Proposed Changes to the Enzyme List

References:

1.	Taylor, M.B. and Juni, E. Stereoisomeric specificities of 2,3-butanediol dehydrogenase. Biochim. Biophys. Acta 39 (1960) 448–457. [DOI] [PMID: 13837186]
2.	Carballo, J., Martin, R., Bernardo, A. and Gonzalez, J. Purification, characterization and some properties of diacetyl(acetoin) reductase from Enterobacter aerogenes. Eur. J. Biochem. 198 (1991) 327–332. [DOI] [PMID: 2040298]
3.	Takusagawa, Y., Otagiri, M., Ui, S., Ohtsuki, T., Mimura, A., Ohkuma, M. and Kudo, T. Purification and characterization of L-2,3-butanediol dehydrogenase of Brevibacterium saccharolyticum C-1012 expressed in Escherichia coli. Biosci. Biotechnol. Biochem. 65 (2001) 1876–1878. [DOI] [PMID: 11577733]

[EC 1.1.1.76 created 1972, modified 2010]

1.1.1.301

Accepted name:

D-arabitol-phosphate dehydrogenase

Reaction:

D-arabinitol 1-phosphate + NAD⁺ = D-xylulose 5-phosphate + NADH + H⁺

Other name(s):

APDH; D-arabitol 1-phosphate dehydrogenase; D-arabitol 5-phosphate dehydrogenase; D-arabinitol 1-phosphate dehydrogenase; D-arabinitol 5-phosphate dehydrogenase

Systematic name:

D-arabinitol-phosphate:NAD⁺ oxidoreductase

Comments:

This enzyme participates in arabinitol catabolism. The enzyme also converts D-arabinitol 5-phosphate to D-ribulose 5-phosphate at a lower rate [1].

Links to other databases:

References:

1.	Povelainen, M., Eneyskaya, E.V., Kulminskaya, A.A., Ivanen, D.R., Kalkkinen, N., Neustroev, K.N. and Miasnikov, A.N. Biochemical and genetic characterization of a novel enzyme of pentitol metabolism: D-arabitol-phosphate dehydrogenase. Biochem. J. 371 (2003) 191–197. [DOI] [PMID: 12467497]

[EC 1.1.1.301 created 2010]

1.1.1.302

Accepted name:

2,5-diamino-6-(ribosylamino)-4(3H)-pyrimidinone 5′-phosphate reductase

Reaction:

2,5-diamino-6-(5-phospho-D-ribitylamino)pyrimidin-4(3H)-one + NAD(P)⁺ = 2,5-diamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + NAD(P)H + H⁺

For diagram of riboflavin biosynthesis (early stages), click here

Other name(s):

2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5′-phosphate reductase; MjaRED; MJ0671 (gene name)

Systematic name:

2,5-diamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one:NAD(P)⁺ oxidoreductase

Comments:

The reaction proceeds in the opposite direction. A step in riboflavin biosynthesis, NADPH and NADH function equally well as reductant. Differs from EC 1.1.1.193 [5-amino-6-(5-phosphoribosylamino)uracil reductase] since it does not catalyse the reduction of 5-amino-6-ribosylaminopyrimidine-2,4(1H,3H)-dione 5′-phosphate [1].

Links to other databases:

References:

1.	Graupner, M., Xu, H. and White, R.H. The pyrimidine nucleotide reductase step in riboflavin and F₄₂₀ biosynthesis in archaea proceeds by the eukaryotic route to riboflavin. J. Bacteriol. 184 (2002) 1952–1957. [DOI] [PMID: 11889103]
2.	Chatwell, L., Krojer, T., Fidler, A., Romisch, W., Eisenreich, W., Bacher, A., Huber, R. and Fischer, M. Biosynthesis of riboflavin: structure and properties of 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5′-phosphate reductase of Methanocaldococcus jannaschii. J. Mol. Biol. 359 (2006) 1334–1351. [DOI] [PMID: 16730025]

[EC 1.1.1.302 created 2010, modified 2011]

1.1.1.303

Accepted name:

diacetyl reductase [(R)-acetoin forming]

Reaction:

(R)-acetoin + NAD⁺ = diacetyl + NADH + H⁺

Other name(s):

(R)-acetoin dehydrogenase

Systematic name:

(R)-acetoin:NAD⁺ oxidoreductase

Comments:

The reaction is catalysed in the reverse direction. This activity is usually associated with butanediol dehydrogenase activity (EC 1.1.1.4 or EC 1.1.1.76). While the butanediol dehydrogenase activity is reversible, diacetyl reductase activity is irreversible. This enzyme has been reported in the yeast Saccharomyces cerevisiae [1,2]. Different from EC 1.1.1.304, diacetyl reductase [(S)-acetoin forming].

Links to other databases:

References:

1.	Heidlas, J. and Tressl, R. Purification and characterization of a (R)-2,3-butanediol dehydrogenase from Saccharomyces cerevisiae. Arch. Microbiol. 154 (1990) 267–273. [PMID: 2222122]
2.	Gonzalez, E., Fernandez, M.R., Larroy, C., Sola, L., Pericas, M.A., Pares, X. and Biosca, J.A. Characterization of a (2R,3R)-2,3-butanediol dehydrogenase as the Saccharomyces cerevisiae YAL060W gene product. Disruption and induction of the gene. J. Biol. Chem. 275 (2000) 35876–35885. [DOI] [PMID: 10938079]

[EC 1.1.1.303 created 2010 (EC 1.1.1.5 created 1961, modified 1976, part incorporated 2010)]

1.1.1.304

Accepted name:

diacetyl reductase [(S)-acetoin forming]

Reaction:

(S)-acetoin + NAD⁺ = diacetyl + NADH + H⁺

Other name(s):

(S)-acetoin dehydrogenase

Systematic name:

(S)-acetoin:NAD⁺ oxidoreductase

Comments:

The reaction is catalysed in the reverse direction. This activity is usually associated with butanediol dehydrogenase activity (EC 1.1.1.4 or EC 1.1.1.76). While the butanediol dehydrogenase activity is reversible, diacetyl reductase activity is irreversible. This enzyme has been reported in the bacteria Geobacillus stearothermophilus, Enterobacter aerogenes and Klebsiella pneumoniae [1-3]. Different from EC 1.1.1.303, diacetyl reductase [(R)-acetoin forming].

Links to other databases:

References:

1.	Giovannini, P.P., Medici, A., Bergamini, C.M. and Rippa, M. Properties of diacetyl (acetoin) reductase from Bacillus stearothermophilus. Bioorg. Med. Chem. 4 (1996) 1197–1201. [DOI] [PMID: 8879540]
2.	Carballo, J., Martin, R., Bernardo, A. and Gonzalez, J. Purification, characterization and some properties of diacetyl(acetoin) reductase from Enterobacter aerogenes. Eur. J. Biochem. 198 (1991) 327–332. [DOI] [PMID: 2040298]
3.	Ui, S., Okajima, Y., Mimura, A., Kanai, H., Kobayashi, T., Kudo, T. Sequence analysis of the gene for and characterization of D-acetoin forming meso-2,3-butanediol dehydrogenase of Klebsiella pneumoniae expressed in Escherichia coli. J. Ferment. Bioeng. 83 (1997) 32–37.

[EC 1.1.1.304 created 2010 (EC 1.1.1.5 created 1961, modified 1976, part incorporated 2010)]

*EC

1.1.3.20

Accepted name:

long-chain-alcohol oxidase

Reaction:

a long-chain alcohol + O₂ = a long-chain aldehyde + H₂O₂

Other name(s):

long-chain fatty alcohol oxidase; fatty alcohol oxidase; fatty alcohol:oxygen oxidoreductase; long-chain fatty acid oxidase

Systematic name:

long-chain-alcohol:oxygen oxidoreductase

Comments:

Oxidizes long-chain fatty alcohols; best substrate is dodecyl alcohol.

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, CAS registry number: 129430-50-8

References:

1.	Moreau, R.A. and Huang, A.H.C. Oxidation of fatty alcohol in the cotyledons of jojoba seedlings. Arch. Biochem. Biophys. 194 (1979) 422–430. [DOI] [PMID: 36040]
2.	Moreau, R.A. and Huang, A.H.C. Enzymes of wax ester catabolism in jojoba. Methods Enzymol. 71 (1981) 804–813.
3.	Cheng, Q., Liu, H.T., Bombelli, P., Smith, A. and Slabas, A.R. Functional identification of AtFao3, a membrane bound long chain alcohol oxidase in Arabidopsis thaliana. FEBS Lett. 574 (2004) 62–68. [DOI] [PMID: 15358540]
4.	Zhao, S., Lin, Z., Ma, W., Luo, D. and Cheng, Q. Cloning and characterization of long-chain fatty alcohol oxidase LjFAO1 in Lotus japonicus. Biotechnol. Prog. 24 (2008) 773–779. [DOI] [PMID: 18396913]
5.	Cheng, Q., Sanglard, D., Vanhanen, S., Liu, H.T., Bombelli, P., Smith, A. and Slabas, A.R. Candida yeast long chain fatty alcohol oxidase is a c-type haemoprotein and plays an important role in long chain fatty acid metabolism. Biochim. Biophys. Acta 1735 (2005) 192–203. [DOI] [PMID: 16046182]

[EC 1.1.3.20 created 1984, modified 2010]

1.1.5.6

Transferred entry:

formate dehydrogenase-N. Now EC 1.17.5.3, formate dehydrogenase-N

[EC 1.1.5.6 created 2010, deleted 2017]

1.1.5.7

Accepted name:

cyclic alcohol dehydrogenase (quinone)

Reaction:

a cyclic alcohol + a quinone = a cyclic ketone + a quinol

Other name(s):

cyclic alcohol dehydrogenase; MCAD

Systematic name:

cyclic alcohol:quinone oxidoreductase

Comments:

This enzyme oxidizes a wide variety of cyclic alcohols. Some minor enzyme activity is found with aliphatic secondary alcohols and sugar alcohols, but not primary alcohols. The enzyme is unable to catalyse the reverse reaction of cyclic ketones or aldehydes to cyclic alcohols. This enzyme differs from EC 1.1.5.5, alcohol dehydrogenase (quinone), which shows activity with ethanol [1].

Links to other databases:

References:

1.	Moonmangmee, D., Fujii, Y., Toyama, H., Theeragool, G., Lotong, N., Matsushita, K. and Adachi, O. Purification and characterization of membrane-bound quinoprotein cyclic alcohol dehydrogenase from Gluconobacter frateurii CHM 9. Biosci. Biotechnol. Biochem. 65 (2001) 2763–2772. [PMID: 11826975]

[EC 1.1.5.7 created 2010]

1.1.99.33

Transferred entry:

formate dehydrogenase (acceptor). Now EC 1.17.99.7, formate dehydrogenase (acceptor)

[EC 1.1.99.33 created 2010, deleted 2017]

1.2.1.77

Accepted name:

3,4-dehydroadipyl-CoA semialdehyde dehydrogenase (NADP⁺)

Reaction:

3,4-didehydroadipyl-CoA semialdehyde + NADP⁺ + H₂O = 3,4-didehydroadipyl-CoA + NADPH + H⁺

For diagram of Benzoyl-CoA catabolism, click here

Other name(s):

BoxD; 3,4-dehydroadipyl-CoA semialdehyde dehydrogenase

Systematic name:

3,4-didehydroadipyl-CoA semialdehyde:NADP⁺ oxidoreductase

Comments:

This enzyme catalyses a step in the aerobic benzoyl-coenzyme A catabolic pathway in Azoarcus evansii and Burkholderia xenovorans.

Links to other databases:

BRENDA, EAWAG-BBD, EXPASY, Gene, KEGG

References:

1.	Gescher, J., Ismail, W., Olgeschlager, E., Eisenreich, W., Worth, J. and Fuchs, G. Aerobic benzoyl-coenzyme A (CoA) catabolic pathway in Azoarcus evansii: conversion of ring cleavage product by 3,4-dehydroadipyl-CoA semialdehyde dehydrogenase. J. Bacteriol. 188 (2006) 2919–2927. [DOI] [PMID: 16585753]
2.	Bains, J. and Boulanger, M.J. Structural and biochemical characterization of a novel aldehyde dehydrogenase encoded by the benzoate oxidation pathway in Burkholderia xenovorans LB400. J. Mol. Biol. 379 (2008) 597–608. [DOI] [PMID: 18462753]

[EC 1.2.1.77 created 2010]

1.2.1.78

Accepted name:

2-formylbenzoate dehydrogenase

Reaction:

2-formylbenzoate + NAD⁺ + H₂O = o-phthalic acid + NADH + H⁺

Glossary:

o-phthalic acid = benzene-1,2-dicarboxylic acid
2-formylbenzoate = 2-carboxybenzaldehyde

Other name(s):

2-carboxybenzaldehyde dehydrogenase; 2CBAL dehydrogenase; PhdK

Systematic name:

2-formylbenzoate:NAD⁺ oxidoreductase

Comments:

The enzyme is involved in phenanthrene degradation.

