proposed additions and amendments to the Enzyme Nomenclature list. They were prepared for the NC-IUBMB by Kristian Axelsen, Richard Cammack, Ron Caspi, Masaaki Kotera, Andrew McDonald, Gerry Moss, Dietmar Schomburg, Ida Schomburg and Keith Tipton. Comments and suggestions on these draft entries should be sent to Dr Andrew McDonald (Department of Biochemistry, Trinity College Dublin, Dublin 2, Ireland). The date on which an enzyme will be made official is appended after the EC number. To prevent confusion please do not quote new EC numbers until they are incorporated into the main list.

An asterisk before 'EC' indicates that this is an amendment to an existing enzyme rather than a new enzyme entry.


Contents

*EC 1.1.1.47 glucose 1-dehydrogenase [NAD(P)+]
*EC 1.1.1.49 glucose-6-phosphate dehydrogenase (NADP+)
*EC 1.1.1.78 methylglyoxal reductase (NADH)
*EC 1.1.1.283 methylglyoxal reductase (NADPH)
EC 1.1.1.361 glucose-6-phosphate 3-dehydrogenase
EC 1.1.1.362 aklaviketone reductase
EC 1.1.1.363 glucose-6-phosphate dehydrogenase [NAD(P)+]
EC 1.1.3.45 aclacinomycin-N oxidase
EC 1.2.7.11 2-oxoacid oxidoreductase (ferredoxin)
*EC 1.3.1.9 enoyl-[acyl-carrier-protein] reductase (NADH)
*EC 1.3.1.21 7-dehydrocholesterol reductase
*EC 1.3.1.39 enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific)
EC 1.3.1.104 enoyl-[acyl-carrier-protein] reductase (NADPH)
EC 1.3.3.14 aclacinomycin-A oxidase
*EC 1.3.8.6 glutaryl-CoA dehydrogenase (ETF)
*EC 1.3.99.32 glutaryl-CoA dehydrogenase (acceptor)
*EC 1.4.4.2 glycine dehydrogenase (aminomethyl-transferring)
EC 1.5.5.2 proline dehydrogenase
EC 1.5.99.8 transferred
*EC 1.6.3.1 NAD(P)H oxidase (H2O2-forming)
EC 1.6.3.2 NAD(P)H oxidase (H2O-forming)
EC 1.6.3.3 NADH oxidase (H2O2-forming)
EC 1.6.3.4 NADH oxidase (H2O-forming)
*EC 1.8.1.14 CoA-disulfide reductase
EC 1.8.1.19 sulfide dehydrogenase
EC 1.13.11.76 2-amino-5-chlorophenol 1,6-dioxygenase
EC 1.13.12.21 tetracenomycin-F1 monooxygenase
EC 1.14.11.42 tRNAPhe (7-(3-amino-3-carboxypropyl)wyosine37-C2)-hydroxylase
EC 1.14.11.43 (S)-dichlorprop dioxygenase (2-oxoglutarate)
EC 1.14.11.44 (R)-dichlorprop dioxygenase (2-oxoglutarate)
EC 1.14.13.180 aklavinone 12-hydroxylase
EC 1.14.13.181 13-deoxydaunorubicin hydroxylase
EC 1.14.13.182 2-heptyl-3-hydroxy-4(1H)-quinolone synthase
EC 1.14.14.14 aromatase
EC 1.14.99.48 heme oxygenase (staphylobilin-producing)
*EC 2.1.1.44 L-histidine Nα-methyltransferase
EC 2.1.1.66 deleted
EC 2.1.1.288 aklanonic acid methyltransferase
EC 2.1.3.13 ATP carbamoyltransferase
EC 2.1.3.14 tobramycin carbamoyltransferase
EC 2.3.1.227 GDP-perosamine N-acetyltransferase
EC 2.3.1.228 isovaleryl-homoserine lactone synthase
EC 2.3.1.229 4-coumaroyl-homoserine lactone synthase
*EC 2.3.2.3 lysyltransferase
*EC 2.3.2.6 lysine/arginine leucyltransferase
*EC 2.3.2.8 arginyltransferase
*EC 2.3.2.10 UDP-N-acetylmuramoylpentapeptide-lysine N6-alanyltransferase
*EC 2.3.2.11 alanylphosphatidylglycerol synthase
*EC 2.4.1.229 [Skp1-protein]-hydroxyproline N-acetylglucosaminyltransferase
*EC 2.4.1.245 α,α-trehalose synthase
*EC 2.5.1.16 spermidine synthase
*EC 2.5.1.22 spermine synthase
*EC 2.5.1.23 sym-norspermidine synthase
EC 2.5.1.111 4-hydroxyphenylpyruvate 3-dimethylallyltransferase
EC 3.1.1.95 aclacinomycin methylesterase
EC 3.1.3.91 7-methylguanosine nucleotidase
EC 3.1.3.92 kanosamine-6-phosphate phosphatase
EC 3.2.1.186 protodioscin 26-O-β-D-glucosidase
EC 3.6.3.55 tungstate-importing ATPase
*EC 3.7.1.9 2-hydroxymuconate-6-semialdehyde hydrolase
*EC 4.1.2.33 fucosterol-epoxide lyase
EC 4.1.2.54 L-threo-3-deoxy-hexylosonate aldolase
EC 4.1.3.44 tRNA 4-demethylwyosine synthase (AdoMet-dependent)
EC 4.2.1.4 deleted
EC 4.2.1.145 capreomycidine synthase
EC 4.2.1.146 L-galactonate dehydratase
EC 4.2.3.144 geranyllinalool synthase
EC 4.4.1.27 carbon disulfide lyase
EC 5.1.3.26 N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol 4-epimerase
EC 5.3.1.29 ribose 1,5-bisphosphate isomerase
EC 5.4.99.59 dTDP-fucopyranose mutase
EC 5.5.1.23 aklanonic acid methyl ester cyclase
EC 6.3.1.16 transferred
EC 6.3.3.6 carbapenam-3-carboxylate synthase
*EC 6.5.1.4 RNA 3′-terminal-phosphate cyclase (ATP)
EC 6.5.1.5 RNA 3′-terminal-phosphate cyclase (GTP)


*EC 1.1.1.47
Accepted name: glucose 1-dehydrogenase [NAD(P)+]
Reaction: D-glucose + NAD(P)+ = D-glucono-1,5-lactone + NAD(P)H + H+
Other name(s): D-glucose dehydrogenase (NAD(P)+); hexose phosphate dehydrogenase; β-D-glucose:NAD(P)+ 1-oxidoreductase; glucose 1-dehydrogenase
Systematic name: D-glucose:NAD(P)+ 1-oxidoreductase
Comments: This enzyme has similar activity with either NAD+ or NADP+. cf. EC 1.1.1.118, glucose 1-dehydrogenase (NAD+) and EC 1.1.1.119, glucose 1-dehydrogenase (NADP+).
Links to other databases: BRENDA, EXPASY, GTD, IUBMB, KEGG, PDB, CAS registry number: 9028-53-9
References:
1.  Banauch, D., Brummer, W., Ebeling, W., Metz, H., Rindfrey, H., Lang, H., Leybold, K. and Rick, W. A glucose dehydrogenase for the determination of glucose concentrations in body fluids. Z. Klin. Chem. Klin. Biochem. 13 (1975) 101–107. [PMID: 810982]
2.  Brink, N.G. Beef liver glucose dehydrogenase. 1. Purification and properties. Acta Chem. Scand. 7 (1953) 1081–1089.
3.  Pauly, H.E. and Pfleiderer, G. D-Glucose dehydrogenase from Bacillus megaterium M 1286: purification, properties and structure. Hoppe-Seylers Z. Physiol. Chem. 356 (1975) 1613–1623. [PMID: 2530]
4.  Strecker, H.J. and Korkes, S. Glucose dehydrogenase. J. Biol. Chem. 196 (1952) 769–784. [PMID: 12981017]
5.  Thompson, R.E. and Carper, W.R. Glucose dehydrogenase from pig liver. I. Isolation and purification. Biochim. Biophys. Acta 198 (1970) 397–406. [PMID: 4392298]
6.  Fujita, Y., Ramaley, R. and Freese, E. Location and properties of glucose dehydrogenase in sporulating cells and spores of Bacillus subtilis. J. Bacteriol. 132 (1977) 282–293. [PMID: 21162]
[EC 1.1.1.47 created 1961, modified 2013]
 
 
*EC 1.1.1.49
Accepted name: glucose-6-phosphate dehydrogenase (NADP+)
Reaction: D-glucose 6-phosphate + NADP+ = 6-phospho-D-glucono-1,5-lactone + NADPH + H+
For diagram of the pentose phosphate pathway (early stages), click here
Other name(s): NADP-glucose-6-phosphate dehydrogenase; Zwischenferment; D-glucose 6-phosphate dehydrogenase; glucose 6-phosphate dehydrogenase (NADP); NADP-dependent glucose 6-phosphate dehydrogenase; 6-phosphoglucose dehydrogenase; Entner-Doudoroff enzyme; glucose-6-phosphate 1-dehydrogenase; G6PDH; GPD; glucose-6-phosphate dehydrogenase
Systematic name: D-glucose-6-phosphate:NADP+ 1-oxidoreductase
Comments: The enzyme catalyses a step of the pentose phosphate pathway. The enzyme is specific for NADP+. cf. EC 1.1.1.363, glucose-6-phosphate dehydrogenase [NAD(P)+] and EC 1.1.1.388, glucose-6-phosphate dehydrogenase (NAD+).
Links to other databases: BRENDA, EXPASY, GTD, IUBMB, KEGG, PDB, CAS registry number: 9001-40-5
References:
1.  Engel, H.J., Domschke, W., Alberti, M. and Domagk, G.F. Protein structure and enzymatic activity. II. Purification and properties of a crystalline glucose-6-phosphate dehydrogenase from Candida utilis. Biochim. Biophys. Acta 191 (1969) 509–516. [PMID: 5363983]
2.  Glaser, L. and Brown, D.H. Purification and properties of D-glucose-6-phosphate dehydrogenase. J. Biol. Chem. 216 (1955) 67–79. [PMID: 13252007]
3.  Julian, G.R., Wolfe, R.G. and Reithel, F.J. The enzymes of mammary gland. II. The preparation of glucose 6-phosphate dehydrogenase. J. Biol. Chem. 236 (1961) 754–758. [PMID: 13790996]
4.  Noltmann, E.A., Gubler, C.J. and Kuby, S.A. Glucose 6-phosphate dehydrogenase (Zwischenferment). I. Isolation of the crystalline enzyme from yeast. J. Biol. Chem. 236 (1961) 1225–1230. [PMID: 13729473]
5.  Miclet, E., Stoven, V., Michels, P.A., Opperdoes, F.R., Lallemand, J.-Y. and Duffieux, F. NMR spectroscopic analysis of the first two steps of the pentose-phosphate pathway elucidates the role of 6-phosphogluconolactonase. J. Biol. Chem. 276 (2001) 34840–34846. [PMID: 11457850]
6.  Olavarria, K., Valdes, D. and Cabrera, R. The cofactor preference of glucose-6-phosphate dehydrogenase from Escherichia coli – modeling the physiological production of reduced cofactors. FEBS J. 279 (2012) 2296–2309. [PMID: 22519976]
7.  Hansen, T., Schlichting, B. and Schonheit, P. Glucose-6-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima: expression of the g6pd gene and characterization of an extremely thermophilic enzyme. FEMS Microbiol. Lett. 216 (2002) 249–253. [PMID: 12435510]
8.  Ibraheem, O., Adewale, I.O. and Afolayan, A. Purification and properties of glucose 6-phosphate dehydrogenase from Aspergillus aculeatus. J. Biochem. Mol. Biol. 38 (2005) 584–590. [PMID: 16202239]
9.  Iyer, R.B., Wang, J. and Bachas, L.G. Cloning, expression, and characterization of the gsdA gene encoding thermophilic glucose-6-phosphate dehydrogenase from Aquifex aeolicus. Extremophiles 6 (2002) 283–289. [PMID: 12215813]
10.  Cho, S.W. and Joshi, J.G. Characterization of glucose-6-phosphate dehydrogenase isozymes from human and pig brain. Neuroscience 38 (1990) 819–828. [PMID: 2270145]
[EC 1.1.1.49 created 1961, modified 2013, modified 2015]
 
 
*EC 1.1.1.78
Accepted name: methylglyoxal reductase (NADH)
Reaction: (R)-lactaldehyde + NAD+ = 2-oxopropanal + NADH + H+
Glossary: 2-oxopropanal = methylglyoxal
Other name(s): methylglyoxal reductase; D-lactaldehyde dehydrogenase; methylglyoxal reductase (NADH-dependent)
Systematic name: (R)-lactaldehyde:NAD+ oxidoreductase
Comments: This mammalian enzyme differs from the yeast enzyme, EC 1.1.1.283, methylglyoxal reductase (NADPH-dependent), by its coenzyme requirement, reaction direction, and enantiomeric preference.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 37250-16-1
References:
1.  Ting, S.-M., Miller, O.N. and Sellinger, O.Z. The metabolism of lactaldehyde. VII. The oxidation of D-lactaldehyde in rat liver. Biochim. Biophys. Acta 97 (1965) 407–415. [PMID: 14323585]
2.  Ray, M. and Ray, S. Purification and partial characterization of a methylglyoxal reductase from goat liver. Biochim. Biophys. Acta 802 (1984) 119–127. [PMID: 6386056]
[EC 1.1.1.78 created 1972, modified 2005, modified 2013]
 
 
*EC 1.1.1.283
Accepted name: methylglyoxal reductase (NADPH)
Reaction: (S)-lactaldehyde + NADP+ = 2-oxopropanal + NADPH + H+
Glossary: 2-oxopropanal = methylglyoxal
Other name(s): lactaldehyde dehydrogenase (NADP+); GRE2 (gene name); methylglyoxal reductase (NADPH-dependent); lactaldehyde:NADP+ oxidoreductase
Systematic name: (S)-lactaldehyde:NADP+ oxidoreductase
Comments: The enzyme from the yeast Saccharomyces cerevisiae catalyses the reduction of a keto group in a number of compounds, forming enantiopure products. Among the substrates are methylglyoxal (which is reduced to (S)-lactaldehyde) [1,2], 3-methylbutanal [3], hexane-2,5-dione [4] and 3-chloro-1-phenylpropan-1-one [5]. The enzyme differs from EC 1.1.1.78, methylglyoxal reductase (NADH), which is found in mammals, by its coenzyme requirement, reaction direction, and enantiomeric preference.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 78310-66-4
References:
1.  Murata, K., Fukuda, Y., Simosaka, M., Watanabe, K., Saikusa, T. and Kimura, A. Metabolism of 2-oxoaldehyde in yeasts. Purification and characterization of NADPH-dependent methylglyoxal-reducing enzyme from Saccharomyces cerevisiae. Eur. J. Biochem. 151 (1985) 631–636. [PMID: 3896793]
2.  Chen, C.N., Porubleva, L., Shearer, G., Svrakic, M., Holden, L.G., Dover, J.L., Johnston, M., Chitnis, P.R. and Kohl, D.H. Associating protein activities with their genes: rapid identification of a gene encoding a methylglyoxal reductase in the yeast Saccharomyces cerevisiae. Yeast 20 (2003) 545–554. [PMID: 12722185]
3.  Hauser, M., Horn, P., Tournu, H., Hauser, N.C., Hoheisel, J.D., Brown, A.J. and Dickinson, J.R. A transcriptome analysis of isoamyl alcohol-induced filamentation in yeast reveals a novel role for Gre2p as isovaleraldehyde reductase. FEMS Yeast Res. 7 (2007) 84–92. [PMID: 16999827]
4.  Muller, M., Katzberg, M., Bertau, M. and Hummel, W. Highly efficient and stereoselective biosynthesis of (2S,5S)-hexanediol with a dehydrogenase from Saccharomyces cerevisiae. Org. Biomol. Chem. 8 (2010) 1540–1550. [PMID: 20237665]
5.  Choi, Y.H., Choi, H.J., Kim, D., Uhm, K.N. and Kim, H.K. Asymmetric synthesis of (S)-3-chloro-1-phenyl-1-propanol using Saccharomyces cerevisiae reductase with high enantioselectivity. Appl. Microbiol. Biotechnol. 87 (2010) 185–193. [PMID: 20111861]
6.  Breicha, K., Muller, M., Hummel, W. and Niefind, K. Crystallization and preliminary crystallographic analysis of Gre2p, an NADP(+)-dependent alcohol dehydrogenase from Saccharomyces cerevisiae. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 66 (2010) 838–841. [PMID: 20606287]
[EC 1.1.1.283 created 2005, modified 2013]
 
 
EC 1.1.1.361
Accepted name: glucose-6-phosphate 3-dehydrogenase
Reaction: D-glucose 6-phosphate + NAD+ = 3-dehydro-D-glucose 6-phosphate + NADH + H+
For diagram of kanosamine biosynthesis, click here
Glossary: kanosamine = 3-amino-3-deoxy-D-glucose
Other name(s): ntdC (gene name)
Systematic name: D-glucose-6-phosphate:NAD+ oxidoreductase
Comments: The enzyme, found in the bacterium Bacillus subtilis, is involved in a kanosamine biosynthesis pathway.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Vetter, N.D., Langill, D.M., Anjum, S., Boisvert-Martel, J., Jagdhane, R.C., Omene, E., Zheng, H., van Straaten, K.E., Asiamah, I., Krol, E.S., Sanders, D.A. and Palmer, D.R. A previously unrecognized kanosamine biosynthesis pathway in Bacillus subtilis. J. Am. Chem. Soc. 135 (2013) 5970–5973. [PMID: 23586652]
[EC 1.1.1.361 created 2013]
 