Links to other databases:

References:

1.	Iwabuchi, T. and Harayama, S. Biochemical and genetic characterization of 2-carboxybenzaldehyde dehydrogenase, an enzyme involved in phenanthrene degradation by Nocardioides sp. strain KP7. J. Bacteriol. 179 (1997) 6488–6494. [DOI] [PMID: 9335300]
2.	Kiyohara, H., Nagao, K. and Yano, K. Isolation and some properties of NAD-linked 2-carboxybenzaldehyde dehydrogenase in Alcaligenes faecalis AFK 2 grown on phenanthrene. J. Gen. Appl. Microbiol. 27 (1981) 443–455.

[EC 1.2.1.78 created 2010]

1.4.3.23

Accepted name:

7-chloro-L-tryptophan oxidase

Reaction:

7-chloro-L-tryptophan + O₂ = 2-imino-3-(7-chloroindol-3-yl)propanoate + H₂O₂

For diagram of rebeccamycin biosynthesis, click here

Other name(s):

RebO

Systematic name:

7-chloro-L-tryptophan:oxygen oxidoreductase

Comments:

Contains a noncovalently bound FAD [1,2]. This enzyme catalyses a step in the biosynthesis of rebeccamycin, an indolocarbazole alkaloid produced by the bacterium Lechevalieria aerocolonigenes. During catalysis, the bound FAD is reoxidized at the expense of molecular oxygen, producing one molecule of hydrogen peroxide. The enzyme shows significant preference for 7-chloro-L-tryptophan over L-tryptophan [1].

Links to other databases:

References:

1.	Nishizawa, T., Aldrich, C.C. and Sherman, D.H. Molecular analysis of the rebeccamycin L-amino acid oxidase from Lechevalieria aerocolonigenes ATCC 39243. J. Bacteriol. 187 (2005) 2084–2092. [DOI] [PMID: 15743957]
2.	Howard-Jones, A.R. and Walsh, C.T. Enzymatic generation of the chromopyrrolic acid scaffold of rebeccamycin by the tandem action of RebO and RebD. Biochemistry 44 (2005) 15652–15663. [DOI] [PMID: 16313168]

[EC 1.4.3.23 created 2010]

1.4 Acting on the CH-NH₂ group of donors

1.4.5 With a quinone or other compound as acceptor

1.4.5.1

Accepted name:

D-amino acid dehydrogenase (quinone)

Reaction:

a D-amino acid + H₂O + a quinone = a 2-oxo carboxylate + NH₃ + a quinol

Other name(s):

DadA

Systematic name:

D-amino acid:quinone oxidoreductase (deaminating)

Comments:

An iron-sulfur flavoprotein (FAD). The enzyme from the bacterium Helicobacter pylori is highly specific for D-proline, while the enzyme from the bacterium Escherichia coli B is most active with D-alanine, D-phenylalanine and D-methionine. This enzyme may be the same as EC 1.4.99.6.

Links to other databases:

References:

1.	Olsiewski, P.J., Kaczorowski, G.J. and Walsh, C. Purification and properties of D-amino acid dehydrogenase, an inducible membrane-bound iron-sulfur flavoenzyme from Escherichia coli B. J. Biol. Chem. 255 (1980) 4487–4494. [PMID: 6102989]
2.	Tanigawa, M., Shinohara, T., Saito, M., Nishimura, K., Hasegawa, Y., Wakabayashi, S., Ishizuka, M. and Nagata, Y. D-Amino acid dehydrogenase from Helicobacter pylori NCTC 11637. Amino Acids 38 (2010) 247–255. [DOI] [PMID: 19212808]

[EC 1.4.5.1 created 2010]

1.5.99.13

Accepted name:

D-proline dehydrogenase

Reaction:

D-proline + acceptor = 1-pyrroline-2-carboxylate + reduced acceptor

Other name(s):

D-Pro DH; D-Pro dehydrogenase; dye-linked D-proline dehydrogenase

Systematic name:

D-proline:acceptor oxidoreductase

Comments:

A flavoprotein (FAD). The enzyme prefers D-proline and acts on other D-amino acids with lower efficiency.

Links to other databases:

References:

1.	Tani, Y., Tanaka, K., Yabutani, T., Mishima, Y., Sakuraba, H., Ohshima, T. and Motonaka, J. Development of a D-amino acids electrochemical sensor based on immobilization of thermostable D-proline dehydrogenase within agar gel membrane. Anal. Chim. Acta 619 (2008) 215–220. [DOI] [PMID: 18558115]
2.	Satomura, T., Kawakami, R., Sakuraba, H. and Ohshima, T. Dye-linked D-proline dehydrogenase from hyperthermophilic archaeon Pyrobaculum islandicum is a novel FAD-dependent amino acid dehydrogenase. J. Biol. Chem. 277 (2002) 12861–12867. [DOI] [PMID: 11823469]

[EC 1.5.99.13 created 2010, modified 2011]

*EC

1.7.3.3

Accepted name:

factor-independent urate hydroxylase

Reaction:

urate + O₂ + H₂O = 5-hydroxyisourate + H₂O₂

For diagram of AMP catabolism, click here

Other name(s):

uric acid oxidase; uricase; uricase II; urate oxidase

Systematic name:

urate:oxygen oxidoreductase

Comments:

This enzyme was previously thought to be a copper protein, but it is now known that the enzymes from soy bean (Glycine max), the mould Aspergillus flavus and Bacillus subtilis contains no copper nor any other transition-metal ion. The 5-hydroxyisourate formed decomposes spontaneously to form allantoin and CO₂, although there is an enzyme-catalysed pathway in which EC 3.5.2.17, hydroxyisourate hydrolase, catalyses the first step. The enzyme is different from EC 1.14.13.113 (FAD-dependent urate hydroxylase).

Links to other databases:

BRENDA, EAWAG-BBD, EXPASY, Gene, KEGG, PDB, CAS registry number: 9002-12-4

References:

1.	London, M. and Hudson, P.B. Purification and properties of solubilized uricase. Biochim. Biophys. Acta 21 (1956) 290–298. [DOI] [PMID: 13363909]
2.	Mahler, H.R., Hübscher, G. and Baum, H. Studies on uricase. I. Preparation, purification, and properties of a cuproprotein. J. Biol. Chem. 216 (1955) 625–641. [PMID: 13271340]
3.	Robbins, K.C., Barnett, E.L. and Grant, N.H. Partial purification of porcine liver uricase. J. Biol. Chem. 216 (1955) 27–35. [PMID: 13252004]
4.	Kahn, K. and Tipton, P.A. Spectroscopic characterization of intermediates in the urate oxidase reaction. Biochemistry 37 (1998) 11651–11659. [DOI] [PMID: 9709003]
5.	Colloc'h, N., el Hajji, M., Bachet, B., L'Hermite, G., Schiltz, M., Prange, T., Castro, B. and Mornon, J.-P. Crystal structure of the protein drug urate oxidase-inhibitor complex at 2.05 Å resolution. Nat. Struct. Biol. 4 (1997) 947–952. [PMID: 9360612]
6.	Imhoff, R.D., Power, N.P., Borrok, M.J. and Tipton, P.A. General base catalysis in the urate oxidase reaction: evidence for a novel Thr-Lys catalytic diad. Biochemistry 42 (2003) 4094–4100. [DOI] [PMID: 12680763]

[EC 1.7.3.3 created 1961, modified 2002, modified 2005, modified 2010]

1.7 Acting on other nitrogenous compounds as donors

1.7.5 With a quinone or similar compound as acceptor

1.7.5.1

Accepted name:

nitrate reductase (quinone)

Reaction:

nitrate + a quinol = nitrite + a quinone + H₂O

Other name(s):

nitrate reductase A; nitrate reductase Z; quinol/nitrate oxidoreductase; quinol-nitrate oxidoreductase; quinol:nitrate oxidoreductase; NarA; NarZ; NarGHI; dissimilatory nitrate reductase

Systematic name:

nitrite:quinone oxidoreductase

Comments:

A membrane-bound enzyme which supports anaerobic respiration on nitrate under anaerobic conditions and in the presence of nitrate. Contains the bicyclic form of the molybdo-bis(molybdopterin guanine dinucleotide) cofactor, iron-sulfur clusters and heme b. Escherichia coli expresses two forms NarA and NarZ, both being comprised of three subunits.

Links to other databases:

References:

1.	Enoch, H.G. and Lester, R.L. The role of a novel cytochrome b-containing nitrate reductase and quinone in the in vitro reconstruction of formate-nitrate reductase activity of E. coli. Biochem. Biophys. Res. Commun. 61 (1974) 1234–1241. [DOI] [PMID: 4616697]
2.	Bertero, M.G., Rothery, R.A., Palak, M., Hou, C., Lim, D., Blasco, F., Weiner, J.H. and Strynadka, N.C. Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A. Nat. Struct. Biol. 10 (2003) 681–687. [DOI] [PMID: 12910261]
3.	Lanciano, P., Magalon, A., Bertrand, P., Guigliarelli, B. and Grimaldi, S. High-stability semiquinone intermediate in nitrate reductase A (NarGHI) from Escherichia coli is located in a quinol oxidation site close to heme b_D. Biochemistry 46 (2007) 5323–5329. [DOI] [PMID: 17439244]
4.	Bertero, M.G., Rothery, R.A., Boroumand, N., Palak, M., Blasco, F., Ginet, N., Weiner, J.H. and Strynadka, N.C. Structural and biochemical characterization of a quinol binding site of Escherichia coli nitrate reductase A. J. Biol. Chem. 280 (2005) 14836–14843. [DOI] [PMID: 15615728]
5.	Bonnefoy, V. and Demoss, J.A. Nitrate reductases in Escherichia coli. Antonie Van Leeuwenhoek 66 (1994) 47–56. [PMID: 7747940]
6.	Guigliarelli, B., Asso, M., More, C., Augier, V., Blasco, F., Pommier, J., Giordano, G. and Bertrand, P. EPR and redox characterization of iron-sulfur centers in nitrate reductases A and Z from Escherichia coli. Evidence for a high-potential and a low-potential class and their relevance in the electron-transfer mechanism. Eur. J. Biochem. 207 (1992) 61–68. [DOI] [PMID: 1321049]
7.	Iobbi-Nivol, C., Santini, C.L., Blasco, F. and Giordano, G. Purification and further characterization of the second nitrate reductase of Escherichia coli K12. Eur. J. Biochem. 188 (1990) 679–687. [DOI] [PMID: 2139607]

[EC 1.7.5.1 created 2010]

*EC

1.7.99.8

Transferred entry:

hydrazine oxidoreductase. Now classified as EC 1.7.2.8, hydrazine dehydrogenase.

[EC 1.7.99.8 created 2003, modified 2010, deleted 2016]

1.8.1.16

Accepted name:

glutathione amide reductase

Reaction:

2 glutathione amide + NAD⁺ = glutathione amide disulfide + NADH + H⁺

Other name(s):

GAR

Systematic name:

glutathione amide:NAD⁺ oxidoreductase

Comments:

A dimeric flavoprotein (FAD). The enzyme restores glutathione amide disulfide, which is produced during the reduction of peroxide by EC 1.11.1.17 (glutathione amide-dependent peroxidase), back to glutathione amide (it catalyses the reaction in the opposite direction to that shown). The enzyme belongs to the family of flavoprotein disulfide oxidoreductases, but unlike other members of the family, which are specific for NADPH, it prefers NADH [1].

Links to other databases:

References:

1.	Vergauwen, B., Pauwels, F., Jacquemotte, F., Meyer, T.E., Cusanovich, M.A., Bartsch, R.G. and Van Beeumen, J.J. Characterization of glutathione amide reductase from Chromatium gracile. Identification of a novel thiol peroxidase (Prx/Grx) fueled by glutathione amide redox cycling. J. Biol. Chem. 276 (2001) 20890–20897. [DOI] [PMID: 11399772]
2.	Vergauwen, B., Van Petegem, F., Remaut, H., Pauwels, F. and Van Beeumen, J.J. Crystallization and preliminary X-ray crystallographic analysis of glutathione amide reductase from Chromatium gracile. Acta Crystallogr. D Biol. Crystallogr. 58 (2002) 339–340. [PMID: 11807270]

[EC 1.8.1.16 created 2010]

1.11.1.17

Accepted name:

glutathione amide-dependent peroxidase

Reaction:

2 glutathione amide + H₂O₂ = glutathione amide disulfide + 2 H₂O

Systematic name:

glutathione amide:hydrogen-peroxide oxidoreductase

Comments:

This enzyme, which has been characterized from the proteobacterium Marichromatium gracile, is a chimeric protein, containing a peroxiredoxin-like N-terminus and a glutaredoxin-like C terminus. The enzyme has peroxidase activity towards hydrogen peroxide and several small alkyl hydroperoxides, and is thought to represent an early adaptation for fighting oxidative stress [1]. The glutathione amide disulfide produced by this enzyme can be restored to glutathione amide by EC 1.8.1.16 (glutathione amide reductase).

Links to other databases:

References:

Vergauwen, B., Pauwels, F., Jacquemotte, F., Meyer, T.E., Cusanovich, M.A., Bartsch, R.G. and Van Beeumen, J.J. Characterization of glutathione amide reductase from Chromatium gracile. Identification of a novel thiol peroxidase (Prx/Grx) fueled by glutathione amide redox cycling. J. Biol. Chem. 276 (2001) 20890–20897. [DOI] [PMID: 11399772]

[EC 1.11.1.17 created 2010]

1.13.11.56

Accepted name:

1,2-dihydroxynaphthalene dioxygenase

Reaction:

naphthalene-1,2-diol + O₂ = 2-hydroxy-2H-chromene-2-carboxylate

For diagram of naphthalene metabolism, click here

Other name(s):

1,2-DHN dioxygenase; DHNDO; 1,2-dihydroxynaphthalene oxygenase; 1,2-dihydroxynaphthalene:oxygen oxidoreductase

Systematic name:

naphthalene-1,2-diol:oxygen oxidoreductase

Comments:

This enzyme is involved in naphthalene degradation. Requires Fe²⁺.

Links to other databases:

BRENDA, EAWAG-BBD, EXPASY, Gene, KEGG, PDB

References:

1.	Kuhm, A.E., Stolz, A., Ngai, K.L. and Knackmuss, H.J. Purification and characterization of a 1,2-dihydroxynaphthalene dioxygenase from a bacterium that degrades naphthalenesulfonic acids. J. Bacteriol. 173 (1991) 3795–3802. [DOI] [PMID: 2050635]
2.	Keck, A., Conradt, D., Mahler, A., Stolz, A., Mattes, R. and Klein, J. Identification and functional analysis of the genes for naphthalenesulfonate catabolism by Sphingomonas xenophaga BN6. Microbiology 152 (2006) 1929–1940. [DOI] [PMID: 16804169]
3.	Patel, T.R. and Barnsley, E.A. Naphthalene metabolism by pseudomonads: purification and properties of 1,2-dihydroxynaphthalene oxygenase. J. Bacteriol. 143 (1980) 668–673. [PMID: 7204331]

[EC 1.13.11.56 created 2010, modified 2010]

1.13.12.17

Accepted name:

dichloroarcyriaflavin A synthase

Reaction:

dichlorochromopyrrolate + 4 O₂ + 4 NADH + 4 H⁺ = dichloroarcyriaflavin A + 2 CO₂ + 6 H₂O + 4 NAD⁺

For diagram of rebeccamycin biosynthesis, click here

Glossary:

dichloro-arcyriaflavin A = rebeccamycin aglycone

Systematic name:

dichlorochromopyrrolate,NADH:oxygen 2,5-oxidoreductase (dichloroarcyriaflavin A-forming)

Comments:

The conversion of dichlorochromopyrrolate to dichloroarcyriaflavin A is a complex process that involves two enzyme components. RebP is an NAD-dependent cytochrome P-450 oxygenase that performs an aryl-aryl bond formation yielding the six-ring indolocarbazole scaffold [1]. Along with RebC, a flavin-dependent hydroxylase, it also catalyses the oxidative decarboxylation of both carboxyl groups. The presence of RebC ensures that the only product is the rebeccamycin aglycone dichloroarcyriaflavin A [2]. The enzymes are similar, but not identical, to StaP and StaC, which are involved in the synthesis of staurosporine [3].

Links to other databases:

References:

1.	Makino, M., Sugimoto, H., Shiro, Y., Asamizu, S., Onaka, H. and Nagano, S. Crystal structures and catalytic mechanism of cytochrome P₄₅₀ StaP that produces the indolocarbazole skeleton. Proc. Natl. Acad. Sci. USA 104 (2007) 11591–11596. [DOI] [PMID: 17606921]
2.	Howard-Jones, A.R. and Walsh, C.T. Staurosporine and rebeccamycin aglycones are assembled by the oxidative action of StaP, StaC, and RebC on chromopyrrolic acid. J. Am. Chem. Soc. 128 (2006) 12289–12298. [DOI] [PMID: 16967980]
3.	Sanchez, C., Zhu, L., Brana, A.F., Salas, A.P., Rohr, J., Mendez, C. and Salas, J.A. Combinatorial biosynthesis of antitumor indolocarbazole compounds. Proc. Natl. Acad. Sci. USA 102:461 (2005). [DOI] [PMID: 15625109]

[EC 1.13.12.17 created 2010]

1.14.12.21

Transferred entry:

benzoyl-CoA 2,3-dioxygenase. Now EC 1.14.13.208, benzoyl-CoA 2,3-epoxidase

[EC 1.14.12.21 created 2010, deleted 2015]

1.14.13.111

Accepted name:

methanesulfonate monooxygenase (NADH)

Reaction:

methanesulfonate + NADH + H⁺ + O₂ = formaldehyde + NAD⁺ + sulfite + H₂O

Glossary:

methanesulfonate = CH₃-SO₃^-
formaldehyde = H-CHO

Other name(s):

mesylate monooxygenase; mesylate,reduced-FMN:oxygen oxidoreductase; MsmABC; methanesulfonic acid monooxygenase; MSA monooxygenase; MSAMO

Systematic name:

methanesulfonate,NADH:oxygen oxidoreductase

Comments:

A flavoprotein. Methanesulfonate is the simplest of the sulfonates and is a substrate for the growth of certain methylotrophic microorganisms. Compared with EC 1.14.14.5, alkanesulfonate monooxygenase, this enzyme has a restricted substrate range that includes only the short-chain aliphatic sulfonates (methanesulfonate to butanesulfonate) and excludes all larger molecules, such as arylsulfonates [1]. The enzyme from the bacterium Methylosulfonomonas methylovora is a multicomponent system comprising a hydroxylase, a reductase (MsmD) and a ferredoxin (MsmC). The hydroxylase has both large (MsmA) and small (MsmB) subunits, with each large subunit containing a Rieske-type [2Fe-2S] cluster. cf. EC 1.14.14.34, methanesulfonate monooxygenase (FMNH₂).

Links to other databases:

BRENDA, EAWAG-BBD, EXPASY, KEGG, PDB

References:

1.	de Marco, P., Moradas-Ferreira, P., Higgins, T.P., McDonald, I., Kenna, E.M. and Murrell, J.C. Molecular analysis of a novel methanesulfonic acid monooxygenase from the methylotroph Methylosulfonomonas methylovora. J. Bacteriol. 181 (1999) 2244–2251. [PMID: 10094704]
2.	Higgins, T.P., Davey, M., Trickett, J., Kelly, D.P. and Murrell, J.C. Metabolism of methanesulfonic acid involves a multicomponent monooxygenase enzyme. Microbiology 142 (1996) 251–260. [DOI] [PMID: 8932698]

[EC 1.14.13.111 created 2009 as EC 1.14.14.6, transferred 2010 to EC 1.14.13.111, modified 2016]

1.14.13.112

Transferred entry:

3-epi-6-deoxocathasterone 23-monooxygenase. Now EC 1.14.14.147, 3-epi-6-deoxocathasterone 23-monooxygenase

[EC 1.14.13.112 created 2010, deleted 2018]

1.14.13.113

Accepted name:

FAD-dependent urate hydroxylase

Reaction:

urate + NADH + H⁺ + O₂ = 5-hydroxyisourate + NAD⁺ + H₂O

Other name(s):

HpxO enzyme; FAD-dependent urate oxidase; urate hydroxylase

Systematic name:

urate,NADH:oxygen oxidoreductase (5-hydroxyisourate-forming)

Comments:

A flavoprotein. The reaction is part of the purine catabolic pathway in the bacterium Klebsiella pneumoniae. The enzyme is different from EC 1.7.3.3, factor-independent urate hydroxylase, found in most plants, which produces hydrogen peroxide. The product of the enzyme is a substrate for EC 3.5.2.17, hydroxyisourate hydrolase.

Links to other databases:

References:

1.	O'Leary, S.E., Hicks, K.A., Ealick, S.E. and Begley, T.P. Biochemical characterization of the HpxO enzyme from Klebsiella pneumoniae, a novel FAD-dependent urate oxidase. Biochemistry 48 (2009) 3033–3035. [DOI] [PMID: 19260710]

[EC 1.14.13.113 created 2010]

1.14.14.6

Transferred entry:

methanesulfonate monooxygenase. Now EC 1.14.13.111, methanesulfonate monooxygenase. Formerly thought to involve FMNH₂ but now shown to use NADH.

[EC 1.14.14.6 created 2009, deleted 2010]

1.14.15.8

Accepted name:

steroid 15β-monooxygenase

Reaction:

progesterone + 2 reduced [2Fe-2S] ferredoxin + O₂ = 15β-hydroxyprogesterone + 2 oxidized [2Fe-2S] ferredoxin + H₂O

Other name(s):

cytochrome P-450_meg; cytochrome P450_meg; steroid 15β-hydroxylase; CYP106A2; BmCYP106A2

Systematic name:

progesterone,reduced-ferredoxin:oxygen oxidoreductase (15β-hydroxylating)

Comments:

The enzyme from the bacterium Bacillus megaterium hydroxylates a variety of 3-oxo-Δ⁴-steroids in position 15β. Ring A-reduced, aromatic, and 3β-hydroxy-Δ⁴-steroids do not serve as substrates [2].

Links to other databases:

References:

1.	Berg, A., Ingelman-Sundberg, M. and Gustafsson, J.A. Purification and characterization of cytochrome P-450meg. J. Biol. Chem. 254 (1979) 5264–5271. [PMID: 109432]
2.	Berg, A., Gustafsson, J.A. and Ingelman-Sundberg, M. Characterization of a cytochrome P-450-dependent steroid hydroxylase system present in Bacillus megaterium. J. Biol. Chem. 251 (1976) 2831–2838. [PMID: 177422]
3.	Lisurek, M., Kang, M.J., Hartmann, R.W. and Bernhardt, R. Identification of monohydroxy progesterones produced by CYP106A2 using comparative HPLC and electrospray ionisation collision-induced dissociation mass spectrometry. Biochem. Biophys. Res. Commun. 319 (2004) 677–682. [DOI] [PMID: 15178459]
4.	Goni, G., Zollner, A., Lisurek, M., Velazquez-Campoy, A., Pinto, S., Gomez-Moreno, C., Hannemann, F., Bernhardt, R. and Medina, M. Cyanobacterial electron carrier proteins as electron donors to CYP106A2 from Bacillus megaterium ATCC 13368. Biochim. Biophys. Acta 1794 (2009) 1635–1642. [DOI] [PMID: 19635596]
5.	Lisurek, M., Simgen, B., Antes, I. and Bernhardt, R. Theoretical and experimental evaluation of a CYP106A2 low homology model and production of mutants with changed activity and selectivity of hydroxylation. ChemBioChem 9 (2008) 1439–1449. [DOI] [PMID: 18481342]

[EC 1.14.15.8 created 2010]

1.14.99.39

Accepted name:

ammonia monooxygenase

Reaction:

NH₃ + a reduced acceptor + O₂ = NH₂OH + an acceptor + H₂O

Other name(s):

AMO

Systematic name:

ammonia,donor:oxygen oxidoreductase (hydroxylamine-producing)

Comments:

The enzyme catalyses the first reaction in the pathway of ammonia oxidation to nitrite. It contains copper [1], iron [5] and possibly zinc [9]. The enzyme requires two electrons, which are derived indirectly from the quinone pool via a membrane-bound donor.