 
EC 1.1.1.362
Accepted name: aklaviketone reductase
Reaction: aklavinone + NADP+ = aklaviketone + NADPH + H+
For diagram of aflatoxin biosynthesis, click here
Glossary: aklavinone = methyl (1R,2R,4S)-2-ethyl-2,4,5,7-tetrahydroxy-6,11-dioxo-1,2,3,4,6,11-hexahydrotetracene-1-carboxylate
aklaviketone = methyl (1R,2R)-2-ethyl-2,5,7-trihydroxy-4,6,11-trioxo-1,2,3,4,6,11-hexahydrotetracene-1-carboxylate
Other name(s): dauE (gene name); aknU (gene name)
Systematic name: aklavinone:NADP+ oxidoreductase
Comments: The enzyme is involved in the synthesis of the aklavinone aglycone, a common precursor for several anthracycline antibiotics including aclacinomycins, daunorubicin and doxorubicin. The enzyme from the Gram-negative bacterium Streptomyces sp. C5 produces daunomycin.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Dickens, M.L., Ye, J. and Strohl, W.R. Cloning, sequencing, and analysis of aklaviketone reductase from Streptomyces sp. strain C5. J. Bacteriol. 178 (1996) 3384–3388. [PMID: 8655529]
[EC 1.1.1.362 created 2013]
 
 
EC 1.1.1.363
Accepted name: glucose-6-phosphate dehydrogenase [NAD(P)+]
Reaction: D-glucose 6-phosphate + NAD(P)+ = 6-phospho-D-glucono-1,5-lactone + NAD(P)H + H+
Other name(s): G6PDH; G6PD; Glc6PD
Systematic name: D-glucose-6-phosphate:NAD(P)+ 1-oxidoreductase
Comments: The enzyme catalyses a step of the pentose phosphate pathway. The enzyme from the Gram-positive bacterium Leuconostoc mesenteroides prefers NADP+ while the enzyme from the Gram-negative bacterium Gluconacetobacter xylinus prefers NAD+. cf. EC 1.1.1.49, glucose-6-phosphate dehydrogenase (NADP+) and EC 1.1.1.388, glucose-6-phosphate dehydrogenase (NAD+).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Olive, C., Geroch, M.E. and Levy, H.R. Glucose 6-phosphate dehydrogenase from Leuconostoc mesenteroides. Kinetic studies. J. Biol. Chem. 246 (1971) 2047–2057. [PMID: 4396688]
2.  Lee, W.T. and Levy, H.R. Lysine-21 of Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase participates in substrate binding through charge-charge interaction. Protein Sci. 1 (1992) 329–334. [PMID: 1304341]
3.  Cosgrove, M.S., Naylor, C., Paludan, S., Adams, M.J. and Levy, H.R. On the mechanism of the reaction catalyzed by glucose 6-phosphate dehydrogenase. Biochemistry 37 (1998) 2759–2767. [PMID: 9485426]
4.  Ragunathan, S. and Levy, H.R. Purification and characterization of the NAD-preferring glucose 6-phosphate dehydrogenase from Acetobacter hansenii (Acetobacter xylinum). Arch. Biochem. Biophys. 310 (1994) 360–366. [PMID: 8179320]
[EC 1.1.1.363 created 2013, modified 2015]
 
 
EC 1.1.3.45
Accepted name: aclacinomycin-N oxidase
Reaction: aclacinomycin N + O2 = aclacinomycin A + H2O2
For diagram of aclacinomycin A and Y biosynthesis, click here
Glossary: aclacinomycin N = 2-ethyl-2,5,7-trihydroxy-6,11-dioxo-4-[[2,3,6-trideoxy-4-O-[2,6-dideoxy-4-O-[(2S,5S,6S)-5-hydroxy-6-methyltetrahydro-2H-pyran-2-yl]-α-L-lyxo-hexopyranosyl]-3-(dimethylamino)-α-L-lyxo-hexopyranosyl]oxy]-1,2,3,4,6,11-hexahydronaphthacene-1-carboxylic acid methyl ester
aclacinomycin A = 2-ethyl-2,5,7-trihydroxy-6,11-dioxo-4-[[2,3,6-trideoxy-4-O-[2,6-dideoxy-4-O-[(2R,6S)-6-methyl-5-oxotetrahydro-2H-pyran-2-yl]-α-L-lyxo-hexopyranosyl]-3-(dimethylamino)-α-L-lyxo-hexopyranosyl]oxy]-1,2,3,4,6,11-hexahydronaphthacene-1-carboxylic acid methyl ester
Other name(s): AknOx (ambiguous); aclacinomycin oxidoreductase (ambiguous)
Systematic name: aclacinomycin-N:oxygen oxidoreductase
Comments: A flavoprotein (FAD). This bifunctional enzyme is a secreted flavin-dependent enzyme that is involved in the modification of the terminal sugar residues in the biosynthesis of aclacinomycins. The enzyme utilizes the same active site to catalyse the oxidation of the rhodinose moiety of aclacinomycin N to the cinerulose A moiety of aclacinomycin A and the oxidation of the latter to the L-aculose moiety of aclacinomycin Y (cf. EC 1.3.3.14, aclacinomycin A oxidase).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Alexeev, I., Sultana, A., Mantsala, P., Niemi, J. and Schneider, G. Aclacinomycin oxidoreductase (AknOx) from the biosynthetic pathway of the antibiotic aclacinomycin is an unusual flavoenzyme with a dual active site. Proc. Natl. Acad. Sci. USA 104 (2007) 6170–6175. [PMID: 17395717]
2.  Sultana, A., Alexeev, I., Kursula, I., Mantsala, P., Niemi, J. and Schneider, G. Structure determination by multiwavelength anomalous diffraction of aclacinomycin oxidoreductase: indications of multidomain pseudomerohedral twinning. Acta Crystallogr. D Biol. Crystallogr. 63 (2007) 149–159. [PMID: 17242508]
[EC 1.1.3.45 created 2013]
 
 
EC 1.2.7.11
Accepted name: 2-oxoacid oxidoreductase (ferredoxin)
Reaction: a 2-oxocarboxylate + CoA + 2 oxidized ferredoxin = an acyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
Other name(s): OFOR
Systematic name: 2-oxocarboxylate:ferredoxin 2-oxidoreductase (decarboxylating, CoA-acylating)
Comments: Contains thiamine diphosphate and [4Fe-4S] clusters [2]. This enzyme is a member of the 2-oxoacid oxidoreductases, a family of enzymes that oxidatively decarboxylate different 2-oxoacids to form their CoA derivatives, and are differentiated based on their substrate specificity. For example, see EC 1.2.7.3, 2-oxoglutarate synthase and EC 1.2.7.7, 3-methyl-2-oxobutanoate dehydrogenase (ferredoxin).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Kerscher, L. and Oesterhelt, D. Purification and properties of two 2-oxoacid:ferredoxin oxidoreductases from Halobacterium halobium. Eur. J. Biochem. 116 (1981) 587–594. [PMID: 6266826]
2.  Zhang, Q., Iwasaki, T., Wakagi, T. and Oshima, T. 2-oxoacid:ferredoxin oxidoreductase from the thermoacidophilic archaeon, Sulfolobus sp. strain 7. J. Biochem. 120 (1996) 587–599. [PMID: 8902625]
3.  Fukuda, E., Kino, H., Matsuzawa, H. and Wakagi, T. Role of a highly conserved YPITP motif in 2-oxoacid:ferredoxin oxidoreductase: heterologous expression of the gene from Sulfolobus sp.strain 7, and characterization of the recombinant and variant enzymes. Eur. J. Biochem. 268 (2001) 5639–5646. [PMID: 11683888]
4.  Fukuda, E. and Wakagi, T. Substrate recognition by 2-oxoacid:ferredoxin oxidoreductase from Sulfolobus sp. strain 7. Biochim. Biophys. Acta 1597 (2002) 74–80. [PMID: 12009405]
5.  Nishizawa, Y., Yabuki, T., Fukuda, E. and Wakagi, T. Gene expression and characterization of two 2-oxoacid:ferredoxin oxidoreductases from Aeropyrum pernix K1. FEBS Lett. 579 (2005) 2319–2322. [PMID: 15848165]
6.  Park, Y.J., Yoo, C.B., Choi, S.Y. and Lee, H.B. Purifications and characterizations of a ferredoxin and its related 2-oxoacid:ferredoxin oxidoreductase from the hyperthermophilic archaeon, Sulfolobus solfataricus P1. J. Biochem. Mol. Biol. 39 (2006) 46–54. [PMID: 16466637]
[EC 1.2.7.11 created 2013]
 
 
*EC 1.3.1.9
Accepted name: enoyl-[acyl-carrier-protein] reductase (NADH)
Reaction: an acyl-[acyl-carrier protein] + NAD+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH + H+
Other name(s): enoyl-[acyl carrier protein] reductase; enoyl-ACP reductase; NADH-enoyl acyl carrier protein reductase; NADH-specific enoyl-ACP reductase; acyl-[acyl-carrier-protein]:NAD+ oxidoreductase; fabI (gene name); inhA (gene name)
Systematic name: acyl-[acyl-carrier protein]:NAD+ oxidoreductase
Comments: The enzyme catalyses an essential step in fatty acid biosynthesis, the reduction of the 2,3-double bond in enoyl-acyl-[acyl-carrier-protein] derivatives of the elongating fatty acid moiety. The enzyme from the bacterium Escherichia coli accepts substrates with carbon chain length from 4 to 18 [3]. The enzyme from the bacterium Mycobacterium tuberculosis prefers substrates with carbon chain length from 12 to 24 carbons [4,5].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, PDB, CAS registry number: 37251-08-4
References:
1.  Shimakata, T. and Stumpf, P.K. Purification and characterizations of β-ketoacyl-[acyl-carrier-protein] reductase, β-hydroxyacyl-[acylcarrier-protein] dehydrase, and enoyl-[acyl-carrier-protein] reductase from Spinacia oleracea leaves. Arch. Biochem. Biophys. 218 (1982) 77–91. [PMID: 6756317]
2.  Weeks, G. and Wakil, S.J. Studies on the mechanism of fatty acid synthesis. 18. Preparation and general properties of the enoyl acyl carrier protein reductases from Escherichia coli. J. Biol. Chem. 243 (1968) 1180–1189. [PMID: 4384650]
3.  Yu, X., Liu, T., Zhu, F. and Khosla, C. In vitro reconstitution and steady-state analysis of the fatty acid synthase from Escherichia coli. Proc. Natl. Acad. Sci. USA 108 (2011) 18643–18648. [PMID: 22042840]
4.  Quemard, A., Sacchettini, J.C., Dessen, A., Vilcheze, C., Bittman, R., Jacobs, W.R., Jr. and Blanchard, J.S. Enzymatic characterization of the target for isoniazid in Mycobacterium tuberculosis. Biochemistry 34 (1995) 8235–8241. [PMID: 7599116]
5.  Rozwarski, D.A., Vilcheze, C., Sugantino, M., Bittman, R. and Sacchettini, J.C. Crystal structure of the Mycobacterium tuberculosis enoyl-ACP reductase, InhA, in complex with NAD+ and a C16 fatty acyl substrate. J. Biol. Chem. 274 (1999) 15582–15589. [PMID: 10336454]
[EC 1.3.1.9 created 1972, modified 2013]
 
 
*EC 1.3.1.21
Accepted name: 7-dehydrocholesterol reductase
Reaction: cholesterol + NADP+ = cholesta-5,7-dien-3β-ol + NADPH + H+
For diagram of sterol ring b, c, D modification, click here
Other name(s): DHCR7 (gene name); 7-DHC reductase; 7-dehydrocholesterol dehydrogenase/cholesterol oxidase; Δ7-sterol reductase
Systematic name: cholesterol:NADP+ Δ7-oxidoreductase
Comments: The enzyme is part of the cholesterol biosynthesis pathway.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 9080-21-1
References:
1.  Dempsey, M.E., Seaton, J.D., Schroepfer, G.J. and Trockman, R.W. The intermediary role of Δ5,7-cholestadien-3β-ol in cholesterol biosynthesis. J. Biol. Chem. 239 (1964) 1381–1387. [PMID: 14189869]
2.  Moebius, F.F., Fitzky, B.U., Lee, J.N., Paik, Y.K. and Glossmann, H. Molecular cloning and expression of the human Δ7-sterol reductase. Proc. Natl. Acad. Sci. USA 95 (1998) 1899–1902. [PMID: 9465114]
[EC 1.3.1.21 created 1972, modified 2013]
 
 
*EC 1.3.1.39
Accepted name: enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific)
Reaction: an acyl-[acyl-carrier protein] + NADP+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+
Other name(s): acyl-ACP dehydrogenase; enoyl-[acyl carrier protein] (reduced nicotinamide adenine dinucleotide phosphate) reductase; NADPH 2-enoyl Co A reductase; enoyl-ACp reductase; enoyl-[acyl-carrier-protein] reductase (NADPH2, A-specific); acyl-[acyl-carrier-protein]:NADP+ oxidoreductase (A-specific); enoyl-[acyl-carrier-protein] reductase (NADPH, A-specific); acyl-[acyl-carrier protein]:NADP+ oxidoreductase (A-specific)
Systematic name: acyl-[acyl-carrier protein]:NADP+ oxidoreductase (Re-specific)
Comments: This enzyme completes each cycle of fatty acid elongation by catalysing the stereospecific reduction of the double bond at position 2 of a growing fatty acid chain, while linked to an acyl-carrier protein. It is one of the activities of EC 2.3.1.85, animal fatty-acid synthase. The mammalian enzyme is Re-specific with respect to NADP+. cf. EC 1.3.1.10, enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific) and EC 1.3.1.104, enoyl-[acyl-carrier-protein] reductase (NADPH).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Dugan, R.E., Slakey, L.L. and Porter, L.W. Stereospecificity of the transfer of hydrogen from reduced nicotinamide adenine dinucleotide phosphate to the acyl chain in the dehydrogenase-catalyzed reactions of fatty acid synthesis. J. Biol. Chem. 245 (1970) 6312–6316. [PMID: 4394955]
2.  Carlisle-Moore, L., Gordon, C.R., Machutta, C.A., Miller, W.T. and Tonge, P.J. Substrate recognition by the human fatty-acid synthase. J. Biol. Chem. 280 (2005) 42612–42618. [PMID: 16215233]
[EC 1.3.1.39 created 1986, modified 2013]
 
 
EC 1.3.1.104
Accepted name: enoyl-[acyl-carrier-protein] reductase (NADPH)
Reaction: an acyl-[acyl-carrier protein] + NADP+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+
Other name(s): acyl-ACP dehydrogenase (ambiguous); enoyl-[acyl carrier protein] (reduced nicotinamide adenine dinucleotide phosphate) reductase; NADPH 2-enoyl Co A reductase; enoyl-ACP reductase (ambiguous); fabL (gene name)
Systematic name: acyl-[acyl-carrier protein]:NADP+ oxidoreductase
Comments: The enzyme completes each cycle of fatty acid elongation by catalysing the stereospecific reduction of the double bond at position 2 of a growing fatty acid chain, while linked to the acyl-carrier protein, in an NADPH-dependent manner. This entry stands for enzymes whose stereo-specificity with respect to NADP+ is not known. [cf. EC 1.3.1.39 enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific), EC 1.3.1.10, enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific) and EC 1.3.1.9, enoyl-[acyl-carrier-protein] reductase (NADH)].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, PDB
References:
1.  Heath, R.J., Su, N., Murphy, C.K. and Rock, C.O. The enoyl-[acyl-carrier-protein] reductases FabI and FabL from Bacillus subtilis. J. Biol. Chem. 275 (2000) 40128–40133. [PMID: 11007778]
2.  Kim, K.H., Park, J.K., Ha, B.H., Moon, J.H. and Kim, E.E. Crystallization and preliminary X-ray crystallographic analysis of enoyl-ACP reductase III (FabL) from Bacillus subtilis. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 63 (2007) 246–248. [PMID: 17329825]
3.  Kim, K.H., Ha, B.H., Kim, S.J., Hong, S.K., Hwang, K.Y. and Kim, E.E. Crystal structures of Enoyl-ACP reductases I (FabI) and III (FabL) from B. subtilis. J. Mol. Biol. 406 (2011) 403–415. [PMID: 21185310]
[EC 1.3.1.104 created 2013]
 
 
EC 1.3.3.14
Accepted name: aclacinomycin-A oxidase
Reaction: aclacinomycin A + O2 = aclacinomycin Y + H2O2
For diagram of aclacinomycin A and Y biosynthesis, click here
Glossary: aclacinomycin A = 2-ethyl-1,2,3,4,6,11-hexahydro-2,5,7-trihydroxy-6,11-dioxo-4-[[2,3,6-trideoxy-4-O-[2,6-dideoxy-4-O-[(2R,6S)-tetrahydro-6-methyl-5-oxo-2H-pyran-2-yl]-α-L-lyxo-hexopyranosyl]-3-(dimethylamino)-α-L-lyxo-hexopyranosyl]oxy]naphthacene-1-carboxylic acid methyl ester
aclacinomycin Y = 2-ethyl-1,2,3,4,6,11-hexahydro-2,5,7-trihydroxy-6,11-dioxo-4-[[2,3,6-trideoxy-4-O-[2,6-dideoxy-4-O-[(2R,6S)-5,6-dihydro-6-methyl-5-oxo-2H-pyran-2-yl]-α-L-lyxo-hexopyranosyl]-3-(dimethylamino)-α-L-lyxo-hexopyranosyl]oxy]naphthacene-1-carboxylic acid methyl ester
Other name(s): AknOx (ambiguous); aclacinomycin oxidoreductase (ambiguous)
Systematic name: aclacinomycin-A:oxygen oxidoreductase
Comments: A flavoprotein (FAD). This bifunctional enzyme is a secreted flavin-dependent enzyme that is involved in the modification of the terminal sugar residues in the biosynthesis of aclacinomycins. The enzyme utilizes the same active site to catalyse the oxidation of the rhodinose moiety of aclacinomycin N to the cinerulose A moiety of aclacinomycin A (cf. EC 1.1.3.45) and the oxidation of the latter to the L-aculose moiety of aclacinomycin Y.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Yoshimoto, A., Ogasawara, T., Kitamura, I., Oki, T., Inui, T., Takeuchi, T. and Umezawa, H. Enzymatic conversion of aclacinomycin A to Y by a specific oxidoreductase in Streptomyces. J. Antibiot. (Tokyo) 32 (1979) 472–481. [PMID: 528393]
2.  Alexeev, I., Sultana, A., Mantsala, P., Niemi, J. and Schneider, G. Aclacinomycin oxidoreductase (AknOx) from the biosynthetic pathway of the antibiotic aclacinomycin is an unusual flavoenzyme with a dual active site. Proc. Natl. Acad. Sci. USA 104 (2007) 6170–6175. [PMID: 17395717]
3.  Sultana, A., Alexeev, I., Kursula, I., Mantsala, P., Niemi, J. and Schneider, G. Structure determination by multiwavelength anomalous diffraction of aclacinomycin oxidoreductase: indications of multidomain pseudomerohedral twinning. Acta Crystallogr. D Biol. Crystallogr. 63 (2007) 149–159. [PMID: 17242508]
[EC 1.3.3.14 created 2013]
 
 
*EC 1.3.8.6
Accepted name: glutaryl-CoA dehydrogenase (ETF)
Reaction: glutaryl-CoA + electron-transfer flavoprotein = crotonyl-CoA + CO2 + reduced electron-transfer flavoprotein (overall reaction)
(1a) glutaryl-CoA + electron-transfer flavoprotein = (E)-glutaconyl-CoA + reduced electron-transfer flavoprotein
(1b) (E)-glutaconyl-CoA = crotonyl-CoA + CO2
For diagram of Benzoyl-CoA catabolism, click here
Glossary: (E)-glutaconyl-CoA = (2E)-4-carboxybut-2-enoyl-CoA
crotonyl-CoA = (E)-but-2-enoyl-CoA
Other name(s): glutaryl coenzyme A dehydrogenase; glutaryl-CoA:(acceptor) 2,3-oxidoreductase (decarboxylating); glutaryl-CoA dehydrogenase
Systematic name: glutaryl-CoA:electron-transfer flavoprotein 2,3-oxidoreductase (decarboxylating)
Comments: Contains FAD. The enzyme catalyses the oxidation of glutaryl-CoA to glutaconyl-CoA (which remains bound to the enzyme), and the decarboxylation of the latter to crotonyl-CoA (cf. EC 4.1.1.70, glutaconyl-CoA decarboxylase). FAD is the electron acceptor in the oxidation of the substrate, and its reoxidation by electron-transfer flavoprotein completes the catalytic cycle. The anaerobic, sulfate-reducing bacterium Desulfococcus multivorans contains two glutaryl-CoA dehydrogenases: a decarboxylating enzyme (this entry), and a non-decarboxylating enzyme that only catalyses the oxidation to glutaconyl-CoA (EC 1.3.99.32).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, PDB, UM-BBD, CAS registry number: 37255-38-2
References:
1.  Besrat, A., Polan, C.E. and Henderson, L.M. Mammalian metabolism of glutaric acid. J. Biol. Chem. 244 (1969) 1461–1467. [PMID: 4304226]
2.  Hartel, U., Eckel, E., Koch, J., Fuchs, G., Linder, D. and Buckel, W. Purification of glutaryl-CoA dehydrogenase from Pseudomonas sp., an enzyme involved in the anaerobic degradation of benzoate. Arch. Microbiol. 159 (1993) 174–181. [PMID: 8439237]
3.  Dwyer, T.M., Zhang, L., Muller, M., Marrugo, F. and Frerman, F. The functions of the flavin contact residues, αArg249 and βTyr16, in human electron transfer flavoprotein. Biochim. Biophys. Acta 1433 (1999) 139–152. [PMID: 10446367]
4.  Rao, K.S., Albro, M., Dwyer, T.M. and Frerman, F.E. Kinetic mechanism of glutaryl-CoA dehydrogenase. Biochemistry 45 (2006) 15853–15861. [PMID: 17176108]
[EC 1.3.8.6 created 1972 as EC 1.3.99.7, transferred 2012 to EC 1.3.8.6, modified 2013]
 
 
*EC 1.3.99.32
Accepted name: glutaryl-CoA dehydrogenase (acceptor)
Reaction: glutaryl-CoA + acceptor = (E)-glutaconyl-CoA + reduced acceptor
Glossary: (E)-glutaconyl-CoA = (2E)-4-carboxybut-2-enoyl-CoA
Other name(s): GDHDes; nondecarboxylating glutaryl-coenzyme A dehydrogenase; nondecarboxylating glutaconyl-coenzyme A-forming GDH; glutaryl-CoA dehydrogenase (non-decarboxylating)
Systematic name: glutaryl-CoA:acceptor 2,3-oxidoreductase (non-decarboxylating)
Comments: The enzyme contains FAD. The anaerobic, sulfate-reducing bacterium Desulfococcus multivorans contains two glutaryl-CoA dehydrogenases: a decarboxylating enzyme (EC 1.3.8.6), and a nondecarboxylating enzyme (this entry). The two enzymes cause different structural changes around the glutaconyl carboxylate group, primarily due to the presence of either a tyrosine or a valine residue, respectively, at the active site.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Wischgoll, S., Taubert, M., Peters, F., Jehmlich, N., von Bergen, M. and Boll, M. Decarboxylating and nondecarboxylating glutaryl-coenzyme A dehydrogenases in the aromatic metabolism of obligately anaerobic bacteria. J. Bacteriol. 191 (2009) 4401–4409. [PMID: 19395484]
2.  Wischgoll, S., Demmer, U., Warkentin, E., Gunther, R., Boll, M. and Ermler, U. Structural basis for promoting and preventing decarboxylation in glutaryl-coenzyme A dehydrogenases. Biochemistry 49 (2010) 5350–5357. [PMID: 20486657]
[EC 1.3.99.32 created 2012, modified 2013]
 
 
*EC 1.4.4.2
Accepted name: glycine dehydrogenase (aminomethyl-transferring)
Reaction: glycine + [glycine-cleavage complex H protein]-N6-lipoyl-L-lysine = [glycine-cleavage complex H protein]-S-aminomethyl-N6-dihydrolipoyl-L-lysine + CO2
For diagram of glycine cleavage system, click here
Glossary: dihydrolipoyl group
Other name(s): P-protein; glycine decarboxylase; glycine-cleavage complex; glycine:lipoylprotein oxidoreductase (decarboxylating and acceptor-aminomethylating); protein P1; glycine dehydrogenase (decarboxylating); glycine cleavage system P-protein; glycine-cleavage complex P-protein
Systematic name: glycine:H-protein-lipoyllysine oxidoreductase (decarboxylating, acceptor-amino-methylating)
Comments: A pyridoxal-phosphate protein. A component of the glycine cleavage system, which is composed of four components that only loosely associate: the P protein (EC 1.4.4.2), the T protein (EC 2.1.2.10, aminomethyltransferase), the L protein (EC 1.8.1.4, dihydrolipoyl dehydrogenase) and the lipoyl-bearing H protein [3]. Previously known as glycine synthase.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, PDB, CAS registry number: 37259-67-9
References:
1.  Hiraga, K. and Kikuchi, G. The mitochondrial glycine cleavage system. Functional association of glycine decarboxylase and aminomethyl carrier protein. J. Biol. Chem. 255 (1980) 11671–11676. [PMID: 7440563]
2.  Perham, R.N. Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions. Annu. Rev. Biochem. 69 (2000) 961–1004. [PMID: 10966480]
3.  Nesbitt, N.M., Baleanu-Gogonea, C., Cicchillo, R.M., Goodson, K., Iwig, D.F., Broadwater, J.A., Haas, J.A., Fox, B.G. and Booker, S.J. Expression, purification, and physical characterization of Escherichia coli lipoyl(octanoyl)transferase. Protein Expr. Purif. 39 (2005) 269–282. [PMID: 15642479]
[EC 1.4.4.2 created 1984, modified 2003, modified 2006, modified 2013]
 
 
EC 1.5.5.2
Accepted name: proline dehydrogenase
Reaction: L-proline + a quinone = (S)-1-pyrroline-5-carboxylate + a quinol
Other name(s): L-proline dehydrogenase; L-proline:(acceptor) oxidoreductase
Systematic name: L-proline:quinone oxidoreductase
Comments: A flavoprotein (FAD). The electrons from L-proline are transferred to the FAD cofactor, and from there to a quinone acceptor [3]. In many organisms, ranging from bacteria to mammals, proline is oxidized to glutamate in a two-step process involving this enzyme and EC 1.2.1.88, L-glutamate γ-semialdehyde dehydrogenase. Both activities are carried out by the same enzyme in enterobacteria.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, PDB, CAS registry number: 9050-70-8
References:
1.  Scarpulla, R.C. and Sofer, R.L. Membrane-bound proline dehydrogenase from Escherichia coli. Solubilization, purification, and characterization. J. Biol. Chem. 253 (1978) 5997–6001. [PMID: 355248]
2.  Brown, E.D. and Wood, J.M. Redesigned purification yields a fully functional PutA protein dimer from Escherichia coli. J. Biol. Chem. 267 (1992) 13086–13092. [PMID: 1618807]
3.  Moxley, M.A., Tanner, J.J. and Becker, D.F. Steady-state kinetic mechanism of the proline:ubiquinone oxidoreductase activity of proline utilization A (PutA) from Escherichia coli. Arch. Biochem. Biophys. 516 (2011) 113–120. [PMID: 22040654]
[EC 1.5.5.2 created 1980 as EC 1.5.99.8, transferred 2013 to EC 1.5.5.2]
 
 
EC 1.5.99.8
Transferred entry: proline dehydrogenase. Now EC 1.5.5.2, proline dehydrogenase.
[EC 1.5.99.8 created 1980, deleted 2013]
 
 
*EC 1.6.3.1
Accepted name: NAD(P)H oxidase (H2O2-forming)
Reaction: NAD(P)H + H+ + O2 = NAD(P)+ + H2O2
Other name(s): THOX2; ThOX; dual oxidase; p138tox; thyroid NADPH oxidase; thyroid oxidase; thyroid oxidase 2; NADPH oxidase; NAD(P)H:oxygen oxidoreductase; NAD(P)H oxidase
Systematic name: NAD(P)H:oxygen oxidoreductase (H2O2-forming)
Comments: Requires FAD, heme and calcium. When calcium is present, this transmembrane glycoprotein generates H2O2 by transfering electrons from intracellular NAD(P)H to extracellular molecular oxygen. The electron bridge within the enzyme contains one molecule of FAD and probably two heme groups. This flavoprotein is expressed at the apical membrane of thyrocytes, and provides H2O2 for the thyroid peroxidase-catalysed biosynthesis of thyroid hormones.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 77106-92-4
References:
1.  Moreno, J.C., Bikker, H., Kempers, M.J., van Trotsenburg, A.S., Baas, F., de Vijlder, J.J., Vulsma, T. and Ris-Stalpers, C. Inactivating mutations in the gene for thyroid oxidase 2 (THOX2) and congenital hypothyroidism. N. Engl. J. Med. 347 (2002) 95–102. [PMID: 12110737]
2.  De Deken, X., Wang, D., Dumont, J.E. and Miot, F. Characterization of ThOX proteins as components of the thyroid H2O2-generating system. Exp. Cell 273 (2002) 187–196. [PMID: 11822874]
3.  De Deken, X., Wang, D., Many, M.C., Costagliola, S., Libert, F., Vassart, G., Dumont, J.E. and Miot, F. Cloning of two human thyroid cDNAs encoding new members of the NADPH oxidase family. J. Biol. Chem. 275 (2000) 23227–23233. [PMID: 10806195]
4.  Dupuy, C., Ohayon, R., Valent, A., Noel-Hudson, M.S., Deme, D. and Virion, A. Purification of a novel flavoprotein involved in the thyroid NADPH oxidase. Cloning of the porcine and human cDNAs. J. Biol. Chem. 274 (1999) 37265–37269. [PMID: 10601291]
5.  Leseney, A.M., Deme, D., Legue, O., Ohayon, R., Chanson, P., Sales, J.P., Pires de Carvalho, D., Dupuy, C. and Virion, A. Biochemical characterization of a Ca2+/NAD(P)H-dependent H2O2 generator in human thyroid tissue. Biochimie 81 (1999) 373–380. [PMID: 10401672]
6.  Dupuy, C., Virion, A., Ohayon, R., Kaniewski, J., Deme, D. and Pommier, J. Mechanism of hydrogen peroxide formation catalyzed by NADPH oxidase in thyroid plasma membrane. J. Biol. Chem. 266 (1991) 3739–3743. [PMID: 1995628]
[EC 1.6.3.1 created 2003, modified 2013]
 
 
EC 1.6.3.2
Accepted name: NAD(P)H oxidase (H2O-forming)
Reaction: 2 NAD(P)H + 2 H+ + O2 = 2 NAD(P)+ + 2 H2O
Systematic name: NAD(P)H:oxygen oxidoreductase (H2O-forming)
Comments: A flavoprotein (FAD). NADPH is a better substrate than NADH [1,3]. By removal of oxygen the enzyme is involved in aerobic tolerance in the thermophilic anaerobic archaeon Thermococcus profundus and in Giardia intestinalis, a microaerophilic single-celled parasite of the order Diplomonadida.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Brown, D.M., Upcroft, J.A. and Upcroft, P. A H2O-producing NADH oxidase from the protozoan parasite Giardia duodenalis. Eur. J. Biochem. 241 (1996) 155–161. [PMID: 8898901]
2.  Li, L. and Wang, C.C. A likely molecular basis of the susceptibility of Giardia lamblia towards oxygen. Mol. Microbiol. 59 (2006) 202–211. [PMID: 16359329]
3.  Jia, B., Park, S.C., Lee, S., Pham, B.P., Yu, R., Le, T.L., Han, S.W., Yang, J.K., Choi, M.S., Baumeister, W. and Cheong, G.W. Hexameric ring structure of a thermophilic archaeon NADH oxidase that produces predominantly H2O. FEBS J. 275 (2008) 5355–5366. [PMID: 18959761]
4.  Jia, B., Lee, S., Pham, B.P., Cho, Y.S., Yang, J.K., Byeon, H.S., Kim, J.C. and Cheong, G.W. An archaeal NADH oxidase causes damage to both proteins and nucleic acids under oxidative stress. Mol. Cells 29 (2010) 363–371. [PMID: 20213313]
[EC 1.6.3.2 created 2013]
 
 
EC 1.6.3.3
Accepted name: NADH oxidase (H2O2-forming)
Reaction: NADH + H+ + O2 = NAD+ + H2O2
Other name(s): NOX-1; H2O2-forming NADH oxidase
Systematic name: NADH:oxygen oxidoreductase (H2O2-forming)
Comments: A flavoprotein (FAD). The bacterium Streptococcus mutans contains two distinct NADH oxidases, a H2O2-forming enzyme and a H2O-forming enzyme (cf. EC 1.6.3.4, NADH oxidase (H2O-forming)) [1]. The enzymes from the anaerobic archaea Methanocaldococcus jannaschii [6] and Pyrococcus furiosus [3] also produce low amounts of H2O. Unlike EC 1.6.3.1 (NAD(P)H oxidase) it has no activity towards NADPH.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Higuchi, M., Shimada, M., Yamamoto, Y., Hayashi, T., Koga, T. and Kamio, Y. Identification of two distinct NADH oxidases corresponding to H2O2-forming oxidase and H2O-forming oxidase induced in Streptococcus mutans. J. Gen. Microbiol. 139 (1993) 2343–2351. [PMID: 8254304]
2.  Ward, D.E., Donnelly, C.J., Mullendore, M.E., van der Oost, J., de Vos, W.M. and Crane, E.J., 3rd. The NADH oxidase from Pyrococcus furiosus. Implications for the protection of anaerobic hyperthermophiles against oxidative stress. Eur. J. Biochem. 268 (2001) 5816–5823. [PMID: 11722568]
3.  Kengen, S.W., van der Oost, J. and de Vos, W.M. Molecular characterization of H2O2-forming NADH oxidases from Archaeoglobus fulgidus. Eur. J. Biochem. 270 (2003) 2885–2894. [PMID: 12823559]
4.  Yang, X. and Ma, K. Characterization of an exceedingly active NADH oxidase from the anaerobic hyperthermophilic bacterium Thermotoga maritima. J. Bacteriol. 189 (2007) 3312–3317. [PMID: 17293421]
5.  Hirano, J., Miyamoto, K. and Ohta, H. Purification and characterization of thermostable H2O2-forming NADH oxidase from 2-phenylethanol-assimilating Brevibacterium sp. KU1309. Appl. Microbiol. Biotechnol. 80 (2008) 71–78. [PMID: 18521590]
6.  Case, C.L., Rodriguez, J.R. and Mukhopadhyay, B. Characterization of an NADH oxidase of the flavin-dependent disulfide reductase family from Methanocaldococcus jannaschii. Microbiology 155 (2009) 69–79. [PMID: 19118348]
[EC 1.6.3.3 created 2013]
 