Links to other databases:

BRENDA, EAWAG-BBD, EXPASY, Gene, KEGG

References:

1.	Ensign, S.A., Hyman, M.R. and Arp, D.J. In vitro activation of ammonia monooxygenase from Nitrosomonas europaea by copper. J. Bacteriol. 175 (1993) 1971–1980. [DOI] [PMID: 8458839]
2.	Hyman, M.R., Page, C.L. and Arp, D.J. Oxidation of methyl fluoride and dimethyl ether by ammonia monooxygenase in Nitrosomonas europaea. Appl. Environ. Microbiol. 60 (1994) 3033–3035. [PMID: 8085841]
3.	Bergmann, D.J. and Hooper, A.B. Sequence of the gene, amoB, for the 43-kDa polypeptide of ammonia monoxygenase of Nitrosomonas europaea. Biochem. Biophys. Res. Commun. 204 (1994) 759–762. [DOI] [PMID: 7980540]
4.	Holmes, A.J., Costello, A., Lidstrom, M.E. and Murrell, J.C. Evidence that particulate methane monooxygenase and ammonia monooxygenase may be evolutionarily related. FEMS Microbiol. Lett. 132 (1995) 203–208. [DOI] [PMID: 7590173]
5.	Zahn, J.A., Arciero, D.M., Hooper, A.B. and DiSpirito, A.A. Evidence for an iron center in the ammonia monooxygenase from Nitrosomonas europaea. FEBS Lett. 397 (1996) 35–38. [DOI] [PMID: 8941709]
6.	Moir, J.W., Crossman, L.C., Spiro, S. and Richardson, D.J. The purification of ammonia monooxygenase from Paracoccus denitrificans. FEBS Lett. 387 (1996) 71–74. [DOI] [PMID: 8654570]
7.	Whittaker, M., Bergmann, D., Arciero, D. and Hooper, A.B. Electron transfer during the oxidation of ammonia by the chemolithotrophic bacterium Nitrosomonas europaea. Biochim. Biophys. Acta 1459 (2000) 346–355. [DOI] [PMID: 11004450]
8.	Arp, D.J., Sayavedra-Soto, L.A. and Hommes, N.G. Molecular biology and biochemistry of ammonia oxidation by Nitrosomonas europaea. Arch. Microbiol. 178 (2002) 250–255. [DOI] [PMID: 12209257]
9.	Gilch, S., Meyer, O. and Schmidt, I. A soluble form of ammonia monooxygenase in Nitrosomonas europaea. Biol. Chem. 390 (2009) 863–873. [DOI] [PMID: 19453274]

[EC 1.14.99.39 created 2010]

1.14.99.40

Transferred entry:

5,6-dimethylbenzimidazole synthase. Now EC 1.13.11.79, 5,6-dimethylbenzimidazole synthase

[EC 1.14.99.40 created 2010, deleted 2014]

1.20.4.3

Accepted name:

mycoredoxin

Reaction:

arseno-mycothiol + mycoredoxin = arsenite + mycothiol-mycoredoxin disulfide

Glossary:

mycothiol = 1-O-[2-(N²-acetyl-L-cysteinamido)-2-deoxy-α-D-glucopyranosyl]-1D-myo-inositol

Other name(s):

Mrx1; MrxI

Systematic name:

arseno-mycothiol:mycoredoxin oxidoreductase

Comments:

Reduction of arsenate is part of a defense mechanism of the cell against toxic arsenate. The substrate arseno-mycothiol is formed by EC 2.8.4.2 (arsenate:mycothiol transferase). A second mycothiol recycles mycoredoxin and forms mycothione.

Links to other databases:

References:

1.	Ordonez, E., Van Belle, K., Roos, G., De Galan, S., Letek, M., Gil, J.A., Wyns, L., Mateos, L.M. and Messens, J. Arsenate reductase, mycothiol, and mycoredoxin concert thiol/disulfide exchange. J. Biol. Chem. 284 (2009) 15107–15116. [DOI] [PMID: 19286650]

[EC 1.20.4.3 created 2010]

1.22 Acting on halogen in donors

1.22.1 With NAD⁺ or NADP⁺ as acceptor

1.22.1.1

Transferred entry:

iodotyrosine deiodinase. Now EC 1.21.1.1, iodotyrosine deiodinase

[EC 1.22.1.1 created 2010, deleted 2015]

*EC

2.1.1.10

Accepted name:

homocysteine S-methyltransferase

Reaction:

S-methyl-L-methionine + L-homocysteine = 2 L-methionine

Other name(s):

S-adenosylmethionine homocysteine transmethylase; S-methylmethionine homocysteine transmethylase; adenosylmethionine transmethylase; methylmethionine:homocysteine methyltransferase; adenosylmethionine:homocysteine methyltransferase; homocysteine methylase; homocysteine methyltransferase; homocysteine transmethylase; L-homocysteine S-methyltransferase; S-adenosyl-L-methionine:L-homocysteine methyltransferase; S-adenosylmethionine-homocysteine transmethylase; S-adenosylmethionine:homocysteine methyltransferase

Systematic name:

S-methyl-L-methionine:L-homocysteine S-methyltransferase

Comments:

The enzyme uses S-adenosyl-L-methionine as methyl donor less actively than S-methyl-L-methionine.

Links to other databases:

BRENDA, EXPASY, Gene, GTD, KEGG, PDB, CAS registry number: 9012-40-2

References:

1.	Balish, E. and Shapiro, S.K. Methionine biosynthesis in Escherichia coli: induction and repression of methylmethionine (or adenosylmethionine):homocysteine methyltransferase. Arch. Biochem. Biophys. 119 (1967) 62–68. [DOI] [PMID: 4861151]
2.	Shapiro, S.K. Adenosylmethionine-homocysteine transmethylase. Biochim. Biophys. Acta 29 (1958) 405–409. [DOI] [PMID: 13572358]
3.	Shapiro, S.K. and Yphantis, D.A. Assay of S-methylmethionine and S-adenosylmethionine homocysteine transmethylases. Biochim. Biophys. Acta 36 (1959) 241–244. [DOI] [PMID: 14445542]
4.	Mudd, S.H. and Datko, A.H. The S-Methylmethionine Cycle in Lemna paucicostata. Plant Physiol. 93 (1990) 623–630. [PMID: 16667513]
5.	Ranocha, P., McNeil, S.D., Ziemak, M.J., Li, C., Tarczynski, M.C. and Hanson, A.D. The S-methylmethionine cycle in angiosperms: ubiquity, antiquity and activity. Plant J. 25 (2001) 575–584. [DOI] [PMID: 11309147]
6.	Ranocha, P., Bourgis, F., Ziemak, M.J., Rhodes, D., Gage, D.A. and Hanson, A.D. Characterization and functional expression of cDNAs encoding methionine-sensitive and -insensitive homocysteine S-methyltransferases from Arabidopsis. J. Biol. Chem. 275 (2000) 15962–15968. [DOI] [PMID: 10747987]
7.	Grue-Sørensen, G., Kelstrup, E., Kjær, A. and Madsen, J.Ø. Diastereospecific, enzymically catalysed transmethylation from S-methyl-L-methionine to L-homocysteine, a naturally occurring process. J. Chem. Soc. Perkin Trans. 1 (1984) 1091–1097.

[EC 2.1.1.10 created 1965, modified 2010]

2.1.1.164

Accepted name:

demethylrebeccamycin-D-glucose O-methyltransferase

Reaction:

4′-demethylrebeccamycin + S-adenosyl-L-methionine = rebeccamycin + S-adenosyl-L-homocysteine

For diagram of rebeccamycin biosynthesis, click here

Other name(s):

RebM

Systematic name:

S-adenosyl-L-methionine:demethylrebeccamycin-D-glucose O-methyltransferase

Comments:

Catalyses the last step in the biosynthesis of rebeccamycin, an indolocarbazole alkaloid produced by the bacterium Lechevalieria aerocolonigenes. The enzyme is able to use a wide variety substrates, tolerating variation on the imide heterocycle, deoxygenation of the sugar moiety, and even indolocarbazole glycoside anomers [1]. The enzyme is a member of the general acid/base-dependent O-methyltransferase family [2].

Links to other databases:

References:

1.	Zhang, C., Albermann, C., Fu, X., Peters, N.R., Chisholm, J.D., Zhang, G., Gilbert, E.J., Wang, P.G., Van Vranken, D.L. and Thorson, J.S. RebG- and RebM-catalyzed indolocarbazole diversification. ChemBioChem 7 (2006) 795–804. [DOI] [PMID: 16575939]
2.	Singh, S., McCoy, J.G., Zhang, C., Bingman, C.A., Phillips, G.N., Jr. and Thorson, J.S. Structure and mechanism of the rebeccamycin sugar 4′-O-methyltransferase RebM. J. Biol. Chem. 283 (2008) 22628–22636. [DOI] [PMID: 18502766]

[EC 2.1.1.164 created 2010]

2.1.1.165

Accepted name:

methyl halide transferase

Reaction:

S-adenosyl-L-methionine + iodide = S-adenosyl-L-homocysteine + methyl iodide

Other name(s):

MCT; methyl chloride transferase; S-adenosyl-L-methionine:halide/bisulfide methyltransferase; AtHOL1; AtHOL2; AtHOL3; HARMLESS TO OZONE LAYER protein; HMT; S-adenosyl-L-methionine: halide ion methyltransferase; SAM:halide ion methyltransferase

Systematic name:

S-adenosylmethionine:iodide methyltransferase

Comments:

This enzyme contributes to the methyl halide emissions from Arabidopsis [6].

Links to other databases:

References:

1.	Ni, X. and Hager, L.P. Expression of Batis maritima methyl chloride transferase in Escherichia coli. Proc. Natl. Acad. Sci. USA 96 (1999) 3611–3615. [DOI] [PMID: 10097085]
2.	Saxena, D., Aouad, S., Attieh, J. and Saini, H.S. Biochemical characterization of chloromethane emission from the wood-rotting fungus Phellinus pomaceus. Appl. Environ. Microbiol. 64 (1998) 2831–2835. [PMID: 9687437]
3.	Attieh, J.M., Hanson, A.D. and Saini, H.S. Purification and characterization of a novel methyltransferase responsible for biosynthesis of halomethanes and methanethiol in Brassica oleracea. J. Biol. Chem. 270 (1995) 9250–9257. [DOI] [PMID: 7721844]
4.	Itoh, N., Toda, H., Matsuda, M., Negishi, T., Taniguchi, T. and Ohsawa, N. Involvement of S-adenosylmethionine-dependent halide/thiol methyltransferase (HTMT) in methyl halide emissions from agricultural plants: isolation and characterization of an HTMT-coding gene from Raphanus sativus (daikon radish). BMC Plant Biol. 9 (2009) 116. [DOI] [PMID: 19723322]
5.	Ohsawa, N., Tsujita, M., Morikawa, S. and Itoh, N. Purification and characterization of a monohalomethane-producing enzyme S-adenosyl-L-methionine: halide ion methyltransferase from a marine microalga, Pavlova pinguis. Biosci. Biotechnol. Biochem. 65 (2001) 2397–2404. [DOI] [PMID: 11791711]
6.	Nagatoshi, Y.and Nakamura, T. Characterization of three halide methyltransferases in Arabidopsis thaliana. Plant Biotechnol. 24 (2007) 503–506.

[EC 2.1.1.165 created 2010]

2.3.1.189

Accepted name:

mycothiol synthase

Reaction:

desacetylmycothiol + acetyl-CoA = CoA + mycothiol

For diagram of mycothiol biosynthesis, click here

Glossary:

desacetylmycothiol = 1-O-[2-(L-cysteinamido)-2-deoxy-α-D-glucopyranosyl]-1D-myo-inositol
mycothiol = 1-O-[2-(N²-acetyl-L-cysteinamido)-2-deoxy-α-D-glucopyranosyl]-1D-myo-inositol

Other name(s):

MshD

Systematic name:

acetyl-CoA:desacetylmycothiol O-acetyltransferase

Comments:

This enzyme catalyses the last step in the biosynthesis of mycothiol, the major thiol in most actinomycetes, including Mycobacterium [1]. The enzyme is a member of a large family of GCN5-related N-acetyltransferases (GNATs) [2]. The enzyme has been purified from Mycobacterium tuberculosis H37Rv. Acetyl-CoA is the preferred CoA thioester but propionyl-CoA is also a substrate [3].