 
EC 1.6.3.4
Accepted name: NADH oxidase (H2O-forming)
Reaction: 2 NADH + 2 H+ + O2 = 2 NAD+ + 2 H2O
Other name(s): H2O-forming NADH oxidase; Nox-2
Systematic name: NADH:oxygen oxidoreductase (H2O-forming)
Comments: A flavoprotein (FAD). The bacterium Streptococcus mutans contains two distinct NADH oxidases, a H2O-forming enzyme and a H2O2-forming enzyme (cf. EC 1.6.3.3, NADH oxidase (H2O2-forming)) [1].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Schmidt, H.L., Stocklein, W., Danzer, J., Kirch, P. and Limbach, B. Isolation and properties of an H2O-forming NADH oxidase from Streptococcus faecalis. Eur. J. Biochem. 156 (1986) 149–155. [PMID: 3082630]
2.  Higuchi, M., Shimada, M., Yamamoto, Y., Hayashi, T., Koga, T. and Kamio, Y. Identification of two distinct NADH oxidases corresponding to H2O2-forming oxidase and H2O-forming oxidase induced in Streptococcus mutans. J. Gen. Microbiol. 139 (1993) 2343–2351. [PMID: 8254304]
3.  Matsumoto, J., Higuchi, M., Shimada, M., Yamamoto, Y. and Kamio, Y. Molecular cloning and sequence analysis of the gene encoding the H2O-forming NADH oxidase from Streptococcus mutans. Biosci. Biotechnol. Biochem. 60 (1996) 39–43. [PMID: 8824824]
4.  Kawasaki, S., Ishikura, J., Chiba, D., Nishino, T. and Niimura, Y. Purification and characterization of an H2O-forming NADH oxidase from Clostridium aminovalericum: existence of an oxygen-detoxifying enzyme in an obligate anaerobic bacteria. Arch. Microbiol. 181 (2004) 324–330. [PMID: 15014929]
5.  Zhang, Y.W., Tiwari, M.K., Gao, H., Dhiman, S.S., Jeya, M. and Lee, J.K. Cloning and characterization of a thermostable H2O-forming NADH oxidase from Lactobacillus rhamnosus. Enzyme Microb. Technol. 50 (2012) 255–262. [PMID: 22418266]
[EC 1.6.3.4 created 2013]
 
 
*EC 1.8.1.14
Accepted name: CoA-disulfide reductase
Reaction: 2 CoA + NADP+ = CoA-disulfide + NADPH + H+
Other name(s): CoA-disulfide reductase (NADH2); NADH2:CoA-disulfide oxidoreductase; CoA:NAD+ oxidoreductase (misleading); CoADR; coenzyme A disulfide reductase
Systematic name: CoA:NADP+ oxidoreductase
Comments: A flavoprotein. Not identical with EC 1.8.1.6 (cystine reductase), EC 1.8.1.7 (glutathione-disulfide reductase) or EC 1.8.1.13 (bis-γ-glutamylcystine reductase). The enzyme from the bacterium Staphylococcus aureus has a strong preference for NADPH [3], while the bacterium Bacillus megaterium contains both NADH and NADPH-dependent enzymes [1].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, PDB, CAS registry number: 206770-55-0
References:
1.  Setlow, B. and Setlow, P. Levels of acetyl coenzyme A, reduced and oxidized coenzyme A, and coenzyme A in disulfide linkage to protein in dormant and germinated spores and growing and sporulating cells of Bacillus megaterium. J. Bacteriol. 132 (1977) 444–452. [PMID: 410791]
2.  delCardayré, S.B., Stock, K.P., Newton, G.L., Fahey, R.C. and Davies, J.E. Coenzyme A disulfide reductase, the primary low molecular weight disulfide reductase from Staphylococcus aureus. Purification and characterization of the native enzyme. J. Biol. Chem. 273 (1998) 5744–5751. [PMID: 9488707]
3.  Luba, J., Charrier, V. and Claiborne, A. Coenzyme A-disulfide reductase from Staphylococcus aureus: evidence for asymmetric behavior on interaction with pyridine nucleotides. Biochemistry 38 (1999) 2725–2737. [PMID: 10052943]
[EC 1.8.1.14 created 1992 as EC 1.6.4.10, transferred 2002 to EC 1.8.1.14, modified 2005, modified 2013]
 
 
EC 1.8.1.19
Accepted name: sulfide dehydrogenase
Reaction: hydrogen sulfide + (sulfide)n + NADP+ = (sulfide)n+1 + NADPH + H+
Other name(s): SuDH
Systematic name: hydrogen sulfide,polysulfide:NADP+ oxidoreductase
Comments: A iron-sulfur flavoprotein. In the archaeon Pyrococcus furiosus the enzyme is involved in the oxidation of NADPH which is produced in peptide degradation. The enzyme also catalyses the reduction of sulfur with lower activity.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Ma, K. and Adams, M.W. Sulfide dehydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus: a new multifunctional enzyme involved in the reduction of elemental sulfur. J. Bacteriol. 176 (1994) 6509–6517. [PMID: 7961401]
2.  Hagen, W.R., Silva, P.J., Amorim, M.A., Hagedoorn, P.L., Wassink, H., Haaker, H. and Robb, F.T. Novel structure and redox chemistry of the prosthetic groups of the iron-sulfur flavoprotein sulfide dehydrogenase from Pyrococcus furiosus; evidence for a [2Fe-2S] cluster with Asp(Cys)3 ligands. J. Biol. Inorg. Chem. 5 (2000) 527–534. [PMID: 10968624]
[EC 1.8.1.19 created 2013]
 
 
EC 1.13.11.76
Accepted name: 2-amino-5-chlorophenol 1,6-dioxygenase
Reaction: 2-amino-5-chlorophenol + O2 = 2-amino-5-chloromuconate 6-semialdehyde
Other name(s): cnbC (gene name); 2-amino-5-chlorophenol:oxygen 1,6-oxidoreductase (decyclizing)
Systematic name: 2-amino-5-chlorophenol:oxygen 1,6-oxidoreductase (ring-opening)
Comments: The enzyme, a member of the nonheme-iron(II)-dependent dioxygenase family, is an extradiol-type dioxygenase that utilizes a non-heme ferrous iron to cleave the aromatic ring at the meta position (relative to the hydroxyl substituent). The enzyme from the bacterium Comamonas testosteroni CNB-1 also has the activity of EC 1.13.11.74, 2-aminophenol 1,6-dioxygenase.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Wu, J.F., Sun, C.W., Jiang, C.Y., Liu, Z.P. and Liu, S.J. A novel 2-aminophenol 1,6-dioxygenase involved in the degradation of p-chloronitrobenzene by Comamonas strain CNB-1: purification, properties, genetic cloning and expression in Escherichia coli. Arch. Microbiol. 183 (2005) 1–8. [PMID: 15580337]
[EC 1.13.11.76 created 2013]
 
 
EC 1.13.12.21
Accepted name: tetracenomycin-F1 monooxygenase
Reaction: tetracenomycin F1 + O2 = tetracenomycin D3 + H2O
For diagram of tetracenomycin biosynthesis, click here
Glossary: tetracenomycin D3 = 3,8,10,12-tetrahydroxy-1-methyl-6,11-dioxo-6,11-dihydrotetracene-2-carboxylate = 6,11-dihydro-3,8,10,12-tetrahydroxy-1-methyl-6,11-dioxonaphthacene-2-carboxylate
tetracenomycin F1 = 3,8,10,12-tetrahydroxy-1-methyl-11-oxo-6,11-dihydro-2-tetracenecarboxylate = 6,11-dihydro-3,8,10,12-tetrahydroxy-1-methyl-11-oxonaphthacene-2-carboxylate
Other name(s): tcmH (gene name)
Systematic name: tetracenomycin-F1:oxygen C5-monooxygenase
Comments: The enzyme is involved in biosynthesis of the anthracycline antibiotic tetracenomycin C by the bacterium Streptomyces glaucescens.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Shen, B. and Hutchinson, C.R. Tetracenomycin F1 monooxygenase: oxidation of a naphthacenone to a naphthacenequinone in the biosynthesis of tetracenomycin C in Streptomyces glaucescens. Biochemistry 32 (1993) 6656–6663. [PMID: 8329392]
[EC 1.13.12.21 created 2013]
 
 
EC 1.14.11.42
Accepted name: tRNAPhe (7-(3-amino-3-carboxypropyl)wyosine37-C2)-hydroxylase
Reaction: 7-(3-amino-3-carboxypropyl)wyosine37 in tRNAPhe + 2-oxoglutarate + O2 = 7-(2-hydroxy-3-amino-3-carboxypropyl)wyosine37 in tRNAPhe + succinate + CO2
For diagram of wyosine biosynthesis, click here
Glossary: 7-(3-amino-3-carboxypropyl)wyosine = 7-[(3S)-3-amino-3-carboxypropyl]-4,6-dimethyl-3-(-D-ribofuranosyl)-3,4-dihydro-9H-imidazo[1,2-a]purin-9-one
7-(2-hydroxy-3-amino-3-carboxypropyl)wyosine = 4-[4,6-dimethyl-9-oxo-3-(-D-ribofuranosyl)-4,9-dihydro-3H-imidazo[1,2-a]purin-7-yl]-L-threonine
Other name(s): TYW5; tRNA yW-synthesizing enzyme 5
Systematic name: tRNAPhe 7-(3-amino-3-carboxypropyl)wyosine37,2-oxoglutarate:oxygen oxidoreductase (2-hydroxylating)
Comments: Requires Fe2+. The enzyme is not active with wybutosine.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Noma, A., Ishitani, R., Kato, M., Nagao, A., Nureki, O. and Suzuki, T. Expanding role of the jumonji C domain as an RNA hydroxylase. J. Biol. Chem. 285 (2010) 34503–34507. [PMID: 20739293]
2.  Kato, M., Araiso, Y., Noma, A., Nagao, A., Suzuki, T., Ishitani, R. and Nureki, O. Crystal structure of a novel JmjC-domain-containing protein, TYW5, involved in tRNA modification. Nucleic Acids Res. 39 (2011) 1576–1585. [PMID: 20972222]
[EC 1.14.11.42 created 2013]
 
 
EC 1.14.11.43
Accepted name: (S)-dichlorprop dioxygenase (2-oxoglutarate)
Reaction: (1) (S)-2-(4-chloro-2-methylphenoxy)propanoate + 2-oxoglutarate + O2 = 4-chloro-2-methylphenol + pyruvate + succinate + CO2
(2) (S)-(2,4-dichlorophenoxy)propanoate + 2-oxoglutarate + O2 = 2,4-dichlorophenol + pyruvate + succinate + CO2
Glossary: (S)-2-(4-chloro-2-methylphenoxy)propanoate = (S)-mecoprop
(S)-(2,4-dichlorophenoxy)propanoate = (S)-dichlorprop
Other name(s): SdpA; α-ketoglutarate-dependent (S)-dichlorprop dioxygenase; (S)-phenoxypropionate/α-ketoglutarate-dioxygenase; 2-oxoglutarate-dependent (S)-dichlorprop dioxygenase; (S)-mecoprop dioxygenase; 2-oxoglutarate-dependent (S)-mecoprop dioxygenase
Systematic name: (S)-2-(4-chloro-2-methylphenoxy)propanoate,2-oxoglutarate:oxygen oxidoreductase (pyruvate-forming)
Comments: Fe2+-dependent enzyme. The enzymes from the Gram-negative bacteria Delftia acidovorans MC1 and Sphingomonas herbicidovorans MH are involved in the degradation of the (S)-enantiomer of the phenoxyalkanoic acid herbicides mecoprop and dichlorprop [1,2].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Westendorf, A., Benndorf, D., Muller, R.H. and Babel, W. The two enantiospecific dichlorprop/α-ketoglutarate-dioxygenases from Delftia acidovorans MC1 – protein and sequence data of RdpA and SdpA. Microbiol. Res. 157 (2002) 317–322. [PMID: 12501996]
2.  Muller, T.A., Fleischmann, T., van der Meer, J.R. and Kohler, H.P. Purification and characterization of two enantioselective α-ketoglutarate-dependent dioxygenases, RdpA and SdpA, from Sphingomonas herbicidovorans MH. Appl. Environ. Microbiol. 72 (2006) 4853–4861. [PMID: 16820480]
3.  Muller, T.A., Zavodszky, M.I., Feig, M., Kuhn, L.A. and Hausinger, R.P. Structural basis for the enantiospecificities of R- and S-specific phenoxypropionate/α-ketoglutarate dioxygenases. Protein Sci. 15 (2006) 1356–1368. [PMID: 16731970]
[EC 1.14.11.43 created 2013]
 
 
EC 1.14.11.44
Accepted name: (R)-dichlorprop dioxygenase (2-oxoglutarate)
Reaction: (1) (R)-2-(4-chloro-2-methylphenoxy)propanoate + 2-oxoglutarate + O2 = 4-chloro-2-methylphenol + pyruvate + succinate + CO2
(2) (R)-(2,4-dichlorophenoxy)propanoate + 2-oxoglutarate + O2 = 2,4-dichlorophenol + pyruvate + succinate + CO2
Glossary: (R)-2-(4-chloro-2-methylphenoxy)propanoate = (R)-mecoprop
(R)-(2,4-dichlorophenoxy)propanoate = (R)-dichlorprop
Other name(s): RdpA; α-ketoglutarate-dependent (R)-dichlorprop dioxygenase; (R)-phenoxypropionate/α-ketoglutarate-dioxygenase; 2-oxoglutarate-dependent (R)-dichlorprop dioxygenase; (R)-mecoprop dioxygenase; 2-oxoglutarate-dependent (R)-mecoprop dioxygenase
Systematic name: (R)-2-(4-chloro-2-methylphenoxy)propanoate,2-oxoglutarate:oxygen oxidoreductase (pyruvate-forming)
Comments: Fe2+-dependent enzyme. The enzymes from the Gram-negative bacteria Delftia acidovorans MC1 and Sphingomonas herbicidovorans MH are involved in the degradation of the (R)-enantiomer of the phenoxyalkanoic acid herbicides mecoprop and dichlorprop [1,2].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Westendorf, A., Benndorf, D., Muller, R.H. and Babel, W. The two enantiospecific dichlorprop/α-ketoglutarate-dioxygenases from Delftia acidovorans MC1 – protein and sequence data of RdpA and SdpA. Microbiol. Res. 157 (2002) 317–322. [PMID: 12501996]
2.  Muller, T.A., Fleischmann, T., van der Meer, J.R. and Kohler, H.P. Purification and characterization of two enantioselective α-ketoglutarate-dependent dioxygenases, RdpA and SdpA, from Sphingomonas herbicidovorans MH. Appl. Environ. Microbiol. 72 (2006) 4853–4861. [PMID: 16820480]
3.  Muller, T.A., Zavodszky, M.I., Feig, M., Kuhn, L.A. and Hausinger, R.P. Structural basis for the enantiospecificities of R- and S-specific phenoxypropionate/α-ketoglutarate dioxygenases. Protein Sci. 15 (2006) 1356–1368. [PMID: 16731970]
[EC 1.14.11.44 created 2013]
 
 
EC 1.14.13.180
Accepted name: aklavinone 12-hydroxylase
Reaction: aklavinone + NADPH + H+ + O2 = ε-rhodomycinone + NADP+ + H2O
For diagram of aflatoxin biosynthesis, click here
Glossary: aklavinone = methyl (1R,2R,4S)-2-ethyl-2,4,5,7-tetrahydroxy-6,11-dioxo-1,2,3,4,6,11-hexahydrotetracene-1-carboxylate
ε-rhodomycinone = methyl (1R,2R,4S)-2-ethyl-2,4,5,7,12-pentahydroxy-6,11-dioxo-1,2,3,4,6,11-hexahydrotetracene-1-carboxylate
Other name(s): DnrF; RdmE; aklavinone 11-hydroxylase (incorrect)
Systematic name: aklavinone,NADPH:oxygen oxidoreductase (12-hydroxylating)
Comments: The enzymes from the Gram-positive bacteria Streptomyces peucetius and Streptomyces purpurascens participate in the biosynthesis of daunorubicin, doxorubicin and rhodomycins. The enzyme from Streptomyces purpurascens is an FAD monooxygenase.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Filippini, S., Solinas, M.M., Breme, U., Schluter, M.B., Gabellini, D., Biamonti, G., Colombo, A.L. and Garofano, L. Streptomyces peucetius daunorubicin biosynthesis gene, dnrF: sequence and heterologous expression. Microbiology 141 (1995) 1007–1016. [PMID: 7773378]
2.  Niemi, J., Wang, Y., Airas, K., Ylihonko, K., Hakala, J. and Mantsala, P. Characterization of aklavinone-11-hydroxylase from Streptomyces purpurascens. Biochim. Biophys. Acta 1430 (1999) 57–64. [PMID: 10082933]
[EC 1.14.13.180 created 2013]
 