Links to other databases:

References:

1.	Spies, H.S. and Steenkamp, D.J. Thiols of intracellular pathogens. Identification of ovothiol A in Leishmania donovani and structural analysis of a novel thiol from Mycobacterium bovis. Eur. J. Biochem. 224 (1994) 203–213. [DOI] [PMID: 8076641]
2.	Koledin, T., Newton, G.L. and Fahey, R.C. Identification of the mycothiol synthase gene (mshD) encoding the acetyltransferase producing mycothiol in actinomycetes. Arch. Microbiol. 178 (2002) 331–337. [DOI] [PMID: 12375100]
3.	Vetting, M.W., Roderick, S.L., Yu, M. and Blanchard, J.S. Crystal structure of mycothiol synthase (Rv0819) from Mycobacterium tuberculosis shows structural homology to the GNAT family of N-acetyltransferases. Protein Sci. 12 (2003) 1954–1959. [DOI] [PMID: 12930994]

[EC 2.3.1.189 created 2010]

2.3.1.190

Accepted name:

acetoin dehydrogenase system

Reaction:

acetoin + CoA + NAD⁺ = acetaldehyde + acetyl-CoA + NADH + H⁺

Other name(s):

acetoin dehydrogenase complex; acetoin dehydrogenase enzyme system; AoDH ES; acetoin dehydrogenase

Systematic name:

acetyl-CoA:acetoin O-acetyltransferase

Comments:

Requires thiamine diphosphate. It belongs to the 2-oxoacid dehydrogenase system family, which also includes EC 1.2.1.104, pyruvate dehydrogenase system, EC 1.2.1.105, 2-oxoglutarate dehydrogenase system, EC 1.2.1.25, branched-chain α-keto acid dehydrogenase system, and EC 1.4.1.27, glycine cleavage system. With the exception of the glycine cleavage system, which contains 4 components, the 2-oxoacid dehydrogenase systems share a common structure, consisting of three main components, namely a 2-oxoacid dehydrogenase (E1), a dihydrolipoamide acyltransferase (E2), and dihydrolipoamide dehydrogenase (E3).

Links to other databases:

References:

1.	Priefert, H., Hein, S., Kruger, N., Zeh, K., Schmidt, B. and Steinbuchel, A. Identification and molecular characterization of the Alcaligenes eutrophus H16 aco operon genes involved in acetoin catabolism. J. Bacteriol. 173 (1991) 4056–4071. [DOI] [PMID: 2061286]
2.	Oppermann, F.B. and Steinbuchel, A. Identification and molecular characterization of the aco genes encoding the Pelobacter carbinolicus acetoin dehydrogenase enzyme system. J. Bacteriol. 176 (1994) 469–485. [DOI] [PMID: 8110297]
3.	Kruger, N., Oppermann, F.B., Lorenzl, H. and Steinbuchel, A. Biochemical and molecular characterization of the Clostridium magnum acetoin dehydrogenase enzyme system. J. Bacteriol. 176 (1994) 3614–3630. [DOI] [PMID: 8206840]
4.	Huang, M., Oppermann, F.B. and Steinbuchel, A. Molecular characterization of the Pseudomonas putida 2,3-butanediol catabolic pathway. FEMS Microbiol. Lett. 124 (1994) 141–150. [DOI] [PMID: 7813883]
5.	Huang, M., Oppermann-Sanio, F.B. and Steinbuchel, A. Biochemical and molecular characterization of the Bacillus subtilis acetoin catabolic pathway. J. Bacteriol. 181 (1999) 3837–3841. [DOI] [PMID: 10368162]

[EC 2.3.1.190 created 2010, modified 2020]

2.4.1.250

Accepted name:

D-inositol-3-phosphate glycosyltransferase

Reaction:

UDP-N-acetyl-α-D-glucosamine + 1D-myo-inositol 3-phosphate = 1-O-(2-acetamido-2-deoxy-α-D-glucopyranosyl)-1D-myo-inositol 3-phosphate + UDP

For diagram of mycothiol biosynthesis, click here

Glossary:

mycothiol = 1-O-[2-(N²-acetyl-L-cysteinamido)-2-deoxy-α-D-glucopyranosyl]-1D-myo-inositol

Other name(s):

mycothiol glycosyltransferases; MshA; UDP-N-acetyl-D-glucosamine:1D-myo-inositol 3-phosphate α-D-glycosyltransferase

Systematic name:

UDP-N-acetyl-α-D-glucosamine:1D-myo-inositol 3-phosphate α-D-glycosyltransferase (configuration-retaining)

Comments:

The enzyme, which belongs to the GT-B fold superfamily, catalyses the first dedicated reaction in the biosynthesis of mycothiol [1]. The substrate was initially believed to be inositol, but eventually shown to be D-myo-inositol 3-phosphate [2]. A substantial conformational change occurs upon UDP binding, which generates the binding site for D-myo-inositol 3-phosphate [3].

Links to other databases:

References:

1.	Newton, G.L., Koledin, T., Gorovitz, B., Rawat, M., Fahey, R.C. and Av-Gay, Y. The glycosyltransferase gene encoding the enzyme catalyzing the first step of mycothiol biosynthesis (mshA). J. Bacteriol. 185 (2003) 3476–3479. [DOI] [PMID: 12754249]
2.	Newton, G.L., Ta, P., Bzymek, K.P. and Fahey, R.C. Biochemistry of the initial steps of mycothiol biosynthesis. J. Biol. Chem. 281 (2006) 33910–33920. [DOI] [PMID: 16940050]
3.	Vetting, M.W., Frantom, P.A. and Blanchard, J.S. Structural and enzymatic analysis of MshA from Corynebacterium glutamicum: substrate-assisted catalysis. J. Biol. Chem. 283 (2008) 15834–15844. [DOI] [PMID: 18390549]

[EC 2.4.1.250 created 2010]

2.4.2.42

Accepted name:

UDP-D-xylose:β-D-glucoside α-1,3-D-xylosyltransferase

Reaction:

UDP-α-D-xylose + [protein with EGF-like domain]-3-O-(β-D-glucosyl)-L-serine = UDP + [protein with EGF-like domain]-3-O-[α-D-xylosyl-(1→3)-β-D-glucosyl]-L-serine

Other name(s):

β-glucoside α-1,3-xylosyltransferase; UDP-α-D-xylose:β-D-glucoside 3-α-D-xylosyltransferase; GXYLT1 (gene name); GXYLT2 (gene name)

Systematic name:

UDP-α-D-xylose:[protein with EGF-like domain]-3-O-(β-D-glucosyl)-L-serine 3-α-D-xylosyltransferase (configuration-retaining)

Comments:

The enzyme, found in animals and insects, is involved in the biosynthesis of the α-D-xylosyl-(1→3)-α-D-xylosyl-(1→3)-β-D-glucosyl trisaccharide on epidermal growth factor-like (EGF-like) domains [2,3]. When present on Notch proteins, the trisaccharide functions as a modulator of the signalling activity of this protein.

Links to other databases:

References:

1.	Omichi, K., Aoki, K., Minamida, S. and Hase, S. Presence of UDP-D-xylose: β-D-glucoside α-1,3-D-xylosyltransferase involved in the biosynthesis of the Xyl α 1-3Glc β-Ser structure of glycoproteins in the human hepatoma cell line HepG2. Eur. J. Biochem. 245 (1997) 143–146. [DOI] [PMID: 9128735]
2.	Ishimizu, T., Sano, K., Uchida, T., Teshima, H., Omichi, K., Hojo, H., Nakahara, Y. and Hase, S. Purification and substrate specificity of UDP-D-xylose:β-D-glucoside α-1,3-D-xylosyltransferase involved in the biosynthesis of the Xyl α1-3Xyl α1-3Glc β1-O-Ser on epidermal growth factor-like domains. J. Biochem. 141 (2007) 593–600. [DOI] [PMID: 17317689]
3.	Sethi, M.K., Buettner, F.F., Krylov, V.B., Takeuchi, H., Nifantiev, N.E., Haltiwanger, R.S., Gerardy-Schahn, R. and Bakker, H. Identification of glycosyltransferase 8 family members as xylosyltransferases acting on O-glucosylated notch epidermal growth factor repeats. J. Biol. Chem. 285 (2010) 1582–1586. [PMID: 19940119]

[EC 2.4.2.42 created 2010, modified 2020]

*EC

2.5.1.34

Accepted name:

4-dimethylallyltryptophan synthase

Reaction:

prenyl diphosphate + L-tryptophan = diphosphate + 4-(3-methylbut-2-en-1-yl)-L-tryptophan

For diagram of ergot alkaloid biosynthesis, click here

Glossary:

prenyl diphosphate = dimethylallyl diphosphate

Other name(s):

dimethylallylpyrophosphate:L-tryptophan dimethylallyltransferase; dimethylallyltryptophan synthetase; dimethylallylpyrophosphate:tryptophan dimethylallyl transferase; DMAT synthetase; 4-(γ,gamma-dimethylallyl)tryptophan synthase; tryptophan dimethylallyltransferase; dimethylallyl-diphosphate:L-tryptophan 4-dimethylallyltransferase

Systematic name:

prenyl-diphosphate:L-tryptophan 4-prenyltransferase

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, PDB, CAS registry number: 55127-01-0

References:

1.	Lee, S.L., Floss, H.G. and Heinstein, P. Purification and properties of dimethylallylpyrophosphate:tryptophan dimethylallyl transferase, the first enzyme of ergot alkaloid biosynthesis in Claviceps sp. SD 58. Arch. Biochem. Biophys. 177 (1976) 84–94. [DOI] [PMID: 999297]

[EC 2.5.1.34 created 1984, modified 2010]

2.5.1.77

Transferred entry:

7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase. Now EC 2.5.1.147, 5-amino-6-(D-ribitylamino)uracil—L-tyrosine 4-methylphenol transferase and EC 4.3.1.32, 7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase.

[EC 2.5.1.77 created 2010, deleted 2018]

2.5.1.78

Accepted name:

6,7-dimethyl-8-ribityllumazine synthase

Reaction:

1-deoxy-L-glycero-tetrulose 4-phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(D-ribityl)lumazine + 2 H₂O + phosphate

For diagram of riboflavin biosynthesis (late stages), click here and for mechanism, click here

Glossary:

5-amino-6-(D-ribitylamino)uracil = 5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione
6,7-dimethyl-8-(1-D-ribityl)lumazine = 1-deoxy-1-(6,7-dimethyl-2,4-dioxo-3,4-dihydropteridin-8(2H)-yl)-D-ribitol

Other name(s):

lumazine synthase; 6,7-dimethyl-8-ribityllumazine synthase 2; 6,7-dimethyl-8-ribityllumazine synthase 1; lumazine synthase 2; lumazine synthase 1; type I lumazine synthase; type II lumazine synthase; RIB4; MJ0303; RibH; Pbls; MbtLS; RibH1 protein; RibH2 protein; RibH1; RibH2

Systematic name:

5-amino-6-(D-ribitylamino)uracil butanedionetransferase

Comments:

Involved in riboflavin biosynthesis.

Links to other databases:

References:

1.	Kis, K., Volk, R. and Bacher, A. Biosynthesis of riboflavin. Studies on the reaction mechanism of 6,7-dimethyl-8-ribityllumazine synthase. Biochemistry 34 (1995) 2883–2892. [PMID: 7893702]
2.	Garcia-Ramirez, J.J., Santos, M.A. and Revuelta, J.L. The Saccharomyces cerevisiae RIB4 gene codes for 6,7-dimethyl-8-ribityllumazine synthase involved in riboflavin biosynthesis. Molecular characterization of the gene and purification of the encoded protein. J. Biol. Chem. 270 (1995) 23801–23807. [DOI] [PMID: 7559556]
3.	Bacher, A., Fischer, M., Kis, K., Kugelbrey, K., Mörtl, S., Scheuring, J., Weinkauf, S., Eberhardt, S., Schmidt-Bäse, K., Huber, R., Ritsert, K., Cushman, M., Ladenstein, R. Biosynthesis of riboflavin: structure and mechanism of lumazine synthase. Biochem. Soc. Trans. 24 (1996) 89–94. [PMID: 8674771]
4.	Mörtl, S., Fischer, M., Richter, G., Tack, J., Weinkauf, S. and Bacher, A. Biosynthesis of riboflavin. Lumazine synthase of Escherichia coli. J. Biol. Chem. 271 (1996) 33201–33207. [DOI] [PMID: 8969176]
5.	Bacher, A., Eberhardt, S., Fischer, M., Mortl, S., Kis, K., Kugelbrey, K., Scheuring, J. and Schott, K. Biosynthesis of riboflavin: lumazine synthase and riboflavin synthase. Methods Enzymol. 280 (1997) 389–399. [DOI] [PMID: 9211334]
6.	Goldbaum, F.A., Velikovsky, C.A., Baldi, P.C., Mortl, S., Bacher, A. and Fossati, C.A. The 18-kDa cytoplasmic protein of Brucella species - an antigen useful for diagnosis - is a lumazine synthase. J. Med. Microbiol. 48 (1999) 833–839. [DOI] [PMID: 10482294]
7.	Jordan, D.B., Bacot, K.O., Carlson, T.J., Kessel, M. and Viitanen, P.V. Plant riboflavin biosynthesis. Cloning, chloroplast localization, expression, purification, and partial characterization of spinach lumazine synthase. J. Biol. Chem. 274 (1999) 22114–22121. [DOI] [PMID: 10419541]
8.	Zhang, X., Meining, W., Fischer, M., Bacher, A. and Ladenstein, R. X-ray structure analysis and crystallographic refinement of lumazine synthase from the hyperthermophile Aquifex aeolicus at 1.6 Å resolution: determinants of thermostability revealed from structural comparisons. J. Mol. Biol. 306 (2001) 1099–1114. [DOI] [PMID: 11237620]
9.	Fischer, M., Haase, I., Feicht, R., Richter, G., Gerhardt, S., Changeux, J.P., Huber, R. and Bacher, A. Biosynthesis of riboflavin: 6,7-dimethyl-8-ribityllumazine synthase of Schizosaccharomyces pombe. Eur. J. Biochem. 269 (2002) 519–526. [DOI] [PMID: 11856310]
10.	Cushman, M., Yang, D., Gerhardt, S., Huber, R., Fischer, M., Kis, K. and Bacher, A. Design, synthesis, and evaluation of 6-carboxyalkyl and 6-phosphonoxyalkyl derivatives of 7-oxo-8-ribitylaminolumazines as inhibitors of riboflavin synthase and lumazine synthase. J. Org. Chem. 67 (2002) 5807–5816. [DOI] [PMID: 12153285]
11.	Haase, I., Mortl, S., Kohler, P., Bacher, A. and Fischer, M. Biosynthesis of riboflavin in archaea. 6,7-dimethyl-8-ribityllumazine synthase of Methanococcus jannaschii. Eur. J. Biochem. 270 (2003) 1025–1032. [DOI] [PMID: 12603336]
12.	Morgunova, E., Meining, W., Illarionov, B., Haase, I., Jin, G., Bacher, A., Cushman, M., Fischer, M. and Ladenstein, R. Crystal structure of lumazine synthase from Mycobacterium tuberculosis as a target for rational drug design: binding mode of a new class of purinetrione inhibitors. Biochemistry 44 (2005) 2746–2758. [DOI] [PMID: 15723519]
13.	Morgunova, E., Saller, S., Haase, I., Cushman, M., Bacher, A., Fischer, M. and Ladenstein, R. Lumazine synthase from Candida albicans as an anti-fungal target enzyme: structural and biochemical basis for drug design. J. Biol. Chem. 282 (2007) 17231–17241. [DOI] [PMID: 17446177]

[EC 2.5.1.78 created 2010]

2.5.1.79

Accepted name:

thermospermine synthase

Reaction:

S-adenosyl 3-(methylsulfanyl)propylamine + spermidine = S-methyl-5′-thioadenosine + thermospermine + H⁺

Glossary:

thermospermine = N¹-[3-(3-aminopropylamino)propyl]butane-1,4-diamine
S-adenosyl 3-(methylsulfanyl)propylamine = (3-aminopropyl){[(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl}methylsulfonium

Other name(s):

TSPMS; ACL5; SAC51; S-adenosyl 3-(methylthio)propylamine:spermidine 3-aminopropyltransferase (thermospermine synthesizing)

Systematic name:

S-adenosyl 3-(methylsulfanyl)propylamine:spermidine 3-aminopropyltransferase (thermospermine-forming)

Comments:

This plant enzyme is crucial for the proper functioning of xylem vessel elements in the vascular tissues of plants [3].

Links to other databases:

References:

1.	Romer, P., Faltermeier, A., Mertins, V., Gedrange, T., Mai, R. and Proff, P. Investigations about N-aminopropyl transferases probably involved in biomineralization. J. Physiol. Pharmacol. 59 Suppl 5 (2008) 27–37. [PMID: 19075322]
2.	Knott, J.M., Romer, P. and Sumper, M. Putative spermine synthases from Thalassiosira pseudonana and Arabidopsis thaliana synthesize thermospermine rather than spermine. FEBS Lett. 581 (2007) 3081–3086. [DOI] [PMID: 17560575]
3.	Muniz, L., Minguet, E.G., Singh, S.K., Pesquet, E., Vera-Sirera, F., Moreau-Courtois, C.L., Carbonell, J., Blazquez, M.A. and Tuominen, H. ACAULIS5 controls Arabidopsis xylem specification through the prevention of premature cell death. Development 135 (2008) 2573–2582. [DOI] [PMID: 18599510]

[EC 2.5.1.79 created 2010, modified 2013]

2.5.1.80

Accepted name:

7-dimethylallyltryptophan synthase

Reaction:

prenyl diphosphate + L-tryptophan = diphosphate + 7-prenyl-L-tryptophan

Glossary:

prenyl = 3-methylbut-2-en-1-yl

Other name(s):

7-DMATS; dimethylallyl-diphosphate:L-tryptophan 7-dimethylallyltransferase

Systematic name:

prenyl-diphosphate:L-tryptophan 7-prenyltransferase

Comments:

This enzyme is more flexible towards the aromatic substrate than EC 2.5.1.34 (4-dimethylallyltryptophan synthase), but similar to that enzyme, accepts only prenyl diphosphate as the prenyl donor.

Links to other databases:

References:

1.	Kremer, A. and Li, S.M. Potential of a 7-dimethylallyltryptophan synthase as a tool for production of prenylated indole derivatives. Appl. Microbiol. Biotechnol. 79 (2008) 951–961. [DOI] [PMID: 18481055]
2.	Kremer, A., Westrich, L. and Li, S.M. A 7-dimethylallyltryptophan synthase from Aspergillus fumigatus: overproduction, purification and biochemical characterization. Microbiology 153 (2007) 3409–3416. [DOI] [PMID: 17906140]

[EC 2.5.1.80 created 2010]

2.7.1.165

Accepted name:

glycerate 2-kinase

Reaction:

ATP + D-glycerate = ADP + 2-phospho-D-glycerate

For diagram of the Entner-Doudoroff pathway, click here

Other name(s):

D-glycerate-2-kinase; glycerate kinase (2-phosphoglycerate forming); ATP:(R)-glycerate 2-phosphotransferase

Systematic name:

ATP:D-glycerate 2-phosphotransferase

Comments:

A key enzyme in the nonphosphorylative Entner-Doudoroff pathway in archaea [1,2]. In the bacterium Hyphomicrobium methylovorum GM2 the enzyme is involved in formaldehyde assimilation I (serine pathway) [5]. In Escherichia coli the enzyme is involved in D-glucarate/D-galactarate degradation [6]. The enzyme requires a divalent metal ion [1].

Links to other databases:

References:

1.	Liu, B., Wu, L., Liu, T., Hong, Y., Shen, Y. and Ni, J. A MOFRL family glycerate kinase from the thermophilic crenarchaeon, Sulfolobus tokodaii, with unique enzymatic properties. Biotechnol. Lett. 31 (2009) 1937–1941. [DOI] [PMID: 19690808]
2.	Reher, M., Bott, M. and Schonheit, P. Characterization of glycerate kinase (2-phosphoglycerate forming), a key enzyme of the nonphosphorylative Entner-Doudoroff pathway, from the thermoacidophilic euryarchaeon Picrophilus torridus. FEMS Microbiol. Lett. 259 (2006) 113–119. [DOI] [PMID: 16684110]
3.	Liu, B., Hong, Y., Wu, L., Li, Z., Ni, J., Sheng, D. and Shen, Y. A unique highly thermostable 2-phosphoglycerate forming glycerate kinase from the hyperthermophilic archaeon Pyrococcus horikoshii: gene cloning, expression and characterization. Extremophiles 11 (2007) 733–739. [DOI] [PMID: 17563835]
4.	Noh, M., Jung, J.H. and Lee, S.B. Purification and characterization of glycerate kinase from the thermoacidophilic archaeon Thermoplasma acidophilum: an enzyme belonging to the second glycerate kinase family. Biotechnol. Bioprocess Eng. 11 (2006) 344–350.
5.	Yoshida, T., Fukuta, K., Mitsunaga, T., Yamada, H. and Izumi, Y. Purification and characterization of glycerate kinase from a serine-producing methylotroph, Hyphomicrobium methylovorum GM2. Eur. J. Biochem. 210 (1992) 849–854. [DOI] [PMID: 1336459]
6.	Hubbard, B.K., Koch, M., Palmer, D.R., Babbitt, P.C. and Gerlt, J.A. Evolution of enzymatic activities in the enolase superfamily: characterization of the (D)-glucarate/galactarate catabolic pathway in Escherichia coli. Biochemistry 37 (1998) 14369–14375. [DOI] [PMID: 9772162]

[EC 2.7.1.165 created 2010]

2.7.7.68

Accepted name:

2-phospho-L-lactate guanylyltransferase

Reaction:

(2S)-2-phospholactate + GTP = (2S)-lactyl-2-diphospho-5′-guanosine + diphosphate

For diagram of coenzyme F₄₂₀ biosynthesis, click here

Other name(s):

cofC (gene name) (ambiguous)

Systematic name:

GTP:2-phospho-L-lactate guanylyltransferase

Comments:

This enzyme is involved in the biosynthesis of coenzyme F₄₂₀, a redox-active cofactor, in all methanogenic archaea. cf. EC 2.7.7.105, phosphoenolpyruvate guanylyltransferase and EC 2.7.7.106, 3-phospho-(R)-glycerate guanylyltransferase.

Links to other databases:

References:

1.	Grochowski, L.L., Xu, H. and White, R.H. Identification and characterization of the 2-phospho-L-lactate guanylyltransferase involved in coenzyme F₄₂₀ biosynthesis. Biochemistry 47 (2008) 3033–3037. [DOI] [PMID: 18260642]
2.	Braga, D., Last, D., Hasan, M., Guo, H., Leichnitz, D., Uzum, Z., Richter, I., Schalk, F., Beemelmanns, C., Hertweck, C. and Lackner, G. Metabolic pathway rerouting in Paraburkholderia rhizoxinica evolved long-overlooked derivatives of coenzyme F₄₂₀. ACS Chem. Biol. 14 (2019) 2088–2094. [PMID: 31469543]

[EC 2.7.7.68 created 2010, revised 2019, modified 2020]

2.7.8.28

Accepted name:

2-phospho-L-lactate transferase

Reaction:

(1) (2S)-lactyl-2-diphospho-5′-guanosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin = GMP + factor 420-0
(2) enolpyruvoyl-2-diphospho-5′-guanosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin = GMP + dehydro factor 420-0
(3) 3-[(R)-glyceryl]-diphospho-5′-guanosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin = GMP + 3PG-factor 420-0

For diagram of coenzyme F₄₂₀ biosynthesis, click here

Glossary:

factor 420 = coenzyme F₄₂₀ = N-(N-{O-[5-(8-hydroxy-2,4-dioxo-2,3,4,10-tetrahydropyrimido[4,5-b]quinolin-10-yl)-5-deoxy-L-ribityl-1-phospho]-(S)-lactyl}-γ-L-glutamyl)-L-glutamate
dehydro coenzyme F₄₂₀-0 = 7,8-didemethyl-8-hydroxy-5-deazariboflavin 5′-(1-carboxyvinyl)phosphate
GMP = guanosine 5′-phosphate

Other name(s):

cofD (gene name); fbiA (gene name); LPPG:Fo 2-phospho-L-lactate transferase; LPPG:7,8-didemethyl-8-hydroxy-5-deazariboflavin 2-phospho-L-lactate transferase; lactyl-2-diphospho-(5′)guanosine:Fo 2-phospho-L-lactate transferase

Systematic name:

(2S)-lactyl-2-diphospho-5′-guanosine:7,8-didemethyl-8-hydroxy-5-deazariboflavin 2-phospho-L-lactate transferase

Comments:

This enzyme is involved in the biosynthesis of factor 420, a redox-active cofactor, in methanogenic archaea and certain bacteria. The specific reaction catalysed in vivo is determined by the availability of substrate, which in turn is determined by the enzyme present in the organism - EC 2.7.7.68, 2-phospho-L-lactate guanylyltransferase, EC 2.7.7.105, phosphoenolpyruvate guanylyltransferase, or EC 2.7.7.106, 3-phospho-D-glycerate guanylyltransferase.