 
EC 1.14.13.181
Accepted name: 13-deoxydaunorubicin hydroxylase
Reaction: (1) 13-deoxydaunorubicin + NADPH + H+ + O2 = 13-dihydrodaunorubicin + NADP+ + H2O
(2) 13-dihydrodaunorubicin + NADPH + H+ + O2 = daunorubicin + NADP+ + 2 H2O
For diagram of daunorubicin biosynthesis, click here
Glossary: 13-dihydrodaunorubicin = daunorubicinol = (1S,3S)-3,5,12-trihydroxy-3-(1-hydroxyethyl)-10-methoxy-6,11-dioxo-1,2,3,4,6,11-hexahydrotetracen-1-yl 3-amino-2,3,6-trideoxy-α-L-lyxo-hexopyranoside
13-deoxydaunorubicin = (1S,3S)-3-ethyl-3,5,12-trihydroxy-10-methoxy-6,11-dioxo-1,2,3,4,6,11-hexahydrotetracen-1-yl 3-amino-2,3,6-trideoxy-α-L-lyxo-hexopyranoside
daunorubicin = (1S,3S)-3-acetyl-3,5,12-trihydroxy-10-methoxy-6,11-dioxo-1,2,3,4,6,11-hexahydrotetracen-1-yl 3-amino-2,3,6-trideoxy-α-L-lyxo-hexopyranoside
Other name(s): DoxA
Systematic name: 13-deoxydaunorubicin,NADPH:oxygen oxidoreductase (13-hydroxylating)
Comments: The enzymes from the Gram-positive bacteria Streptomyces sp. C5 and Streptomyces peucetius show broad substrate specificity for structures based on an anthracycline aglycone, but have a strong preference for 4-methoxy anthracycline intermediates (13-deoxydaunorubicin and 13-dihydrodaunorubicin) over their 4-hydroxy analogues (13-deoxycarminomycin and 13-dihydrocarminomycin), as well as a preference for substrates hydroxylated at the C-13 rather than the C-14 position.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Walczak, R.J., Dickens, M.L., Priestley, N.D. and Strohl, W.R. Purification, properties, and characterization of recombinant Streptomyces sp. strain C5 DoxA, a cytochrome P-450 catalyzing multiple steps in doxorubicin biosynthesis. J. Bacteriol. 181 (1999) 298–304. [PMID: 9864343]
2.  Dickens, M.L., Priestley, N.D. and Strohl, W.R. In vivo and in vitro bioconversion of ε-rhodomycinone glycoside to doxorubicin: functions of DauP, DauK, and DoxA. J. Bacteriol. 179 (1997) 2641–2650. [PMID: 9098063]
[EC 1.14.13.181 created 2013]
 
 
EC 1.14.13.182
Accepted name: 2-heptyl-3-hydroxy-4(1H)-quinolone synthase
Reaction: 2-heptyl-4(1H)-quinolone + NADH + H+ + O2 = 2-heptyl-3-hydroxy-4(1H)-quinolone + NAD+ + H2O
Glossary: 2-heptyl-4(1H)-quinolone = 2-heptyl-4-hydroxyquinoline
2-heptyl-3-hydroxy-4(1H)-quinolone = 2-heptyl-3,4-dihydroxyquinoline
Other name(s): PqsH; 2-heptyl-3,4-dihydroxyquinoline synthase
Systematic name: 2-heptyl-4(1H)-quinolone,NADH:oxygen oxidoreductase (3-hydroxylating)
Comments: The enzyme from the bacterium Pseudomonas aeruginosa catalyses the terminal step in biosynthesis of the signal molecule 2-heptyl-3,4-dihydroxyquinoline that plays a role in regulation of virulence genes.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Schertzer, J.W., Brown, S.A. and Whiteley, M. Oxygen levels rapidly modulate Pseudomonas aeruginosa social behaviours via substrate limitation of PqsH. Mol. Microbiol. 77 (2010) 1527–1538. [PMID: 20662781]
[EC 1.14.13.182 created 2013]
 
 
EC 1.14.14.14
Accepted name: aromatase
Reaction: (1) testosterone + 3 O2 + 3 [reduced NADPH—hemoprotein reductase] = 17β-estradiol + formate + 4 H2O + 3 [oxidized NADPH—hemoprotein reductase] (overall reaction)
(1a) testosterone + O2 + [reduced NADPH—hemoprotein reductase] = 19-hydroxytestosterone + H2O + [oxidized NADPH—hemoprotein reductase]
(1b) 19-hydroxytestosterone + O2 + [reduced NADPH—hemoprotein reductase] = 19-oxotestosterone + 2 H2O + [oxidized NADPH—hemoprotein reductase]
(1c) 19-oxotestosterone + O2 + [reduced NADPH—hemoprotein reductase] = 17β-estradiol + formate + H2O + [oxidized NADPH—hemoprotein reductase]
(2) androst-4-ene-3,17-dione + 3 O2 + 3 [reduced NADPH—hemoprotein reductase] = estrone + formate + 4 H2O + 3 [oxidized NADPH—hemoprotein reductase] (overall reaction)
(2a) androst-4-ene-3,17-dione + O2 + [reduced NADPH—hemoprotein reductase] = 19-hydroxyandrost-4-ene-3,17-dione + H2O + [oxidized NADPH—hemoprotein reductase]
(2b) 19-hydroxyandrost-4-ene-3,17-dione + O2 + [reduced NADPH—hemoprotein reductase] = 19-oxo-androst-4-ene-3,17-dione + 2 H2O + [oxidized NADPH—hemoprotein reductase]
(2c) 19-oxoandrost-4-ene-3,17-dione + O2 + [reduced NADPH—hemoprotein reductase] = estrone + formate + H2O + [oxidized NADPH—hemoprotein reductase]
Other name(s): CYP19A1 (gene name); estrogen synthetase (incorrect)
Systematic name: testosteronel,NADPH—hemoprotein reductase:oxygen oxidoreductase (17β-estradiol-forming)
Comments: A cytochrome P-450. The enzyme catalyses three sequential hydroxylations of the androgens androst-4-ene-3,17-dione and testosterone, resulting in their aromatization and forming the estrogens estrone and 17β-estradiol, respectively. The direct electron donor to the enzyme is EC 1.6.2.4, NADPH—hemoprotein reductase.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Thompson, E.A., Jr. and Siiteri, P.K. The involvement of human placental microsomal cytochrome P-450 in aromatization. J. Biol. Chem. 249 (1974) 5373–5378. [PMID: 4370479]
2.  Fishman, J. and Goto, J. Mechanism of estrogen biosynthesis. Participation of multiple enzyme sites in placental aromatase hydroxylations. J. Biol. Chem. 256 (1981) 4466–4471. [PMID: 7217091]
3.  Kellis, J.T., Jr. and Vickery, L.E. Purification and characterization of human placental aromatase cytochrome P-450. J. Biol. Chem. 262 (1987) 4413–4420. [PMID: 3104339]
4.  Ghosh, D., Griswold, J., Erman, M. and Pangborn, W. Structural basis for androgen specificity and oestrogen synthesis in human aromatase. Nature 457 (2009) 219–223. [PMID: 19129847]
[EC 1.14.14.14 created 2013]
 
 
*EC 1.14.99.48 – private review until 29 June 2017 [Last modified: 2013-11-22 15:58:58]
Accepted name: heme oxygenase (staphylobilin-producing)
Reaction: (1) protoheme + 5 reduced acceptor + 4 O2 = β-staphylobilin + Fe2+ + formaldehyde + 5 acceptor + 4 H2O
(2) protoheme + 5 reduced acceptor + 4 O2 = δ-staphylobilin + Fe2+ + formaldehyde + 5 acceptor + 4 H2O
Glossary: β-staphylobilin = 10-oxo-β-bilirubin = 3,7-bis(2-carboxyethyl)-2,8,13,18-tetramethyl-12,17-divinylbiladiene-ac-1,10,19(21H,24H)-trione
δ-staphylobilin = 10-oxo-δ-bilirubin = 3,7-bis(2-carboxyethyl)-2,8,12,17-tetramethyl-13,18-divinylbiladiene-ac-1,10,19(21H,24H)-trione
Other name(s): haem oxygenase (ambiguous); heme oxygenase (decyclizing) (ambiguous); heme oxidase (ambiguous); haem oxidase (ambiguous); heme oxygenase (ambiguous); isdG (gene name); isdI (gene name)
Systematic name: protoheme,hydrogen-donor:oxygen oxidoreductase (δ/β-methene-oxidizing, hydroxylating)
Comments: This enzyme, which is found in some pathogenic bacteria, is involved in an iron acquisition system that catabolizes the host’s hemoglobin. The two enzymes from the bacterium Staphylococcus aureus, encoded by the isdG and isdI genes, produce 67.5 % and 56.2 % δ-staphylobilin, respectively.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, MetaCyc
References:
1.  Reniere, M.L., Ukpabi, G.N., Harry, S.R., Stec, D.F., Krull, R., Wright, D.W., Bachmann, B.O., Murphy, M.E. and Skaar, E.P. The IsdG-family of haem oxygenases degrades haem to a novel chromophore. Mol. Microbiol. 75 (2010) 1529–1538. [PMID: 20180905]
2.  Matsui, T., Nambu, S., Ono, Y., Goulding, C.W., Tsumoto, K. and Ikeda-Saito, M. Heme degradation by Staphylococcus aureus IsdG and IsdI liberates formaldehyde rather than carbon monoxide. Biochemistry 52 (2013) 3025–3027. [PMID: 23600533]
3.  Streit, B.R., Kant, R., Tokmina-Lukaszewska, M., Celis, A.I., Machovina, M.M., Skaar, E.P., Bothner, B. and DuBois, J.L. Time-resolved studies of IsdG protein identify molecular signposts along the non-canonical heme oxygenase pathway. J. Biol. Chem. 291 (2016) 862–871. [PMID: 26534961]
[EC 1.14.99.48 created 2013]
 
 
*EC 2.1.1.44
Accepted name: L-histidine Nα-methyltransferase
Reaction: 3 S-adenosyl-L-methionine + L-histidine = 3 S-adenosyl-L-homocysteine + hercynine (overall reaction)
(1a) S-adenosyl-L-methionine + L-histidine = S-adenosyl-L-homocysteine + Nα-methyl-L-histidine
(1b) S-adenosyl-L-methionine + Nα-methyl-L-histidine = S-adenosyl-L-homocysteine + Nα,Nα-dimethyl-L-histidine
(1c) S-adenosyl-L-methionine + Nα,Nα-dimethyl-L-histidine = S-adenosyl-L-homocysteine + hercynine
For diagram of ergothioneine and ovothiol biosynthesis, click here
Glossary: hercynine = Nα,Nα,Nα-trimethyl-L-histidine
Other name(s): dimethylhistidine N-methyltransferase; dimethylhistidine methyltransferase; histidine-α-N-methyltransferase; S-adenosyl-L-methionine:α-N,α-N-dimethyl-L-histidine α-N-methyltransferase; S-adenosyl-L-methionine:Nα,Nα-dimethyl-L-histidine Nα-methyltransferase
Systematic name: S-adenosyl-L-methionine:L-histidine Nα-methyltransferase (hercynine-forming)
Comments: Part of the biosynthetic pathway of ergothioneine.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 62213-53-0
References:
1.  Ishikawa, Y. and Melville, D.B. The enzymatic α-N-methylation of histidine. J. Biol. Chem. 245 (1970) 5967–5973. [PMID: 5484456]
2.  Seebeck, F.P. In vitro reconstitution of Mycobacterial ergothioneine biosynthesis. J. Am. Chem. Soc. 132 (2010) 6632–6633. [PMID: 20420449]
[EC 2.1.1.44 created 1976, modified 2013]
 
 
EC 2.1.1.66
Deleted entry: rRNA (adenosine-2′-O-)-methyltransferase. Now covered by EC 2.1.1.230, 23S rRNA (adenosine1067-2-O)-methyltransferase.
[EC 2.1.1.66 created 1984, deleted 2013]
 
 
EC 2.1.1.288
Accepted name: aklanonic acid methyltransferase
Reaction: S-adenosyl-L-methionine + aklanonate = S-adenosyl-L-homocysteine + methyl aklanonate
For diagram of aflatoxin biosynthesis, click here
Glossary: methyl aklanonate = methyl [1,4,5-trihydroxy-9,10-dioxo-3-(3-oxopentanoyl)-9,10-dihydroanthracen-2-yl]acetate
aklanonate = [4,5-dihydroxy-9,10-dioxo-3-(3-oxopentanoyl)-9,10-dihydroanthracen-2-yl]acetic acid
Other name(s): DauC; AAMT
Systematic name: S-adenosyl-L-methionine:aklanonate O-methyltransferase
Comments: The enzyme from the Gram-positive bacterium Streptomyces sp. C5 is involved in the biosynthesis of the anthracycline daunorubicin.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Dickens, M.L., Ye, J. and Strohl, W.R. Analysis of clustered genes encoding both early and late steps in daunomycin biosynthesis by Streptomyces sp. strain C5. J. Bacteriol. 177 (1995) 536–543. [PMID: 7836284]
[EC 2.1.1.288 created 2013]
 
 
EC 2.1.3.13
Deleted entry: ATP carbamoyltransferase. The enzyme has been replaced by EC 6.1.2.2, nebramycin 5′ synthase.
[EC 2.1.3.13 created 2013, deleted 2014]
 
 
EC 2.1.3.14
Deleted entry: tobramycin carbamoyltransferase. The enzyme has been replaced by EC 6.1.2.2, nebramycin 5′ synthase
[EC 2.1.3.14 created 2013, deleted 2014]
 
 
EC 2.3.1.227
Accepted name: GDP-perosamine N-acetyltransferase
Reaction: acetyl-CoA + GDP-4-amino-4,6-dideoxy-α-D-mannose = CoA + GDP-4-acetamido-4,6-dideoxy-α-D-mannose
Glossary: GDP-4-amino-4,6-dideoxy-α-D-mannose = GDP-α-D-perosamine
GDP-4-acetamido-4,6-dideoxy-α-D-mannose = GDP-N-acetyl-α-D-perosamine
Other name(s): perB (gene name); GDP-α-D-perosamine N-acetyltransferase
Systematic name: acetyl-CoA:GDP-4-amino-4,6-dideoxy-α-D-mannose N-acetyltransferase
Comments: D-Perosamine is one of several dideoxy sugars found in the O-antigen component of the outer membrane lipopolysaccharides of Gram-negative bacteria.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Albermann, C. and Beuttler, H. Identification of the GDP-N-acetyl-d-perosamine producing enzymes from Escherichia coli O157:H7. FEBS Lett. 582 (2008) 479–484. [PMID: 18201574]
[EC 2.3.1.227 created 2013]
 
 
EC 2.3.1.228
Accepted name: isovaleryl-homoserine lactone synthase
Reaction: isovaleryl-CoA + S-adenosyl-L-methionine = CoA + S-methyl-5′-thioadenosine + N-isovaleryl-L-homoserine lactone
Other name(s): IV-HSL synthase; BjaI
Systematic name: isovaleryl-CoA:S-adenosyl-L-methionine isovaleryltranserase (lactone-forming, methylthioadenosine-releasing)
Comments: The enzyme, found in the bacterium Bradyrhizobium japonicum, does not accept isovaleryl-[acyl-carrier protein] as acyl donor (cf. EC 2.3.1.184, acyl-homoserine-lactone synthase).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Lindemann, A., Pessi, G., Schaefer, A.L., Mattmann, M.E., Christensen, Q.H., Kessler, A., Hennecke, H., Blackwell, H.E., Greenberg, E.P. and Harwood, C.S. Isovaleryl-homoserine lactone, an unusual branched-chain quorum-sensing signal from the soybean symbiont Bradyrhizobium japonicum. Proc. Natl. Acad. Sci. USA 108 (2011) 16765–16770. [PMID: 21949379]
[EC 2.3.1.228 created 2013]
 
 
EC 2.3.1.229
Accepted name: 4-coumaroyl-homoserine lactone synthase
Reaction: 4-coumaroyl-CoA + S-adenosyl-L-methionine = CoA + S-methyl-5′-thioadenosine + N-(4-coumaroyl)-L-homoserine lactone
Other name(s): p-coumaryl-homoserine lactone synthase; RpaI
Systematic name: 4-coumaroyl-CoA:S-adenosyl-L-methionine trans-4-coumaroyltranserase (lactone-forming, methylthioadenosine-releasing)
Comments: The enzyme is found in the bacterium Rhodopseudomonas palustris, which produces N-(4-coumaroyl)-L-homoserine lactone as a quorum-sensing signal.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Schaefer, A.L., Greenberg, E.P., Oliver, C.M., Oda, Y., Huang, J.J., Bittan-Banin, G., Peres, C.M., Schmidt, S., Juhaszova, K., Sufrin, J.R. and Harwood, C.S. A new class of homoserine lactone quorum-sensing signals. Nature 454 (2008) 595–599. [PMID: 18563084]
[EC 2.3.1.229 created 2013]
 
 
*EC 2.3.2.3
Accepted name: lysyltransferase
Reaction: L-lysyl-tRNALys + phosphatidylglycerol = tRNALys + 3-O-L-lysyl-1-O-phosphatidylglycerol
Other name(s): L-lysyl-tRNA:phosphatidylglycerol 3-O-lysyltransferase
Systematic name: L-lysyl-tRNALys:phosphatidylglycerol 3-O-lysyltransferase
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 37257-20-8
References:
1.  Lennarz, W.J., Bonsen, P.P.M. and van Deenan, L.L.M. Substrate specificity of O-L-lysylphosphatidylglycerol synthetase. Enzymatic studies on the structure of O-L-lysylphosphatidylglycerol. Biochemistry 6 (1967) 2307–2312. [PMID: 6049461]
[EC 2.3.2.3 created 1972, modified 2013]
 
 
*EC 2.3.2.6
Accepted name: lysine/arginine leucyltransferase
Reaction: (1) L-leucyl-tRNALeu + N-terminal L-lysyl-[protein] = tRNALeu + N-terminal L-leucyl-L-lysyl-[protein]
(2) L-leucyl-tRNALeu + N-terminal L-arginyl-[protein] = tRNALeu + N-terminal L-leucyl-L-arginyl-[protein]
Other name(s): leucyl, phenylalanine-tRNA-protein transferase; leucyl-phenylalanine-transfer ribonucleate-protein aminoacyltransferase; leucyl-phenylalanine-transfer ribonucleate-protein transferase; L-leucyl-tRNA:protein leucyltransferase; leucyltransferase (misleading); L/FK,R-transferase; aat (gene name); L-leucyl-tRNALeu:protein leucyltransferase
Systematic name: L-leucyl-tRNALeu:[protein] N-terminal L-lysine/L-arginine leucyltransferase
Comments: Requires a univalent cation. The enzyme participates in the N-end rule protein degradation pathway in certain bacteria, by attaching the primary destabilizing residue L-leucine to the N-termini of proteins that have an N-terminal L-arginine or L-lysine residue. Once modified, the proteins are recognized by EC 3.4.21.92, the ClpAP/ClpS endopeptidase system. The enzyme also transfers L-phenylalanine in vitro, but this has not been observed in vivo [5]. cf. EC 2.3.2.29, aspartate/glutamate leucyltransferase, and EC 2.3.2.8, arginyltransferase.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, PDB, CAS registry number: 37257-22-0
References:
1.  Leibowitz, M.J. and Soffer, R.L. A soluble enzyme from Escherichia coli which catalyzes the transfer of leucine and phenylalanine from tRNA to acceptor proteins. Biochem. Biophys. Res. Commun. 36 (1969) 47–53. [PMID: 4894363]
2.  Leibowitz, M.J. and Soffer, R.L. Enzymatic modification of proteins. 3. Purification and properties of a leucyl, phenylalanyl transfer ribonucleic acid protein transferase from Escherichia coli. J. Biol. Chem. 245 (1970) 2066–2073. [PMID: 4909560]
3.  Soffer, R.L. Peptide acceptors in the leucine, phenylalanine transfer reaction. J. Biol. Chem. 248 (1973) 8424–8428. [PMID: 4587124]
4.  Tobias, J.W., Shrader, T.E., Rocap, G. and Varshavsky, A. The N-end rule in bacteria. Science 254 (1991) 1374–1377. [PMID: 1962196]
5.  Shrader, T.E., Tobias, J.W. and Varshavsky, A. The N-end rule in Escherichia coli: cloning and analysis of the leucyl, phenylalanyl-tRNA-protein transferase gene aat. J. Bacteriol. 175 (1993) 4364–4374. [PMID: 8331068]
6.  Abramochkin, G. and Shrader, T.E. The leucyl/phenylalanyl-tRNA-protein transferase. Overexpression and characterization of substrate recognition, domain structure, and secondary structure. J. Biol. Chem. 270 (1995) 20621–20628. [PMID: 7657641]
[EC 2.3.2.6 created 1972, modified 1976, modified 2013, modified 2016]
 
 
*EC 2.3.2.8
Accepted name: arginyltransferase
Reaction: L-arginyl-tRNAArg + protein = tRNAArg + L-arginyl-[protein]
Other name(s): arginine transferase; arginyl-transfer ribonucleate-protein aminoacyltransferase; arginyl-transfer ribonucleate-protein transferase; arginyl-tRNA protein transferase; L-arginyl-tRNA:protein arginyltransferase
Systematic name: L-arginyl-tRNAArg:protein arginyltransferase
Comments: Requires mercaptoethanol and a univalent cation. Peptides and proteins containing an N-terminal glutamate, aspartate or cystine residue can act as acceptors.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 37257-24-2
References:
1.  Soffer, R.L. Enzymatic modification of proteins. II. Purification and properties of the arginyl transfer ribonucleic acid-protein transferase from rabbit liver cytoplasm. J. Biol. Chem. 245 (1970) 731–737. [PMID: 5416661]
2.  Soffer, R.L. Peptide acceptors in the arginine transfer reaction. J. Biol. Chem. 248 (1973) 2918–2921. [PMID: 4572514]
3.  Soffer, R.L. and Horinishi, H. Enzymic modification of proteins. I. General characteristics of the arginine-transfer reaction in rabbit liver cytoplasm. J. Mol. Biol. 43 (1969) 163–175. [PMID: 5811819]
[EC 2.3.2.8 created 1972, modified 1976, modified 2013]
 
 
*EC 2.3.2.10
Accepted name: UDP-N-acetylmuramoylpentapeptide-lysine N6-alanyltransferase
Reaction: L-alanyl-tRNAAla + UDP-N-acetyl-α-D-muramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine = tRNAAla + UDP-N-acetyl-α-D-muramoyl-L-alanyl-D-glutamyl-N6-(L-alanyl)-L-lysyl-D-alanyl-D-alanine
Other name(s): alanyl-transfer ribonucleate-uridine diphosphoacetylmuramoylpentapeptide transferase; UDP-N-acetylmuramoylpentapeptide lysine N6-alanyltransferase; uridine diphosphoacetylmuramoylpentapeptide lysine N6-alanyltransferase; L-alanyl-tRNA:UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine 6-N-alanyltransferase; L-alanyl-tRNA:UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine N6-alanyltransferase
Systematic name: L-alanyl-tRNAAla:UDP-N-acetyl-α-D-muramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine N6-alanyltransferase
Comments: Also acts on L-seryl-tRNASer.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 37257-26-4
References:
1.  Plapp, R. and Strominger, J.L. Biosynthesis of the peptidoglycan of bacterial cell walls. 18. Purification and properties of L-alanyl transfer ribonucleic acid-uridine diphosphate-N-acetylmuramyl-pentapeptide transferase from Lactobacillus viridescens. J. Biol. Chem. 245 (1970) 3675–3682. [PMID: 4248527]
[EC 2.3.2.10 created 1972, modified 2013]
 
 
*EC 2.3.2.11
Accepted name: alanylphosphatidylglycerol synthase
Reaction: L-alanyl-tRNAAla + phosphatidylglycerol = tRNAAla + 3-O-L-alanyl-1-O-phosphatidylglycerol
Other name(s): O-alanylphosphatidylglycerol synthase; alanyl phosphatidylglycerol synthetase
Systematic name: L-alanyl-tRNAAla:phosphatidylglycerol alanyltransferase
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 37257-27-5
References:
1.  Gould, R.M., Thornton, M.P., Liepkalns, V. and Lennarz, W.J. Participation of aminoacyl transfer ribonucleic acid in aminoacyl phosphatidylglycerol synthesis. II. Specificity of alanyl phosphatidylglycerol synthetase. J. Biol. Chem. 243 (1968) 3096–3104. [PMID: 4297471]
[EC 2.3.2.11 created 1972, modified 2013]
 
 
*EC 2.4.1.229
Accepted name: [Skp1-protein]-hydroxyproline N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + [Skp1-protein]-trans-4-hydroxy-L-proline = UDP + [Skp1-protein]-O-(N-acetyl-α-D-glucosaminyl)-trans-4-hydroxy-L-proline
Other name(s): Skp1-HyPro GlcNAc-transferase; UDP-N-acetylglucosamine (GlcNAc):hydroxyproline polypeptide GlcNAc-transferase; UDP-GlcNAc:Skp1-hydroxyproline GlcNAc-transferase; UDP-GlcNAc:hydroxyproline polypeptide GlcNAc-transferase; UDP-N-acetyl-D-glucosamine:[Skp1-protein]-hydroxyproline N-acetyl-D-glucosaminyl-transferase
Systematic name: UDP-N-acetyl-α-D-glucosamine:[Skp1-protein]-trans-4-hydroxy-L-proline N-acetyl-α-D-glucosaminyl-transferase
Comments: Skp1 is a cytoplasmic and nuclear protein required for the ubiquitination of cell cycle regulatory proteins and transcriptional factors. In Dictyostelium Skp1 is modified by the linear pentasaccharide Galα1-6Galα1-L-Fucα1-2Galβ1-3GlcNAc, which is attached to a hydroxyproline residue at position 143. This enzyme catalyses the first step in the building up of the pentasaccharide by attaching an N-acetylglucosaminyl group to the hydroxyproline residue. It requires dithiothreitol and a divalent cation for activity.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 256531-81-4
References:
1.  van der Wel, H., Morris, H.R., Panico, M., Paxton, T., Dell, A., Kaplan, L. and West, C.M. Molecular cloning and expression of a UDP-N-acetylglucosamine (GlcNAc):hydroxyproline polypeptide GlcNAc-transferase that modifies Skp1 in the cytoplasm of Dictyostelium. J. Biol. Chem. 277 (2002) 46328–46337. [PMID: 12244115]
2.  Teng-umnuay, P., van der Wel, H. and West, C.M. Identification of a UDP-GlcNAc:Skp1-hydroxyproline GlcNAc-transferase in the cytoplasm of Dictyostelium. J. Biol. Chem. 274 (1999) 36392–36402. [PMID: 10593934]
3.  West, C.M., van der Wel, H. and Gaucher, E.A. Complex glycosylation of Skp1 in Dictyostelium: implications for the modification of other eukaryotic cytoplasmic and nuclear proteins. Glycobiology 12 (2002) 17. [PMID: 11886837]
[EC 2.4.1.229 created 2003, modified 2013]
 
 
*EC 2.4.1.245
Accepted name: α,α-trehalose synthase
Reaction: NDP-α-D-glucose + D-glucose = α,α-trehalose + NDP
Glossary: NDP = a nucleoside diphosphate
Other name(s): trehalose synthase; trehalose synthetase; UDP-glucose:glucose 1-glucosyltransferase; TreT; PhGT; ADP-glucose:D-glucose 1-α-D-glucosyltransferase
Systematic name: NDP-α-D-glucose:D-glucose 1-α-D-glucosyltransferase
Comments: Requires Mg2+ for maximal activity [1]. The enzyme-catalysed reaction is reversible [1]. In the reverse direction to that shown above, the enzyme is specific for α,α-trehalose as substrate, as it cannot use α- or β-paranitrophenyl glucosides, maltose, sucrose, lactose or cellobiose [1]. While the enzymes from the thermophilic bacterium Rubrobacter xylanophilus and the hyperthermophilic archaeon Pyrococcus horikoshii can use ADP-, UDP- and GDP-α-D-glucose to the same extent [2,3], that from the hyperthermophilic archaeon Thermococcus litoralis has a marked preference for ADP-α-D-glucose [1] and that from the hyperthermophilic archaeon Thermoproteus tenax has a marked preference for UDP-α-D-glucose [4].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Qu, Q., Lee, S.J. and Boos, W. TreT, a novel trehalose glycosyltransferring synthase of the hyperthermophilic archaeon Thermococcus litoralis. J. Biol. Chem. 279 (2004) 47890–47897. [PMID: 15364950]
2.  Ryu, S.I., Park, C.S., Cha, J., Woo, E.J. and Lee, S.B. A novel trehalose-synthesizing glycosyltransferase from Pyrococcus horikoshii: molecular cloning and characterization. Biochem. Biophys. Res. Commun. 329 (2005) 429–436. [PMID: 15737605]
3.  Nobre, A., Alarico, S., Fernandes, C., Empadinhas, N. and da Costa, M.S. A unique combination of genetic systems for the synthesis of trehalose in Rubrobacter xylanophilus: properties of a rare actinobacterial TreT. J. Bacteriol. 190 (2008) 7939–7946. [PMID: 18835983]
4.  Kouril, T., Zaparty, M., Marrero, J., Brinkmann, H. and Siebers, B. A novel trehalose synthesizing pathway in the hyperthermophilic Crenarchaeon Thermoproteus tenax: the unidirectional TreT pathway. Arch. Microbiol. 190 (2008) 355–369. [PMID: 18483808]
[EC 2.4.1.245 created 2008, modified 2013]
 
 
*EC 2.5.1.16
Accepted name: spermidine synthase
Reaction: S-adenosyl 3-(methylthio)propylamine + putrescine = S-methyl-5′-thioadenosine + spermidine
For diagram of spermine biosynthesis, click here
Glossary: spermidine = N-(3-aminopropyl)butane-1,4-diamine
spermine = N,N′-bis(3-aminopropyl)butane-1,4-diamine
putrescine = butane-1,4-diamine
S-adenosyl 3-(methylthio)propylamine = (3-aminopropyl){[(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl}methylsulfonium
Other name(s): aminopropyltransferase; putrescine aminopropyltransferase; spermidine synthetase; SpeE; S-adenosylmethioninamine:putrescine 3-aminopropyltransferase
Systematic name: S-adenosyl 3-(methylthio)propylamine:putrescine 3-aminopropyltransferase
Comments: The enzymes from the plant Glycine max and from mammalia are highly specific for putrescine as the amine acceptor [2,7]. The enzymes from the bacteria Escherichia coli and Thermotoga maritima prefer putrescine but are more tolerant towards other amine acceptors, such as spermidine and cadaverine [5,6]. cf. EC 2.5.1.22 (spermine synthase) and EC 2.5.1.23 (sym-norspermidine synthase).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, PDB, CAS registry number: 37277-82-0
References:
1.  Hannonen, P., Janne, J. and Raina, A. Partial purification and characterization of spermine synthase from rat brain. Biochim. Biophys. Acta 289 (1972) 225–231. [PMID: 4564056]
2.  Pegg, A.E., Shuttleworth, K. and Hibasami, H. Specificity of mammalian spermidine synthase and spermine synthase. Biochem. J. 197 (1981) 315–320. [PMID: 6798961]
3.  Tabor, C.W. Propylamine transferase (spermidine synthesis). Methods Enzymol. 5 (1962) 761–765.
4.  Tabor, H. and Tabor, C.W. Biosynthesis and metabolism of 1,4-diaminobutane, spermidine, spermine, and related amines. Adv. Enzymol. Relat. Areas Mol. Biol. 36 (1972) 203–268. [PMID: 4628436]
5.  Bowman, W.H., Tabor, C.W. and Tabor, H. Spermidine biosynthesis. Purification and properties of propylamine transferase from Escherichia coli. J. Biol. Chem. 248 (1973) 2480–2486. [PMID: 4572733]
6.  Korolev, S., Ikeguchi, Y., Skarina, T., Beasley, S., Arrowsmith, C., Edwards, A., Joachimiak, A., Pegg, A.E. and Savchenko, A. The crystal structure of spermidine synthase with a multisubstrate adduct inhibitor. Nat. Struct. Biol. 9 (2002) 27–31. [PMID: 11731804]
7.  Yoon, S.O., Lee, Y.S., Lee, S.H. and Cho, Y.D. Polyamine synthesis in plants: isolation and characterization of spermidine synthase from soybean (Glycine max) axes. Biochim. Biophys. Acta 1475 (2000) 17–26. [PMID: 10806333]
[EC 2.5.1.16 created 1972, modified 1982, modified 2013]
 
 
*EC 2.5.1.22
Accepted name: spermine synthase
Reaction: S-adenosyl 3-(methylthio)propylamine + spermidine = S-methyl-5′-thioadenosine + spermine
For diagram of spermine biosynthesis, click here
Glossary: spermidine = N-(3-aminopropyl)butane-1,4-diamine
spermine = N,N′-bis(3-aminopropyl)butane-1,4-diamine
S-adenosyl 3-(methylthio)propylamine = (3-aminopropyl){[(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl}methylsulfonium
Other name(s): spermidine aminopropyltransferase; spermine synthetase; S-adenosylmethioninamine:spermidine 3-aminopropyltransferase
Systematic name: S-adenosyl 3-(methylthio)propylamine:spermidine 3-aminopropyltransferase
Comments: The enzyme from mammalia is highly specific for spermidine [2,3]. cf. EC 2.5.1.16 (spermidine synthase) and EC 2.5.1.23 (sym-norspermidine synthase).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, PDB, CAS registry number: 74812-43-4
References:
1.  Hibasami, H., Borchardt, R.T., Chen, S.-Y., Coward, J.K. and Pegg, A.E. Studies of inhibition of rat spermidine synthase and spermine synthase. Biochem. J. 187 (1980) 419–428. [PMID: 7396856]
2.  Pajula, R.-L., Raina, A. and Eloranta, T. Polyamine synthesis in mammalian tissues. Isolation and characterization of spermine synthase from bovine brain. Eur. J. Biochem. 101 (1979) 619–626. [PMID: 520313]
3.  Pegg, A.E., Shuttleworth, K. and Hibasami, H. Specificity of mammalian spermidine synthase and spermine synthase. Biochem. J. 197 (1981) 315–320. [PMID: 6798961]
[EC 2.5.1.22 created 1982, modified 2013]
 
 
*EC 2.5.1.23
Accepted name: sym-norspermidine synthase
Reaction: S-adenosyl 3-(methylthio)propylamine + propane-1,3-diamine = S-methyl-thioadenosine + bis(3-aminopropyl)amine
Glossary: S-adenosyl 3-(methylthio)propylamine = (3-aminopropyl){[(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl}methylsulfonium
Other name(s): S-adenosylmethioninamine:propane-1,3-diamine 3-aminopropyltransferase
Systematic name: S-adenosyl 3-(methylthio)propylamine:propane-1,3-diamine 3-aminopropyltransferase
Comments: The enzyme has been originally characterized from the protist Euglena gracilis [1,2]. The enzyme from the archaeon Sulfolobus solfataricus can transfer the propylamine moiety from S-adenosyl 3-(methylthio)propylamine to putrescine, sym-norspermidine and spermidine with lower efficiency [3]. cf. EC 2.5.1.16 (spermidine synthase) and EC 2.5.1.22 (spermine synthase).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Aleksijevic, A., Grove, J. and Schuber, F. Studies on polyamine biosynthesis in Euglena gracilis. Biochim. Biophys. Acta 565 (1979) 199–207. [PMID: 116684]
2.  Villanueva, V.R., Adlakha, R.C. and Calbayrac, R. Biosynthesis of polyamines in Euglena gracilis. Phytochemistry 19 (1980) 787–790.
3.  Cacciapuoti, G., Porcelli, M., Carteni-Farina, M., Gambacorta, A. and Zappia, V. Purification and characterization of propylamine transferase from Sulfolobus solfataricus, an extreme thermophilic archaebacterium. Eur. J. Biochem. 161 (1986) 263–271. [PMID: 3096734]
[EC 2.5.1.23 created 1983, modified 2013]
 
 
EC 2.5.1.111
Accepted name: 4-hydroxyphenylpyruvate 3-dimethylallyltransferase
Reaction: dimethylallyl diphosphate + 4-hydroxyphenylpyruvate = diphosphate + 3-dimethylallyl-4-hydroxyphenylpyruvate
For diagram of 4-hydroxyphenylpyruvate metabolites, click here
Glossary: 3-dimethylallyl-4-hydroxyphenylpyruvate = 3-[4-hydroxy-3-(3-methylbut-2-en-1-yl)phenyl]-2-oxopropanoate
Other name(s): CloQ; 4HPP dimethylallyltransferase; NovQ
Systematic name: dimethylallyl diphosphate:4-hydroxyphenylpyruvate 3-dimethylallyltransferase
Comments: The enzyme is involved in the biosynthesis of the 3-dimethylallyl-4-hydroxyphenylpyruvate moiety of the aminocoumarin antibiotics clorobiocin and novobiocin [1].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Pojer, F., Wemakor, E., Kammerer, B., Chen, H., Walsh, C.T., Li, S.M. and Heide, L. CloQ, a prenyltransferase involved in clorobiocin biosynthesis. Proc. Natl. Acad. Sci. USA 100 (2003) 2316–2321. [PMID: 12618544]
2.  Keller, S., Pojer, F., Heide, L. and Lawson, D.M. Crystallization and preliminary X-ray analysis of the aromatic prenyltransferase CloQ from the clorobiocin biosynthetic cluster of Streptomyces roseochromogenes. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 62 (2006) 1153–1155. [PMID: 17077503]
3.  Metzger, U., Keller, S., Stevenson, C.E., Heide, L. and Lawson, D.M. Structure and mechanism of the magnesium-independent aromatic prenyltransferase CloQ from the clorobiocin biosynthetic pathway. J. Mol. Biol. 404 (2010) 611–626. [PMID: 20946900]
4.  Ozaki, T., Mishima, S., Nishiyama, M. and Kuzuyama, T. NovQ is a prenyltransferase capable of catalyzing the addition of a dimethylallyl group to both phenylpropanoids and flavonoids. J. Antibiot. (Tokyo) 62 (2009) 385–392. [PMID: 19557032]
[EC 2.5.1.111 created 2013]
 
 
EC 3.1.1.95
Accepted name: aclacinomycin methylesterase
Reaction: aclacinomycin T + H2O = 15-demethylaclacinomycin T + methanol
For diagram of aflatoxin biosynthesis, click here
Glossary: aclacinomycin T = 2-ethyl-1,2,3,4,6,11-hexahydro-2,5,7-trihydroxy-6,11-dioxo-4-{[2,3,6-trideoxy-3-(dimethylamino)-α-L-lyxo-hexopyranosyl]oxy}-1-naphthacenecarboxylic acid methyl ester = methyl (1R,2R,4S)-2-ethyl-2,5,7-trihydroxy-6,11-dioxo-4-{[2,3,6-trideoxy-3-(dimethylamino)-α-L-lyxo-hexopyranosyl]oxy}-1,2,3,4,6,11-hexahydrotetracene-1-carboxylate
15-demethoxyaclacinomycin T = (1R,2R,4S)-2-ethyl-1,2,3,4,6,11-hexahydro-2,5,7-trihydroxy-6,11-dioxo-4-{[2,3,6-trideoxy-3-(dimethylamino)-α-L-lyxo-hexopyranosyl]oxy}-1-naphthacenecarboxylic acid = (1R,2R,4S)-2-ethyl-2,5,7-trihydroxy-6,11-dioxo-4-{[2,3,6-trideoxy-3-(dimethylamino)-α-L-lyxo-hexopyranosyl]oxy}-1,2,3,4,6,11-hexahydrotetracene-1-carboxylic acid
Other name(s): RdmC; aclacinomycin methyl esterase
Systematic name: aclacinomycin T acylhydrolase
Comments: The enzyme is involved in the modification of the aklavinone skeleton in the biosynthesis of anthracyclines in Streptomyces species.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Wang, Y., Niemi, J., Airas, K., Ylihonko, K., Hakala, J. and Mantsala, P. Modifications of aclacinomycin T by aclacinomycin methyl esterase (RdmC) and aclacinomycin-10-hydroxylase (RdmB) from Streptomyces purpurascens. Biochim. Biophys. Acta 1480 (2000) 191–200. [PMID: 11004563]
2.  Jansson, A., Niemi, J., Mantsala, P. and Schneider, G. Crystal structure of aclacinomycin methylesterase with bound product analogues: implications for anthracycline recognition and mechanism. J. Biol. Chem. 278 (2003) 39006–39013. [PMID: 12878604]
[EC 3.1.1.95 created 2013]
 
 
EC 3.1.3.91
Accepted name: 7-methylguanosine nucleotidase
Reaction: (1) N7-methyl-GMP + H2O = N7-methyl-guanosine + phosphate
(2) CMP + H2O = cytidine + phosphate
Other name(s): cytosolic nucleotidase III-like; cNIII-like; N7-methylguanylate 5′-phosphatase
Systematic name: N7-methyl-GMP phosphohydrolase
Comments: The enzyme also has low activity with N7-methyl-GDP, producing N7-methyl-GMP. Does not accept AMP or GMP, and has low activity with UMP.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Buschmann, J., Moritz, B., Jeske, M., Lilie, H., Schierhorn, A. and Wahle, E. Identification of Drosophila and human 7-methyl GMP-specific nucleotidases. J. Biol. Chem. 288 (2013) 2441–2451. [PMID: 23223233]
[EC 3.1.3.91 created 2013]
 
 
EC 3.1.3.92
Accepted name: kanosamine-6-phosphate phosphatase
Reaction: kanosamine 6-phosphate + H2O = kanosamine + phosphate
For diagram of kanosamine biosynthesis, click here
Glossary: kanosamine = 3-amino-3-deoxy-D-glucose
Other name(s): ntdB (gene name)
Systematic name: kanosamine-6-phosphate phosphohydrolase
Comments: The enzyme, found in the bacterium Bacillus subtilis, is involved in a kanosamine biosynthesis pathway.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Vetter, N.D., Langill, D.M., Anjum, S., Boisvert-Martel, J., Jagdhane, R.C., Omene, E., Zheng, H., van Straaten, K.E., Asiamah, I., Krol, E.S., Sanders, D.A. and Palmer, D.R. A previously unrecognized kanosamine biosynthesis pathway in Bacillus subtilis. J. Am. Chem. Soc. 135 (2013) 5970–5973. [PMID: 23586652]
[EC 3.1.3.92 created 2013]
 
 
EC 3.2.1.186
Accepted name: protodioscin 26-O-β-D-glucosidase
Reaction: protodioscin + H2O = 26-deglucoprotodioscin + D-glucose
Other name(s): F26G; torvosidase; CSF26G1; furostanol glycoside 26-O-β-D-glucosidase; furostanol 26-O-β-D-glucoside glucohydrolase
Systematic name: protodioscin glucohydrolase
Comments: The enzyme has been characterized from the plants Cheilocostus speciosus and Solanum torvum. It also hydrolyses the 26-β-D-glucose group from related steroid glucosides such as protogracillin, torvoside A and torvoside H.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Inoue, K. and Ebizuka, Y. Purification and characterization of furostanol glycoside 26-O-β-glucosidase from Costus speciosus rhizomes. FEBS Lett. 378 (1996) 157–160. [PMID: 8549824]
2.  Arthan, D., Kittakoop, P., Esen, A. and Svasti, J. Furostanol glycoside 26-O-β-glucosidase from the leaves of Solanum torvum. Phytochemistry 67 (2006) 27–33. [PMID: 16289258]
[EC 3.2.1.186 created 2013]
 
 
EC 3.6.3.55
Accepted name: tungstate-importing ATPase
Reaction: ATP + H2O + tungstate[side 1] = ADP + phosphate + tungstate[side 2]
Other name(s): tungstate transporter; WtpABC; TupABC; tungstate-specific ABC transporter
Systematic name: ATP phosphohydrolase (tungstate-importing)
Comments: An ABC-type (ATP-binding cassette-type) ATPase. The enzymes from the archaeon Pyrococcus furiosus, the Gram-positive bacterium Eubacterium acidaminophilum and the Gram-negative bacterium Campylobacter jejuni transport tungsten into the cell for incorporation into tungsten-dependent enzymes.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Makdessi, K., Andreesen, J.R. and Pich, A. Tungstate uptake by a highly specific ABC transporter in Eubacterium acidaminophilum. J. Biol. Chem. 276 (2001) 24557–24564. [PMID: 11292832]
2.  Bevers, L.E., Hagedoorn, P.L., Krijger, G.C. and Hagen, W.R. Tungsten transport protein A (WtpA) in Pyrococcus furiosus: the first member of a new class of tungstate and molybdate transporters. J. Bacteriol. 188 (2006) 6498–6505. [PMID: 16952940]
3.  Smart, J.P., Cliff, M.J. and Kelly, D.J. A role for tungsten in the biology of Campylobacter jejuni: tungstate stimulates formate dehydrogenase activity and is transported via an ultra-high affinity ABC system distinct from the molybdate transporter. Mol. Microbiol. 74 (2009) 742–757. [PMID: 19818021]
[EC 3.6.3.55 created 2013]
 
 
*EC 3.7.1.9
Accepted name: 2-hydroxymuconate-6-semialdehyde hydrolase
Reaction: 2-hydroxymuconate-6-semialdehyde + H2O = formate + 2-oxopent-4-enoate
For diagram of catechol catabolism (meta ring cleavage), click here
Glossary: 2-hydroxymuconate-6-semialdehyde = (2Z,4E)-2-hydroxy-6-oxohexa-2,4-dienoate
Other name(s): 2-hydroxy-6-oxohepta-2,4-dienoate hydrolase; 2-hydroxymuconic semialdehyde hydrolase; HMSH; HOD hydrolase; xylF (gene name); 2-hydroxymuconate-semialdehyde formylhydrolase; 2-hydroxymuconate-semialdehyde hydrolase
Systematic name: 2-hydroxymuconate-6-semialdehyde formylhydrolase
Comments: The enzyme is involved in the degradation of catechols.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, UM-BBD, CAS registry number: 54004-61-4
References:
1.  Sala-Trepat, J.M. and Evans, W.C. The meta cleavage of catechol by Azotobacter species. 4-Oxalocrotonate pathway. Eur. J. Biochem. 20 (1971) 400–413. [PMID: 4325686]
2.  Harayama, S., Rekik, M., Wasserfallen, A. and Bairoch, A. Evolutionary relationships between catabolic pathways for aromatics: conservtion of gene order and nucleotide sequences of catechol oxidation genes of pWW0 and NAH7 plasmids. MGG Mol. Gen. Genet. 210 (1987) 241–247. [PMID: 3481421]
3.  Diaz, E. and Timmis, K.N. Identification of functional residues in a 2-hydroxymuconic semialdehyde hydrolase. A new member of the α/β hydrolase-fold family of enzymes which cleaves carbon-carbon bonds. J. Biol. Chem. 270 (1995) 6403–6411. [PMID: 7890778]
[EC 3.7.1.9 created 1990, modified 2013]
 
 
*EC 4.1.2.33
Accepted name: fucosterol-epoxide lyase
Reaction: (24R,241R)-fucosterol epoxide = desmosterol + acetaldehyde
Glossary: (24R,241R)-fucosterol epoxide = (3β,24R,28R)-24,28-epoxystigmast-5-en-3-ol
Other name(s): (24R,24′R)-fucosterol-epoxide acetaldehyde-lyase; (24R,24′R)-fucosterol-epoxide acetaldehyde-lyase (desmosterol-forming)
Systematic name: (24R,241R)-fucosterol-epoxide acetaldehyde-lyase (desmosterol-forming)
Comments: The insect enzyme is involved in the conversion of sitosterol into cholesterol.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 99676-42-3
References:
1.  Prestwich, G.D., Angelastro, M., De Palma, A. and Perino, M.A. Fucosterol epoxide lyase of insects: synthesis of labeled substrates and development of a partition assay. Anal. Biochem. 151 (1985) 315–326. [PMID: 3913328]
[EC 4.1.2.33 created 1989, modified 2013]
 
 
EC 4.1.2.54
Accepted name: L-threo-3-deoxy-hexylosonate aldolase
Reaction: 2-dehydro-3-deoxy-L-galactonate = pyruvate + L-glyceraldehyde
Other name(s): GAAC; LGA1
Systematic name: 2-dehydro-3-deoxy-L-galactonate L-glyceraldehyde-lyase (pyruvate-forming)
Comments: The enzyme takes part in a D-galacturonate degradation pathway in the fungi Aspergillus niger and Trichoderma reesei (Hypocrea jecorina).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Hilditch, S., Berghall, S., Kalkkinen, N., Penttila, M. and Richard, P. The missing link in the fungal D-galacturonate pathway: identification of the L-threo-3-deoxy-hexulosonate aldolase. J. Biol. Chem. 282 (2007) 26195–26201. [PMID: 17609199]
2.  Martens-Uzunova, E.S. and Schaap, P.J. An evolutionary conserved D-galacturonic acid metabolic pathway operates across filamentous fungi capable of pectin degradation. Fungal Genet. Biol. 45 (2008) 1449–1457. [PMID: 18768163]
[EC 4.1.2.54 created 2013]
 
 
EC 4.1.3.44
Accepted name: tRNA 4-demethylwyosine synthase (AdoMet-dependent)
Reaction: N1-methylguanine37 in tRNAPhe + pyruvate + S-adenosyl-L-methionine = 4-demethylwyosine37 in tRNAPhe + L-methionine + 5′-deoxyadenosine + CO2 + H2O
For diagram of wyosine biosynthesis, click here
Glossary: 4-demethylwyosine = imG-14 = 6-methyl-3-(β-D-ribofuranosyl)-3,5-dihydro-9H-imidazo[1,2-a]purin-9-one
Other name(s): TYW1
Systematic name: tRNAPhe N1-methylguanine,pyruvate acetaldehyde-lyase (tRNAPhe 4-demethylwyosine-forming, decarboxylating, dehydrating)
Comments: This enzyme, which is a member of the superfamily of S-adenosyl-L-methionine-dependent radical (radical AdoMet) enzymes, binds two [4Fe-4S] clusters [3,4]. Carbons C2 and C3 from pyruvate are incorporated into 4-demethylwyosine [3]. The enzyme is found in eukaryotes where it is part of the pathway for wybutosine synthesis, and in archaea, where it is involved in the biosynthesis of archaeal wye bases, such as wyosine, isowyosine, and methylwyosine.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Goto-Ito, S., Ishii, R., Ito, T., Shibata, R., Fusatomi, E., Sekine, S.I., Bessho, Y. and Yokoyama, S. Structure of an archaeal TYW1, the enzyme catalyzing the second step of wye-base biosynthesis. Acta Crystallogr. D Biol. Crystallogr. 63 (2007) 1059–1068. [PMID: 17881823]
2.  Suzuki, Y., Noma, A., Suzuki, T., Senda, M., Senda, T., Ishitani, R. and Nureki, O. Crystal structure of the radical SAM enzyme catalyzing tricyclic modified base formation in tRNA. J. Mol. Biol. 372 (2007) 1204–1214. [PMID: 17727881]
3.  Young, A.P. and Bandarian, V. Pyruvate is the source of the two carbons that are required for formation of the imidazoline ring of 4-demethylwyosine. Biochemistry 50 (2011) 10573–10575. [PMID: 22026549]
4.  Perche-Letuvée, P., Kathirvelu, V., Berggren, G., Clemancey, M., Latour, J.M., Maurel, V., Douki, T., Armengaud, J., Mulliez, E., Fontecave, M., Garcia-Serres, R., Gambarelli, S. and Atta, M. 4-Demethylwyosine synthase from Pyrococcus abyssi is a radical-S-adenosyl-L-methionine enzyme with an additional [4Fe-4S]2+ cluster that interacts with the pyruvate co-substrate. J. Biol. Chem. 287 (2012) 41174–41185. [PMID: 23043105]
[EC 4.1.3.44 created 2013]
 
 
EC 4.2.1.4
Deleted entry: citrate dehydratase. Now known to be a partial reaction catalysed by EC 4.2.1.3, aconitate hydratase.
[EC 4.2.1.4 created 1961, deleted 2013]
 
 
EC 4.2.1.145
Accepted name: capreomycidine synthase
Reaction: (2S,3S)-3-hydroxyarginine = (2S,3R)-capreomycidine + H2O
Glossary: (2S,3R)-capreomycidine = (S)-2-amino-2-[(R)-2-iminohexahydropyrimidin-4-yl]acetic acid
Other name(s): VioD (ambiguous)
Systematic name: (2S,3S)-3-hydroxyarginine hydro-lyase (cyclizing, (2S,3R)-capreomycidine-forming)
Comments: A pyridoxal 5′-phosphate protein. The enzyme is involved in the biosynthesis of the cyclic pentapeptide antibiotic viomycin.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Yin, X., McPhail, K.L., Kim, K.J. and Zabriskie, T.M. Formation of the nonproteinogenic amino acid (2S,3R)-capreomycidine by VioD from the viomycin biosynthesis pathway. ChemBioChem. 5 (2004) 1278–1281. [PMID: 15368581]
2.  Ju, J., Ozanick, S.G., Shen, B. and Thomas, M.G. Conversion of (2S)-arginine to (2S,3R)-capreomycidine by VioC and VioD from the viomycin biosynthetic pathway of Streptomyces sp. strain ATCC11861. ChemBioChem. 5 (2004) 1281–1285. [PMID: 15368582]
[EC 4.2.1.145 created 2013]
 
 
EC 4.2.1.146
Accepted name: L-galactonate dehydratase
Reaction: L-galactonate = 2-dehydro-3-deoxy-L-galactonate + H2O
Other name(s): LGD1
Systematic name: L-galactonate hydro-lyase (2-dehydro-3-deoxy-L-galactonate-forming)
Comments: The enzyme takes part in a D-galacturonate degradation pathway in the fungi Trichoderma reesei (Hypocrea jecorina) and Aspergillus niger.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Kuorelahti, S., Jouhten, P., Maaheimo, H., Penttila, M. and Richard, P. L-Galactonate dehydratase is part of the fungal path for D-galacturonic acid catabolism. Mol. Microbiol. 61 (2006) 1060–1068. [PMID: 16879654]
2.  Martens-Uzunova, E.S. and Schaap, P.J. An evolutionary conserved D-galacturonic acid metabolic pathway operates across filamentous fungi capable of pectin degradation. Fungal Genet. Biol. 45 (2008) 1449–1457. [PMID: 18768163]
[EC 4.2.1.146 created 2013]
 
 
EC 4.2.3.144
Accepted name: geranyllinalool synthase
Reaction: geranylgeranyl diphosphate + H2O = (E,E)-geranyllinalool + diphosphate
For diagram of acyclic diterpenoid biosynthesis, click here
Glossary: geranylgeranyl diphosphate = (2E,6E,10E)-3,7,11,15-tetramethylhexadeca-2,6,10,14-tetraen-1-yl diphosphate
(E,E)-geranyllinalool = (6E,10E)-3,7,11,15-tetramethylhexadeca-1,6,10,14-tetraen-3-ol
Other name(s): TPS04/GES; GES
Systematic name: geranylgeranyl diphosphate diphosphate-lyase ((E,E)-geranyllinalool-forming)
Comments: The enzyme is a component of the herbivore-induced indirect defense system. The product, (E,E)-geranyllinalool, is a precursor to the volatile compound 4,8,12-trimethyl-1,3,7,11-tridecatetraene (TMTT), which is released by many plants in response to damage.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Herde, M., Gartner, K., Kollner, T.G., Fode, B., Boland, W., Gershenzon, J., Gatz, C. and Tholl, D. Identification and regulation of TPS04/GES, an Arabidopsis geranyllinalool synthase catalyzing the first step in the formation of the insect-induced volatile C16-homoterpene TMTT. Plant Cell 20 (2008) 1152–1168. [PMID: 18398052]
2.  Attaran, E., Rostas, M. and Zeier, J. Pseudomonas syringae elicits emission of the terpenoid (E,E)-4,8,12-trimethyl-1,3,7,11-tridecatetraene in Arabidopsis leaves via jasmonate signaling and expression of the terpene synthase TPS4. Mol Plant Microbe Interact 21 (2008) 1482–1497. [PMID: 18842097]
[EC 4.2.3.144 created 2013]
 
 
EC 4.4.1.27 – public review until 20 December 2013 [Last modified: 2013-11-22 16:06:20]
Transferred entry: carbon disulfide lyase. Now EC 3.13.1.5, carbon disulfide hydrolase
[EC 4.4.1.27 created 2013, deleted 2017]
 
 
EC 5.1.3.26
Accepted name: N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol 4-epimerase
Reaction: N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = N-acetyl-α-D-galactosaminyl-diphospho-ditrans,octacis-undecaprenol
Other name(s): GlcNAc-P-P-Und epimerase; GlcNAc-P-P-Und 4-epimerase; gne (gene name)
Systematic name: N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol 4-epimerase
Comments: The enzyme is involved in biosynthesis of the repeating tetrasaccharide unit of the O-antigen produced by some Gram-negative bacteria.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Rush, J.S., Alaimo, C., Robbiani, R., Wacker, M. and Waechter, C.J. A novel epimerase that converts GlcNAc-P-P-undecaprenol to GalNAc-P-P-undecaprenol in Escherichia coli O157. J. Biol. Chem. 285 (2010) 1671–1680. [PMID: 19923219]
[EC 5.1.3.26 created 2013]
 
 
EC 5.3.1.29
Accepted name: ribose 1,5-bisphosphate isomerase
Reaction: α-D-ribose 1,5-bisphosphate = D-ribulose 1,5-bisphosphate
For diagram of AMP catabolism, click here
Other name(s): R15P isomerase; ribulose 1,5-bisphosphate synthase; RuBP synthase
Systematic name: α-D-ribose 1,5-bisphosphate aldose-ketose-isomerase
Comments: This archaeal enzyme is involved in AMP metabolism and CO2 fixation through type III RubisCO enzymes. The enzyme is activated by cAMP [2].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Sato, T., Atomi, H. and Imanaka, T. Archaeal type III RuBisCOs function in a pathway for AMP metabolism. Science 315 (2007) 1003–1006. [PMID: 17303759]
2.  Aono, R., Sato, T., Yano, A., Yoshida, S., Nishitani, Y., Miki, K., Imanaka, T. and Atomi, H. Enzymatic characterization of AMP phosphorylase and ribose-1,5-bisphosphate isomerase functioning in an archaeal AMP metabolic pathway. J. Bacteriol. 194 (2012) 6847–6855. [PMID: 23065974]
3.  Nakamura, A., Fujihashi, M., Aono, R., Sato, T., Nishiba, Y., Yoshida, S., Yano, A., Atomi, H., Imanaka, T. and Miki, K. Dynamic, ligand-dependent conformational change triggers reaction of ribose-1,5-bisphosphate isomerase from Thermococcus kodakarensis KOD1. J. Biol. Chem. 287 (2012) 20784–20796. [PMID: 22511789]
[EC 5.3.1.29 created 2013]
 
 
EC 5.4.99.59
Accepted name: dTDP-fucopyranose mutase
Reaction: dTDP-α-D-fucopyranose = dTDP-α-D-fucofuranose
For diagram of dTDP-6-deoxyhexose biosynthesis, click here
Other name(s): Fcf2
Systematic name: dTDP-α-D-fucopyranose furanomutase
Comments: The enzyme is involved in the biosynthesis of the Escherichia coli O52 O antigen.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Wang, Q., Ding, P., Perepelov, A.V., Xu, Y., Wang, Y., Knirel, Y.A., Wang, L. and Feng, L. Characterization of the dTDP-D-fucofuranose biosynthetic pathway in Escherichia coli O52. Mol. Microbiol. 70 (2008) 1358–1367. [PMID: 19019146]
[EC 5.4.99.59 created 2013]
 
 
EC 5.5.1.23
Accepted name: aklanonic acid methyl ester cyclase
Reaction: aklaviketone = methyl aklanonate
For diagram of aklavinone biosynthesis, click here
Glossary: aklaviketone = methyl (1R,2R)-2-ethyl-2,5,7-trihydroxy-4,6,11-trioxo-1,2,3,4,6,11-hexahydrotetracene-1-carboxylate
methyl aklanonate = methyl [4,5-dihydroxy-9,10-dioxo-3-(3-oxopentanoyl)-9,10-dihydroanthracen-2-yl]acetate
Other name(s): dauD (gene name); aknH (gene name); dnrD (gene name); methyl aklanonate cyclase; methyl aklanonate-aklaviketone isomerase (cyclizing); aklaviketone lyase (decyclizing)
Systematic name: aklaviketone lyase (ring-opening)
Comments: The enzyme is involved in the biosynthesis of aklaviketone, an intermediate in the biosynthetic pathways leading to formation of several anthracycline antibiotics, including aclacinomycin, daunorubicin and doxorubicin.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Dickens, M.L., Ye, J. and Strohl, W.R. Analysis of clustered genes encoding both early and late steps in daunomycin biosynthesis by Streptomyces sp. strain C5. J. Bacteriol. 177 (1995) 536–543. [PMID: 7836284]
2.  Kendrew, S.G., Katayama, K., Deutsch, E., Madduri, K. and Hutchinson, C.R. DnrD cyclase involved in the biosynthesis of doxorubicin: purification and characterization of the recombinant enzyme. Biochemistry 38 (1999) 4794–4799. [PMID: 10200167]
3.  Kallio, P., Sultana, A., Niemi, J., Mantsala, P. and Schneider, G. Crystal structure of the polyketide cyclase AknH with bound substrate and product analogue: implications for catalytic mechanism and product stereoselectivity. J. Mol. Biol. 357 (2006) 210–220. [PMID: 16414075]
[EC 5.5.1.23 created 2013, modified 2014]
 
 
EC 6.3.1.16
Transferred entry: carbapenam-3-carboxylate synthetase. The enzyme was discovered at the public-review stage to have been misclassified and so was withdrawn. See EC 6.3.3.6, carbapenam-3-carboxylate synthase
[EC 6.3.1.16 created 2013, deleted 2013]
 
 
EC 6.3.3.6
Accepted name: carbapenam-3-carboxylate synthase
Reaction: ATP + (2S,5S)-5-carboxymethylproline = AMP + diphosphate + (3S,5S)-carbapenam 3-carboxylate
Other name(s): CarA (ambiguous); CPS (ambiguous); carbapenam-3-carboxylate ligase; 6-methyl-(2S,5S)-5-carboxymethylproline cyclo-ligase (AMP-forming)
Systematic name: (2S,5S)-5-carboxymethylproline cyclo-ligase (AMP-forming)
Comments: The enzyme is involved in the biosynthesis of the carbapenem β-lactam antibiotic (5R)-carbapen-2-em-3-carboxylate in the bacterium Pectobacterium carotovorum.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Gerratana, B., Stapon, A. and Townsend, C.A. Inhibition and alternate substrate studies on the mechanism of carbapenam synthetase from Erwinia carotovora. Biochemistry 42 (2003) 7836–7847. [PMID: 12820893]
2.  Miller, M.T., Gerratana, B., Stapon, A., Townsend, C.A. and Rosenzweig, A.C. Crystal structure of carbapenam synthetase (CarA). J. Biol. Chem. 278 (2003) 40996–41002. [PMID: 12890666]
3.  Raber, M.L., Arnett, S.O. and Townsend, C.A. A conserved tyrosyl-glutamyl catalytic dyad in evolutionarily linked enzymes: carbapenam synthetase and β-lactam synthetase. Biochemistry 48 (2009) 4959–4971. [PMID: 19371088]
4.  Arnett, S.O., Gerratana, B. and Townsend, C.A. Rate-limiting steps and role of active site Lys443 in the mechanism of carbapenam synthetase. Biochemistry 46 (2007) 9337–9345. [PMID: 17658887]
[EC 6.3.3.6 created 2013 as 6.3.1.16, transferred 2013 to EC 6.3.3.6]
 
 
*EC 6.5.1.4
Accepted name: RNA 3′-terminal-phosphate cyclase (ATP)
Reaction: ATP + [RNA]-3′-(3′-phospho-ribonucleoside) = AMP + diphosphate + [RNA]-3′-(2′,3′-cyclophospho)-ribonucleoside (overall reaction)
(1a) ATP + [RNA 3′-phosphate cyclase]-L-histidine = [RNA 3′-phosphate cyclase]-Nτ-(5′-adenylyl)-L-histidine + diphosphate
(1b) [RNA 3′-phosphate cyclase]-Nτ-(5′-adenylyl)-L-histidine + [RNA]-3′-(3′-phospho-ribonucleoside) = [RNA 3′-phosphate cyclase]-L-histidine + [RNA]-3′-ribonucleoside-3′-(5′-diphosphoadenosine)
(1c) [RNA]-3′-ribonucleoside-3′-(5′-diphosphoadenosine) = [RNA]-3′-(2′,3′-cyclophospho)-ribonucleoside + AMP
Other name(s): rtcA (gene name); RNA cyclase (ambiguous); RNA-3′-phosphate cyclase (ambiguous)
Systematic name: RNA-3′-phosphate:RNA ligase (cyclizing, AMP-forming)
Comments: The enzyme converts the 3′-terminal phosphate of various RNA substrates into the 2′,3′-cyclic phosphodiester in an ATP-dependent reaction. Catalysis occurs by a three-step mechanism, starting with the activation of the enzyme by ATP, forming a phosphoramide bond between adenylate and a histidine residue [5,6]. The adenylate group is then transferred to the 3′-phosphate terminus of the substrate, forming the capped structure [RNA]-3′-(5′-diphosphoadenosine). Finally, the enzyme catalyses an attack of the vicinal O-2′ on the 3′-phosphorus, which results in formation of cyclic phosphate and release of the adenylate. The enzyme also has a polynucleotide 5′ adenylylation activity [7]. cf. EC 6.5.1.5, RNA 3′-terminal-phosphate cyclase (GTP).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, PDB, CAS registry number: 85638-41-1
References:
1.  Filipowicz, W., Konarska, M., Gross, H.J. and Shatkin, A.J. RNA 3′-terminal phosphate cyclase activity and RNA ligation in HeLa cell extract. Nucleic Acids Res. 11 (1983) 1405–1418. [PMID: 6828385]
2.  Reinberg, D., Arenas, J. and Hurwitz, J. The enzymatic conversion of 3′-phosphate terminated RNA chains to 2′,3′-cyclic phosphate derivatives. J. Biol. Chem. 260 (1985) 6088–6097. [PMID: 2581947]
3.  Genschik, P., Billy, E., Swianiewicz, M. and Filipowicz, W. The human RNA 3′-terminal phosphate cyclase is a member of a new family of proteins conserved in Eucarya, Bacteria and Archaea. EMBO J. 16 (1997) 2955–2967. [PMID: 9184239]
4.  Genschik, P., Drabikowski, K. and Filipowicz, W. Characterization of the Escherichia coli RNA 3′-terminal phosphate cyclase and its σ54-regulated operon. J. Biol. Chem. 273 (1998) 25516–25526. [PMID: 9738023]
5.  Billy, E., Hess, D., Hofsteenge, J. and Filipowicz, W. Characterization of the adenylation site in the RNA 3′-terminal phosphate cyclase from Escherichia coli. J. Biol. Chem. 274 (1999) 34955–34960. [PMID: 10574971]
6.  Tanaka, N. and Shuman, S. Structure-activity relationships in human RNA 3′-phosphate cyclase. RNA 15 (2009) 1865–1874. [PMID: 19690099]
7.  Chakravarty, A.K. and Shuman, S. RNA 3′-phosphate cyclase (RtcA) catalyzes ligase-like adenylylation of DNA and RNA 5′-monophosphate ends. J. Biol. Chem. 286 (2011) 4117–4122. [PMID: 21098490]
8.  Das, U. and Shuman, S. 2′-Phosphate cyclase activity of RtcA: a potential rationale for the operon organization of RtcA with an RNA repair ligase RtcB in Escherichia coli and other bacterial taxa. RNA 19 (2013) 1355–1362. [PMID: 23945037]
[EC 6.5.1.4 created 1986, modified 1989, modified 2013, modified 2016]
 
 
EC 6.5.1.5
Accepted name: RNA 3′-terminal-phosphate cyclase (GTP)
Reaction: GTP + [RNA]-3′-(3′-phospho-ribonucleoside) = GMP + diphosphate + [RNA]-3′-(2′,3′-cyclophospho)-ribonucleoside (overall reaction)
(1a) GTP + [RNA 3′-phosphate cyclase]-L-histidine = 5′-guanosyl [RNA 3′-phosphate cyclase]-Nτ-phosphono-L-histidine + diphosphate
(1b) 5′-guanosyl [RNA 3′-phosphate cyclase]-Nτ-phosphono-L-histidine + [RNA]-3′-(3′-phospho-ribonucleoside) = [RNA 3′-phosphate cyclase]-L-histidine + [RNA]-3′-ribonucleoside-3′-(5′-diphosphoguanosine)
(1c) [RNA]-3′-ribonucleoside-3′-(5′-diphosphoguanosine) = [RNA]-3′-(2′,3′-cyclophospho)-ribonucleoside + GMP
Other name(s): Pf-Rtc; RNA-3′-phosphate cyclase (GTP)
Systematic name: RNA-3′-phosphate:RNA ligase (cyclizing, GMP-forming)
Comments: The enzyme, which is specific for GTP, was characterized from the archaeon Pyrococcus furiosus. The enzyme converts the 3′-terminal phosphate of various RNA substrates into the 2′,3′-cyclic phosphodiester in a GTP-dependent reaction. Catalysis occurs by a three-step mechanism, starting with the activation of the enzyme by GTP, forming a phosphoramide bond between guanylate and a histidine residue. The guanylate group is then transferred to the 3′-phosphate terminus of the substrate, forming the capped structure [RNA]-3′-(5′-diphosphoguanosine). Finally, the enzyme catalyses an attack of the vicinal O-2′ on the 3′-phosphorus, which results in formation of cyclic phosphate and release of the guanylate. cf. EC 6.5.1.4, RNA-3′-phosphate cyclase (ATP).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Sato, A., Soga, T., Igarashi, K., Takesue, K., Tomita, M. and Kanai, A. GTP-dependent RNA 3′-terminal phosphate cyclase from the hyperthermophilic archaeon Pyrococcus furiosus. Genes Cells 16 (2011) 1190–1199. [PMID: 22074260]
[EC 6.5.1.5 created 2013, modified 2016]
 
 


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