Links to other databases:

References:

1.	Graupner, M., Xu, H. and White, R.H. Characterization of the 2-phospho-L-lactate transferase enzyme involved in coenzyme F₄₂₀ biosynthesis in Methanococcus jannaschii. Biochemistry 41 (2002) 3754–3761. [DOI] [PMID: 11888293]
2.	Forouhar, F., Abashidze, M., Xu, H., Grochowski, L.L., Seetharaman, J., Hussain, M., Kuzin, A., Chen, Y., Zhou, W., Xiao, R., Acton, T.B., Montelione, G.T., Galinier, A., White, R.H. and Tong, L. Molecular insights into the biosynthesis of the F₄₂₀ coenzyme. J. Biol. Chem. 283 (2008) 11832–11840. [DOI] [PMID: 18252724]
3.	Braga, D., Last, D., Hasan, M., Guo, H., Leichnitz, D., Uzum, Z., Richter, I., Schalk, F., Beemelmanns, C., Hertweck, C. and Lackner, G. Metabolic pathway rerouting in Paraburkholderia rhizoxinica evolved long-overlooked derivatives of coenzyme F₄₂₀. ACS Chem. Biol. 14 (2019) 2088–2094. [PMID: 31469543]

[EC 2.7.8.28 created 2010, modified 2020]

2.8.4.2

Accepted name:

arsenate-mycothiol transferase

Reaction:

arsenate + mycothiol = arseno-mycothiol + H₂O

Glossary:

mycothiol = 1-O-[2-(N²-acetyl-L-cysteinamido)-2-deoxy^--D-glucopyranosyl]-1D-myo-inositol

Other name(s):

ArsC1; ArsC2; mycothiol:arsenate transferase

Systematic name:

mycothiol:arsenate S-arsenotransferase

Comments:

Reduction of arsenate is part of a defence mechanism of the cell against toxic arsenate. The product arseno-mycothiol is reduced by EC 1.20.4.3 (mycoredoxin) to arsenite and mycothiol-mycoredoxin disulfide. Finally, a second mycothiol recycles mycoredoxin and forms mycothione.

Links to other databases:

References:

1.	Ordonez, E., Van Belle, K., Roos, G., De Galan, S., Letek, M., Gil, J.A., Wyns, L., Mateos, L.M. and Messens, J. Arsenate reductase, mycothiol, and mycoredoxin concert thiol/disulfide exchange. J. Biol. Chem. 284 (2009) 15107–15116. [DOI] [PMID: 19286650]

[EC 2.8.4.2 created 2010]

3.1.1.84

Accepted name:

cocaine esterase

Reaction:

cocaine + H₂O = ecgonine methyl ester + benzoate

Glossary:

ecgonine methyl ester = 2β-carbomethoxy-3β-tropine = methyl (1R,2R,3S,5S)-3-hydroxy-8-methyl-8-azabicyclo[3.2.1]octane-2-carboxylate

Other name(s):

CocE; hCE2; hCE-2; human carboxylesterase 2

Systematic name:

cocaine benzoylhydrolase

Comments:

Rhodococcus sp. strain MB1 and Pseudomonas maltophilia strain MB11L can utilize cocaine as sole source of carbon and energy [2,3].

Links to other databases:

BRENDA, EAWAG-BBD, EXPASY, Gene, KEGG, PDB

References:

1.	Gao, D., Narasimhan, D.L., Macdonald, J., Brim, R., Ko, M.C., Landry, D.W., Woods, J.H., Sunahara, R.K. and Zhan, C.G. Thermostable variants of cocaine esterase for long-time protection against cocaine toxicity. Mol. Pharmacol. 75 (2009) 318–323. [DOI] [PMID: 18987161]
2.	Bresler, M.M., Rosser, S.J., Basran, A. and Bruce, N.C. Gene cloning and nucleotide sequencing and properties of a cocaine esterase from Rhodococcus sp. strain MB1. Appl. Environ. Microbiol. 66 (2000) 904–908. [DOI] [PMID: 10698749]
3.	Britt, A.J., Bruce, N.C. and Lowe, C.R. Identification of a cocaine esterase in a strain of Pseudomonas maltophilia. J. Bacteriol. 174 (1992) 2087–2094. [DOI] [PMID: 1551831]
4.	Larsen, N.A., Turner, J.M., Stevens, J., Rosser, S.J., Basran, A., Lerner, R.A., Bruce, N.C. and Wilson, I.A. Crystal structure of a bacterial cocaine esterase. Nat. Struct. Biol. 9 (2002) 17–21. [DOI] [PMID: 11742345]
5.	Pindel, E.V., Kedishvili, N.Y., Abraham, T.L., Brzezinski, M.R., Zhang, J., Dean, R.A. and Bosron, W.F. Purification and cloning of a broad substrate specificity human liver carboxylesterase that catalyzes the hydrolysis of cocaine and heroin. J. Biol. Chem. 272 (1997) 14769–14775. [DOI] [PMID: 9169443]

[EC 3.1.1.84 created 2010]

3.1.3.80

Accepted name:

2,3-bisphosphoglycerate 3-phosphatase

Reaction:

2,3-bisphospho-D-glycerate + H₂O = 2-phospho-D-glycerate + phosphate

Other name(s):

MIPP1; 2,3-BPG 3-phosphatase

Systematic name:

2,3-bisphospho-D-glycerate 3-phosphohydrolase

Comments:

This reaction is a shortcut in the Rapoport-Luebering shunt. It bypasses the reactions of EC 5.4.2.11/EC 5.4.2.12 [phosphoglycerate mutases (2,3-diphosphoglycerate-dependent and independent)] and directly forms 2-phospho-D-glycerate by removing the 3-phospho-group of 2,3-diphospho-D-glycerate [1]. The MIPP1 protein also catalyses the reaction of EC 3.1.3.62 (multiple inositol-polyphosphate phosphatase).

Links to other databases:

References:

1.	Cho, J., King, J.S., Qian, X., Harwood, A.J. and Shears, S.B. Dephosphorylation of 2,3-bisphosphoglycerate by MIPP expands the regulatory capacity of the Rapoport-Luebering glycolytic shunt. Proc. Natl. Acad. Sci. USA 105 (2008) 5998–6003. [DOI] [PMID: 18413611]

[EC 3.1.3.80 created 2010]

*EC

3.1.13.2

Accepted name:

exoribonuclease H

Reaction:

3′-end directed exonucleolytic cleavage of viral RNA-DNA hybrid

Comments:

This is a secondary reaction to the RNA 5′-end directed cleavage 13-19 nucleotides from the RNA end performed by EC 3.1.26.13 (retroviral ribonuclease H).

Links to other databases:

References:

1.	Schatz, O., Mous, J. and Le Grice, S.F. HIV-1 RT-associated ribonuclease H displays both endonuclease and 3′—5′ exonuclease activity. EMBO J. 9 (1990) 1171–1176. [PMID: 1691093]

[EC 3.1.13.2 created 1978, modified 2010]

*EC

3.1.26.4

Accepted name:

ribonuclease H

Reaction:

Endonucleolytic cleavage to 5′-phosphomonoester

Other name(s):

endoribonuclease H (calf thymus); RNase H; RNA*DNA hybrid ribonucleotidohydrolase; hybrid ribonuclease; hybridase; hybridase (ribonuclease H); ribonuclease H; hybrid nuclease; calf thymus ribonuclease H

Comments:

Acts on RNA-DNA hybrids.

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, PDB, CAS registry number: 9050-76-4

References:

1.	Haberkern, R.C. and Cantoni, G.L. Studies on a calf thymus ribonuclease specific for ribonucleic acid-deoxyribonucleic acid hybrids. Biochemistry 12 (1973) 2389–2395. [PMID: 4709937]
2.	Stavrianopoulos, J.G. and Chargaff, E. Purification and properties of ribonuclease H of calf thymus. Proc. Natl. Acad. Sci. USA 70 (1973) 1959–1963. [DOI] [PMID: 4516197]

[EC 3.1.26.4 created 1978, modified 2010]

3.5.1.102

Accepted name:

2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5′-monophosphate deformylase

Reaction:

2-amino-5-formylamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + H₂O = 2,5-diamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + formate

Other name(s):

ArfB

Systematic name:

2-amino-5-formylamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one amidohydrolase

Comments:

The enzyme catalyses the second step in archaeal riboflavin and 7,8-didemethyl-8-hydroxy-5-deazariboflavin biosynthesis. The first step is catalysed by EC 3.5.4.29 (GTP cyclohydrolase IIa). The bacterial enzyme, EC 3.5.4.25 (GTP cyclohydrolase II) catalyses both reactions.

Links to other databases:

References:

1.	Grochowski, L.L., Xu, H. and White, R.H. An iron(II) dependent formamide hydrolase catalyzes the second step in the archaeal biosynthetic pathway to riboflavin and 7,8-didemethyl-8-hydroxy-5-deazariboflavin. Biochemistry 48 (2009) 4181–4188. [DOI] [PMID: 19309161]

[EC 3.5.1.102 created 2010, modified 2011]

3.5.1.103

Accepted name:

N-acetyl-1-D-myo-inositol-2-amino-2-deoxy-α-D-glucopyranoside deacetylase

Reaction:

1-O-(2-acetamido-2-deoxy-α-D-glucopyranosyl)-1D-myo-inositol + H₂O = 1-O-(2-amino-2-deoxy-α-D-glucopyranosyl)-1D-myo-inositol + acetate

For diagram of mycothiol biosynthesis, click here

Glossary:

mycothiol = 1-O-[2-(N²-acetyl-L-cysteinamido)-2-deoxy-α-D-glucopyranosyl]-1D-myo-inositol

Other name(s):

MshB

Systematic name:

1-(2-acetamido-2-deoxy-α-D-glucopyranosyl)-1D-myo-inositol acetylhydrolase

Comments:

This enzyme is considered the key enzyme and rate limiting step in the mycothiol biosynthesis pathway [1]. In addition to acetylase activity, the enzyme possesses weak activity of EC 3.5.1.115, mycothiol S-conjugate amidase, and shares sequence similarity with that enzyme [2]. The enzyme requires a divalent transition metal ion for activity, believed to be Zn²⁺ [3].

Links to other databases:

References:

1.	Rawat, M., Kovacevic, S., Billman-Jacobe, H. and Av-Gay, Y. Inactivation of mshB, a key gene in the mycothiol biosynthesis pathway in Mycobacterium smegmatis. Microbiology 149 (2003) 1341–1349. [DOI] [PMID: 12724395]
2.	Newton, G.L., Av-Gay, Y. and Fahey, R.C. N-Acetyl-1-D-myo-inosityl-2-amino-2-deoxy-α-D-glucopyranoside deacetylase (MshB) is a key enzyme in mycothiol biosynthesis. J. Bacteriol. 182 (2000) 6958–6963. [DOI] [PMID: 11092856]
3.	Maynes, J.T., Garen, C., Cherney, M.M., Newton, G., Arad, D., Av-Gay, Y., Fahey, R.C. and James, M.N. The crystal structure of 1-D-myo-inosityl 2-acetamido-2-deoxy-α-D-glucopyranoside deacetylase (MshB) from Mycobacterium tuberculosis reveals a zinc hydrolase with a lactate dehydrogenase fold. J. Biol. Chem. 278 (2003) 47166–47170. [DOI] [PMID: 12958317]

[EC 3.5.1.103 created 2010]

4.1.2.44

Accepted name:

2,3-epoxybenzoyl-CoA dihydrolase

Reaction:

2,3-epoxy-2,3-dihydrobenzoyl-CoA + 2 H₂O = (3Z)-6-oxohex-3-enoyl-CoA + formate

For diagram of Benzoyl-CoA catabolism, click here

Glossary:

(3Z)-6-oxohex-3-enoyl-CoA = 3,4-didehydroadipyl-CoA semialdehyde

Other name(s):

2,3-dihydro-2,3-dihydroxybenzoyl-CoA lyase/hydrolase (deformylating); BoxC; dihydrodiol transforming enzyme; benzoyl-CoA oxidation component C; 2,3-dihydro-2,3-dihydroxybenzoyl-CoA 3,4-didehydroadipyl-CoA semialdehyde-lyase (formate-forming); benzoyl-CoA-dihydrodiol lyase (incorrect); 2,3-dihydro-2,3-dihydroxybenzoyl-CoA 3,4-didehydroadipyl-CoA-semialdehyde-lyase (formate-forming)

Systematic name:

2,3-epoxy-2,3-dihydrobenzoyl-CoA (3Z)-6-oxohex-3-enoyl-CoA-lyase (formate-forming)

Comments:

The enzyme is involved in the aerobic benzoyl-CoA catabolic pathway of the bacterium Azoarcus evansii. The enzyme converts 2,3-epoxy-2,3-dihydrobenzoyl-CoA to its oxepin form prior to the ring-opening and the formation of a dialdehyde intermediate.

Links to other databases:

BRENDA, EAWAG-BBD, EXPASY, Gene, KEGG

References:

1.	Gescher, J., Eisenreich, W., Worth, J., Bacher, A. and Fuchs, G. Aerobic benzoyl-CoA catabolic pathway in Azoarcus evansii: studies on the non-oxygenolytic ring cleavage enzyme. Mol. Microbiol. 56 (2005) 1586–1600. [DOI] [PMID: 15916608]
2.	Rather, L.J., Knapp, B., Haehnel, W. and Fuchs, G. Coenzyme A-dependent aerobic metabolism of benzoate via epoxide formation. J. Biol. Chem. 285 (2010) 20615–20624. [DOI] [PMID: 20452977]

[EC 4.1.2.44 created 2010, modified 2015]

4.1.2.45

Accepted name:

trans-o-hydroxybenzylidenepyruvate hydratase-aldolase

Reaction:

(3E)-4-(2-hydroxyphenyl)-2-oxobut-3-enoate + H₂O = salicylaldehyde + pyruvate

For diagram of naphthalene metabolism, click here

Glossary:

(3E)-4-(2-hydroxyphenyl)-2-oxobut-3-enoate = (E)-2′-hydroxybenzylidenepyruvate
salicylaldehyde = 2-hydroxybenzaldehyde

Other name(s):

2′-hydroxybenzalpyruvate aldolase; NsaE; tHBPA hydratase-aldolase

Systematic name:

(3E)-4-(2-hydroxyphenyl)-2-oxobut-3-enoate hydro-lyase

Comments:

This enzyme is involved in naphthalene degradation. The enzyme catalyses a retro-aldol reaction in vitro, and it accepts a broad range of aldehydes and 4-substituted 2-oxobut-3-enoates as substrates [4].

Links to other databases:

References:

1.	Kuhm, A.E., Knackmuss, H.J. and Stolz, A. Purification and properties of 2′-hydroxybenzalpyruvate aldolase from a bacterium that degrades naphthalenesulfonates. J. Biol. Chem. 268 (1993) 9484–9489. [PMID: 8486638]
2.	Keck, A., Conradt, D., Mahler, A., Stolz, A., Mattes, R. and Klein, J. Identification and functional analysis of the genes for naphthalenesulfonate catabolism by Sphingomonas xenophaga BN6. Microbiology 152 (2006) 1929–1940. [DOI] [PMID: 16804169]
3.	Eaton, R.W. Organization and evolution of naphthalene catabolic pathways: sequence of the DNA encoding 2-hydroxychromene-2-carboxylate isomerase and trans-o-hydroxybenzylidenepyruvate hydratase-aldolase from the NAH7 plasmid. J. Bacteriol. 176 (1994) 7757–7762. [DOI] [PMID: 8002605]
4.	Eaton, R.W. trans-o-Hydroxybenzylidenepyruvate hydratase-aldolase as a biocatalyst. Appl. Environ. Microbiol. 66 (2000) 2668–2672. [DOI] [PMID: 10831455]

[EC 4.1.2.45 created 2010, modified 2011]

4.3.1.26

Transferred entry:

chromopyrrolate synthase. Now EC 1.21.3.9, dichlorochromopyrrolate synthase

[EC 4.3.1.26 created 2010, deleted 2013]

4.3.3.5

Accepted name:

4′-demethylrebeccamycin synthase

Reaction:

4′-O-demethylrebeccamycin + H₂O = dichloro-arcyriaflavin A + β-D-glucose

For diagram of rebeccamycin biosynthesis, click here

Glossary:

dichloro-arcyriaflavin A = rebeccamycin aglycone

Other name(s):

arcyriaflavin A N-glycosyltransferase; RebG

Systematic name:

4′-demethylrebeccamycin D-glucose-lyase

Comments:

This enzyme catalyses a step in the biosynthesis of rebeccamycin, an indolocarbazole alkaloid produced by the bacterium Lechevalieria aerocolonigenes. The enzyme is a glycosylase, and acts in the reverse direction to that shown. It has a wide substrate range, and was shown to glycosylate several substrates, including the staurosporine aglycone, EJG-III-108A, J-104303, 6-N-methyl-arcyriaflavin C and indolo-[2,3-a]-carbazole [1,2].

Links to other databases:

References:

1.	Ohuchi, T., Ikeda-Araki, A., Watanabe-Sakamoto, A., Kojiri, K., Nagashima, M., Okanishi, M. and Suda, H. Cloning and expression of a gene encoding N-glycosyltransferase (ngt) from Saccharothrix aerocolonigenes ATCC39243. J. Antibiot. (Tokyo) 53 (2000) 393–403. [PMID: 10866221]
2.	Zhang, C., Albermann, C., Fu, X., Peters, N.R., Chisholm, J.D., Zhang, G., Gilbert, E.J., Wang, P.G., Van Vranken, D.L. and Thorson, J.S. RebG- and RebM-catalyzed indolocarbazole diversification. ChemBioChem 7 (2006) 795–804. [DOI] [PMID: 16575939]

[EC 4.3.3.5 created 2010]

5.99.1.4

Accepted name:

2-hydroxychromene-2-carboxylate isomerase

Reaction:

2-hydroxy-2H-chromene-2-carboxylate = (3E)-4-(2-hydroxyphenyl)-2-oxobut-3-enoate

For diagram of naphthalene metabolism, click here

Other name(s):

HCCA isomerase; 2HC2CA isomerase; 2-hydroxychromene-2-carboxylic acid isomerase

Systematic name:

2-hydroxy-2H-chromene-2-carboxylate—(3E)-4-(2-hydroxyphenyl)-2-oxobut-3-enoate isomerase

Comments:

This enzyme is involved in naphthalene degradation.

Links to other databases:

BRENDA, EAWAG-BBD, EXPASY, Gene, KEGG, PDB

References:

1.	Ohmoto, T., Kinoshita, T., Moriyoshi, K., Sakai, K., Hamada, N. and Ohe, T. Purification and some properties of 2-hydroxychromene-2-carboxylate isomerase from naphthalenesulfonate-assimilating Pseudomonas sp. TA-2. J. Biochem. 124 (1998) 591–597. [PMID: 9722670]
2.	Keck, A., Conradt, D., Mahler, A., Stolz, A., Mattes, R. and Klein, J. Identification and functional analysis of the genes for naphthalenesulfonate catabolism by Sphingomonas xenophaga BN6. Microbiology 152 (2006) 1929–1940. [DOI] [PMID: 16804169]
3.	Eaton, R.W. Organization and evolution of naphthalene catabolic pathways: sequence of the DNA encoding 2-hydroxychromene-2-carboxylate isomerase and trans-o-hydroxybenzylidenepyruvate hydratase-aldolase from the NAH7 plasmid. J. Bacteriol. 176 (1994) 7757–7762. [DOI] [PMID: 8002605]
4.	Thompson, L.C., Ladner, J.E., Codreanu, S.G., Harp, J., Gilliland, G.L. and Armstrong, R.N. 2-Hydroxychromene-2-carboxylic acid isomerase: a kappa class glutathione transferase from Pseudomonas putida. Biochemistry 46 (2007) 6710–6722. [DOI] [PMID: 17508726]

[EC 5.99.1.4 created 2010]

6.3.2.31

Accepted name:

coenzyme F₄₂₀-0:L-glutamate ligase

Reaction:

GTP + coenzyme F₄₂₀-0 + L-glutamate = GDP + phosphate + coenzyme F₄₂₀-1

For diagram of coenzyme F₄₂₀ biosynthesis, click here

Glossary:

coenzyme F₄₂₀ = N-(N-{O-[5-(8-hydroxy-2,4-dioxo-2,3,4,10-tetrahydropyrimido[4,5-b]quinolin-10-yl)-5-deoxy-L-ribityl-1-phospho]-(S)-lactyl}-γ-L-glutamyl)-L-glutamate

Other name(s):

CofE-AF; MJ0768; CofE

Systematic name:

L-glutamate:coenzyme F₄₂₀-0 ligase (GDP-forming)

Comments:

This protein catalyses the successive addition of two glutamate residues to factor F₄₂₀ (coenzyme F₄₂₀) by two distinct and independent reactions. In the reaction described here the enzyme attaches a glutamate via its α-amine group to F₄₂₀-0. In the second reaction (EC 6.3.2.34, coenzyme F₄₂₀-1:γ-L-glutamate ligase) it catalyses the addition of a second L-glutamate residue to the γ-carboxyl of the first glutamate.

Links to other databases:

References:

1.	Li, H., Graupner, M., Xu, H. and White, R.H. CofE catalyzes the addition of two glutamates to F₄₂₀-0 in F₄₂₀ coenzyme biosynthesis in Methanococcus jannaschii. Biochemistry 42 (2003) 9771–9778. [DOI] [PMID: 12911320]
2.	Nocek, B., Evdokimova, E., Proudfoot, M., Kudritska, M., Grochowski, L.L., White, R.H., Savchenko, A., Yakunin, A.F., Edwards, A. and Joachimiak, A. Structure of an amide bond forming F₄₂₀:γ-glutamyl ligase from Archaeoglobus fulgidus — a member of a new family of non-ribosomal peptide synthases. J. Mol. Biol. 372 (2007) 456–469. [DOI] [PMID: 17669425]

[EC 6.3.2.31 created 2010]

6.3.2.32

Accepted name:

coenzyme γ-F₄₂₀-2:α-L-glutamate ligase

Reaction:

ATP + coenzyme γ-F₄₂₀-2 + L-glutamate = ADP + phosphate + coenzyme α-F₄₂₀-3

For diagram of coenzyme F₄₂₀ biosynthesis, click here

Other name(s):

MJ1001; CofF protein; γ-F₄₂₀-2:α-L-glutamate ligase

Systematic name:

L-glutamate:coenzyme γ-F₄₂₀-2 (ADP-forming)

Comments:

The enzyme caps the γ-glutamyl tail of the hydride carrier coenzyme F₄₂₀ [1].

Links to other databases:

References:

1.	Li, H., Xu, H., Graham, D.E. and White, R.H. Glutathione synthetase homologs encode α-L-glutamate ligases for methanogenic coenzyme F₄₂₀ and tetrahydrosarcinapterin biosyntheses. Proc. Natl. Acad. Sci. USA 100 (2003) 9785–9790. [DOI] [PMID: 12909715]

[EC 6.3.2.32 created 2010]

6.3.2.33

Accepted name:

tetrahydrosarcinapterin synthase

Reaction:

ATP + tetrahydromethanopterin + L-glutamate = ADP + phosphate + 5,6,7,8-tetrahydrosarcinapterin

For diagram of methanopterin biosynthesis (part 4), click here

Other name(s):

H₄MPT:α-L-glutamate ligase; MJ0620; MptN protein

Systematic name:

tetrahydromethanopterin:α-L-glutamate ligase (ADP-forming)

Comments:

This enzyme catalyses the biosynthesis of 5,6,7,8-tetrahydrosarcinapterin, a modified form of tetrahydromethanopterin found in the Methanosarcinales. It does not require K⁺, and does not discriminate between ATP and GTP [1].

Links to other databases:

References:

1.	Li, H., Xu, H., Graham, D.E. and White, R.H. Glutathione synthetase homologs encode α-L-glutamate ligases for methanogenic coenzyme F₄₂₀ and tetrahydrosarcinapterin biosyntheses. Proc. Natl. Acad. Sci. USA 100 (2003) 9785–9790. [DOI] [PMID: 12909715]

[EC 6.3.2.33 created 2010]

6.3.2.34

Accepted name:

coenzyme F₄₂₀-1:γ-L-glutamate ligase

Reaction:

GTP + coenzyme F₄₂₀-1 + L-glutamate = GDP + phosphate + coenzyme γ-F₄₂₀-2

For diagram of coenzyme F₄₂₀ biosynthesis, click here

Glossary:

coenzyme F₄₂₀ = N-(N-{O-[5-(8-hydroxy-2,4-dioxo-2,3,4,10-tetrahydropyrimido[4,5-b]quinolin-10-yl)-5-deoxy-L-ribityl-1-phospho]-(S)-lactyl}-γ-L-glutamyl)-L-glutamate

Other name(s):

F₄₂₀:γ-glutamyl ligase; CofE-AF; MJ0768; CofE

Systematic name:

L-glutamate:coenzyme F₄₂₀-1 ligase (GDP-forming)

Comments:

This protein catalyses the successive addition of two glutamate residues to factor 420 (coenzyme F₄₂₀) by two distinct and independent reactions. In the first reaction (EC 6.3.2.31, coenzyme F₄₂₀-0:L-glutamate ligase) the enzyme attaches a glutamate via its α-amine group to F₄₂₀-0. In the second reaction, which is described here, the enzyme catalyses the addition of a second L-glutamate residue to the γ-carboxyl of the first glutamate.

Links to other databases: