The Enzyme Database

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EC 1.1.1.23     
Accepted name: histidinol dehydrogenase
Reaction: L-histidinol + 2 NAD+ + H2O = L-histidine + 2 NADH + 3 H+
Other name(s): L-histidinol dehydrogenase
Systematic name: L-histidinol:NAD+ oxidoreductase
Comments: Also oxidizes L-histidinal. The Neurospora enzyme also catalyses the reactions of EC 3.5.4.19 (phosphoribosyl-AMP cyclohydrolase) and EC 3.6.1.31 (phosphoribosyl-ATP diphosphatase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9028-27-7
References:
1.  Adams, E. Enzymatic synthesis of histidine from histidinol. J. Biol. Chem. 209 (1954) 829–846. [PMID: 13192138]
2.  Adams, E. L-Histidinal, a biosynthetic precursor of histidine. J. Biol. Chem. 217 (1955) 325–344. [PMID: 13271397]
3.  Loper, J.C. Histidinol dehydrogenase from Salmonella typhimurium. Crystallization and composition studies. J. Biol. Chem. 243 (1968) 3264–3272. [PMID: 4872177]
4.  Yourno, J. and Ino, I. Purification and crystallization of histidinol dehydrogenase from Salmonella typhimurium LT-2. J. Biol. Chem. 243 (1968) 3273–3276. [PMID: 4872176]
[EC 1.1.1.23 created 1961]
 
 
EC 1.1.1.33      
Deleted entry: mevaldate reductase (NADPH), now included with EC 1.1.1.2, alcohol dehydrogenase (NADP+).
[EC 1.1.1.33 created 1961, deleted 2022]
 
 
EC 1.1.1.38     
Accepted name: malate dehydrogenase (oxaloacetate-decarboxylating)
Reaction: (1) (S)-malate + NAD+ = pyruvate + CO2 + NADH
(2) oxaloacetate = pyruvate + CO2
Other name(s): ’malic’ enzyme (ambiguous); pyruvic-malic carboxylase (ambiguous); NAD+-specific malic enzyme; NAD+-malic enzyme; NAD+-linked malic enzyme
Systematic name: (S)-malate:NAD+ oxidoreductase (oxaloacetate-decarboxylating)
Comments: Unlike EC 1.1.1.39, malate dehydrogenase (decarboxylating), this enzyme can also decarboxylate oxaloacetate. cf. EC 1.1.1.40, malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9080-52-8
References:
1.  Kaufman, S., Korkes, S. and del Campillo, A. Biosynthesis of dicarboxylic acids by carbon dioxide fixation. V. Further studies of the "malic" enzyme of Lactobacillus arabinosus. J. Biol. Chem. 192 (1951) 301–312. [PMID: 14917678]
2.  Yamaguchi, M. Studies on regulatory functions of malic enzymes. IV. Effects of sulfhydryl group modification on the catalytic function of NAD-linked malic enzyme from Escherichia coli. J. Biochem. 86 (1979) 325–333. [PMID: 225306]
[EC 1.1.1.38 created 1961]
 
 
EC 1.1.1.43     
Accepted name: phosphogluconate 2-dehydrogenase
Reaction: 6-phospho-D-gluconate + NAD(P)+ = 6-phospho-2-dehydro-D-gluconate + NAD(P)H + H+
Other name(s): 6-phosphogluconic dehydrogenase; phosphogluconate dehydrogenase; gluconate 6-phosphate dehydrogenase; 6-phosphogluconate dehydrogenase (NAD); 2-keto-6-phosphogluconate reductase
Systematic name: 6-phospho-D-gluconate:NAD(P)+ 2-oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9001-82-5
References:
1.  Frampton, E.W. and Wood, W.A. Carbohydrate oxidation by Pseudomonas fluorescens. VI. Conversion of 2-keto-6-phosphogluconate to pyruvate. J. Biol. Chem. 236 (1961) 2571–2577. [PMID: 13894458]
[EC 1.1.1.43 created 1961]
 
 
EC 1.1.1.138     
Accepted name: mannitol 2-dehydrogenase (NADP+)
Reaction: D-mannitol + NADP+ = D-fructose + NADPH + H+
Other name(s): mannitol 2-dehydrogenase (NADP)
Systematic name: D-mannitol:NADP+ 2-oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37250-68-3
References:
1.  Edmundowicz, J.M. and Wriston, J.C., Jr. Mannitol dehydrogenase from Agaricus campestris. J. Biol. Chem. 238 (1963) 3539–3541. [PMID: 14109183]
2.  Strobel, G.A. and Kosuge, T. Polyol metabolism in Diplodia viticola Desm. Arch. Biochem. Biophys. 109 (1965) 622–626. [DOI] [PMID: 14320506]
[EC 1.1.1.138 created 1972]
 
 
EC 1.1.1.154     
Accepted name: ureidoglycolate dehydrogenase
Reaction: (S)-ureidoglycolate + NAD(P)+ = oxalureate + NAD(P)H + H+
For diagram of AMP catabolism, click here
Systematic name: (S)-ureidoglycolate:NAD(P)+ oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 62213-62-1
References:
1.  van der Drift, C., van Helvoort, P.E. and Vogels, G.D. S-Ureidoglycolate dehydrogenase: purification and properties. Arch. Biochem. Biophys. 145 (1971) 465–469. [DOI] [PMID: 4399430]
[EC 1.1.1.154 created 1976]
 
 
EC 1.1.1.198     
Accepted name: (+)-borneol dehydrogenase
Reaction: (+)-borneol + NAD+ = (+)-camphor + NADH + H+
For diagram of bornane and related monoterpenoids, click here
Other name(s): bicyclic monoterpenol dehydrogenase
Systematic name: (+)-borneol:NAD+ oxidoreductase
Comments: NADP+ can also act, but more slowly.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 111940-47-7
References:
1.  Croteau, R., Hooper, C.L. and Felton, M. Biosynthesis of monoterpenes. Partial purification and characterization of a bicyclic monoterpenol dehydrogenase from sage (Salvia officinalis). Arch. Biochem. Biophys. 188 (1978) 182–193. [DOI] [PMID: 677891]
2.  Dehal, S.S. and Croteau, R. Metabolism of monoterpenes: specificity of the dehydrogenases responsible for the biosynthesis of camphor, 3-thujone, and 3-isothujone. Arch. Biochem. Biophys. 258 (1987) 287–291. [DOI] [PMID: 3310901]
[EC 1.1.1.198 created 1984, modified 1990 (EC 1.1.1.182 created 1983, part incorporated 1990)]
 
 
EC 1.1.1.205     
Accepted name: IMP dehydrogenase
Reaction: IMP + NAD+ + H2O = XMP + NADH + H+
For diagram of AMP and GMP biosynthesis, click here
Glossary: IMP = inosine 5′-phosphate
XMP = xanthosine 5′-phosphate
Other name(s): inosine-5′-phosphate dehydrogenase; inosinic acid dehydrogenase; inosinate dehydrogenase; inosine 5′-monophosphate dehydrogenase; inosine monophosphate dehydrogenase; IMP oxidoreductase; inosine monophosphate oxidoreductase
Systematic name: IMP:NAD+ oxidoreductase
Comments: The enzyme acts on the hydroxy group of the hydrated derivative of the substrate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9028-93-7
References:
1.  Magasanik, B., Moyed, H.S. and Gehring, L.B. Enzymes essential for the biosynthesis of nucleic acid guanine; inosine 5′-phosphate dehydrogenase of Aerobacter aerogenes. J. Biol. Chem. 226 (1957) 339–350. [PMID: 13428767]
2.  Turner, J.F. and King, J.E. Inosine 5-phosphate dehydrogenase of pea seeds. Biochem. J. 79 (1961) 147. [PMID: 13778733]
[EC 1.1.1.205 created 1961 as EC 1.2.1.14, transferred 1984 to EC 1.1.1.205]
 
 
EC 1.1.1.227     
Accepted name: (-)-borneol dehydrogenase
Reaction: (-)-borneol + NAD+ = (-)-camphor + NADH + H+
Systematic name: (-)-borneol:NAD+ oxidoreductase
Comments: NADP+ can also act, but more slowly.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 111940-48-8
References:
1.  Dehal, S.S. and Croteau, R. Metabolism of monoterpenes: specificity of the dehydrogenases responsible for the biosynthesis of camphor, 3-thujone, and 3-isothujone. Arch. Biochem. Biophys. 258 (1987) 287–291. [DOI] [PMID: 3310901]
[EC 1.1.1.227 created 1990 (EC 1.1.1.182 created 1983, part incorporated 1990)]
 
 
EC 1.1.1.228     
Accepted name: (+)-sabinol dehydrogenase
Reaction: (+)-cis-sabinol + NAD+ = (+)-sabinone + NADH + H+
For diagram of thujane monoterpenoid biosynthesis, click here
Other name(s): (+)-cis-sabinol dehydrogenase
Systematic name: (+)-cis-sabinol:NAD+ oxidoreductase
Comments: NADP+ can also act, but more slowly. Involved in the biosynthesis of (+)-3-thujone and (–)-3-isothujone.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 111940-50-2
References:
1.  Dehal, S.S. and Croteau, R. Metabolism of monoterpenes: specificity of the dehydrogenases responsible for the biosynthesis of camphor, 3-thujone, and 3-isothujone. Arch. Biochem. Biophys. 258 (1987) 287–291. [DOI] [PMID: 3310901]
[EC 1.1.1.228 created 1990 (EC 1.1.1.182 created 1983, part incorporated 1990)]
 
 
EC 1.1.1.306     
Accepted name: S-(hydroxymethyl)mycothiol dehydrogenase
Reaction: S-(hydroxymethyl)mycothiol + NAD+ = S-formylmycothiol + NADH + H+
Glossary: mycothiol = 1-O-[2-(N2-acetyl-L-cysteinamido)-2-deoxy-α-D-glucopyranosyl]-1D-myo-inositol
Other name(s): NAD/factor-dependent formaldehyde dehydrogenase; mycothiol-dependent formaldehyde dehydrogenase
Systematic name: S-(hydroxymethyl)mycothiol:NAD+ oxidoreductase
Comments: S-hydroxymethylmycothiol is believed to form spontaneously from formaldehyde and mycothiol. This enzyme oxidizes the product of this spontaneous reaction to S-formylmycothiol, in a reaction that is analogous to EC 1.1.1.284, S-(hydroxymethyl)glutathione dehydrogenase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 192140-85-5
References:
1.  Misset-Smits, M., Van Ophem, P.W., Sakuda, S. and Duine, J.A. Mycothiol, 1-O-(2′-[N-acetyl-L-cysteinyl]amido-2′-deoxy-α-D-glucopyranosyl)-D-myo-inositol, is the factor of NAD/factor-dependent formaldehyde dehydrogenase. FEBS Lett. 409 (1997) 221–222. [DOI] [PMID: 9202149]
2.  Norin, A., Van Ophem, P.W., Piersma, S.R., Person, B., Duine, J.A. and Jornvall, H. Mycothiol-dependent formaldehyde dehydrogenase, a prokaryotic medium-chain dehydrogenase/reductase, phylogenetically links different eukaryotic alcohol dehydrogenase's - primary structure, conformational modelling and functional correlations. Eur. J. Biochem. 248 (1997) 282–289. [DOI] [PMID: 9346279]
3.  Vogt, R.N., Steenkamp, D.J., Zheng, R. and Blanchard, J.S. The metabolism of nitrosothiols in the Mycobacteria: identification and characterization of S-nitrosomycothiol reductase. Biochem. J. 374 (2003) 657–666. [DOI] [PMID: 12809551]
4.  Rawat, M. and Av-Gay, Y. Mycothiol-dependent proteins in actinomycetes. FEMS Microbiol. Rev. 31 (2007) 278–292. [DOI] [PMID: 17286835]
[EC 1.1.1.306 created 2010 as EC 1.2.1.66, transferred 2010 to EC 1.1.1.306]
 
 
EC 1.1.1.317     
Accepted name: perakine reductase
Reaction: raucaffrinoline + NADP+ = perakine + NADPH + H+
For diagram of peraksine biosynthesis, click here
Glossary: raucaffrinoline = (17R,20α,21β)-1,2-didehydro-1-demethyl-19-hydroxy-21-methyl-18-norajmalan-17-yl acetate
perakine = raucaffrine = (17R,20α,21β)-1,2-didehydro-1-demethyl-17-(acetyloxy)-21-methyl-18-norajmalan-19-al
Systematic name: raucaffrinoline:NADP+ oxidoreductase
Comments: The biosynthesis of raucaffrinoline from perakine is a side route of the ajmaline biosynthesis pathway. The enzyme is a member of the aldo-keto reductase enzyme superfamily from higher plants.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Sun, L., Ruppert, M., Sheludko, Y., Warzecha, H., Zhao, Y. and Stockigt, J. Purification, cloning, functional expression and characterization of perakine reductase: the first example from the AKR enzyme family, extending the alkaloidal network of the plant Rauvolfia. Plant Mol. Biol. 67 (2008) 455–467. [DOI] [PMID: 18409028]
2.  Rosenthal, C., Mueller, U., Panjikar, S., Sun, L., Ruppert, M., Zhao, Y. and Stockigt, J. Expression, purification, crystallization and preliminary X-ray analysis of perakine reductase, a new member of the aldo-keto reductase enzyme superfamily from higher plants. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 62 (2006) 1286–1289. [DOI] [PMID: 17142919]
[EC 1.1.1.317 created 2011]
 
 
EC 1.1.1.326     
Accepted name: zerumbone synthase
Reaction: 10-hydroxy-α-humulene + NAD+ = zerumbone + NADH + H+
For diagram of zerumbone biosynthesis, click here
Other name(s): ZSD1
Systematic name: 10-hydroxy-α-humulene:NAD+ oxidoreductase
Comments: The enzyme was cloned from shampoo ginger, Zingiber zerumbet.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Okamoto, S., Yu, F., Harada, H., Okajima, T., Hattan, J., Misawa, N. and Utsumi, R. A short-chain dehydrogenase involved in terpene metabolism from Zingiber zerumbet. FEBS J. 278 (2011) 2892–2900. [DOI] [PMID: 21668645]
[EC 1.1.1.326 created 2012]
 
 
EC 1.1.1.327     
Accepted name: 5-exo-hydroxycamphor dehydrogenase
Reaction: 5-exo-hydroxycamphor + NAD+ = bornane-2,5-dione + NADH + H+
For diagram of camphor catabolism, click here
Other name(s): F-dehydrogenase; FdeH
Systematic name: 5-exo-hydroxycamphor:NAD+ oxidoreductase
Comments: Contains Zn2+. Isolated from Pseudomonas putida, and involved in degradation of (+)-camphor.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc
References:
1.  Rheinwald, J.G., Chakrabarty, A.M. and Gunsalus, I.C. A transmissible plasmid controlling camphor oxidation in Pseudomonas putida. Proc. Natl. Acad. Sci. USA 70 (1973) 885–889. [DOI] [PMID: 4351810]
2.  Koga, H., Yamaguchi, E., Matsunaga, K., Aramaki, H. and Horiuchi, T. Cloning and nucleotide sequences of NADH-putidaredoxin reductase gene (camA) and putidaredoxin gene (camB) involved in cytochrome P-450cam hydroxylase of Pseudomonas putida. J. Biochem. 106 (1989) 831–836. [PMID: 2613690]
3.  Aramaki, H., Koga, H., Sagara, Y., Hosoi, M. and Horiuchi, T. Complete nucleotide sequence of the 5-exo-hydroxycamphor dehydrogenase gene on the CAM plasmid of Pseudomonas putida (ATCC 17453). Biochim. Biophys. Acta 1174 (1993) 91–94. [DOI] [PMID: 8334169]
[EC 1.1.1.327 created 2012]
 
 
EC 1.1.1.337     
Accepted name: L-2-hydroxycarboxylate dehydrogenase (NAD+)
Reaction: a (2S)-2-hydroxycarboxylate + NAD+ = a 2-oxocarboxylate + NADH + H+
Other name(s): (R)-sulfolactate:NAD+ oxidoreductase; L-sulfolactate dehydrogenase; (R)-sulfolactate dehydrogenase; L-2-hydroxyacid dehydrogenase (NAD+); ComC
Systematic name: (2S)-2-hydroxycarboxylate:NAD+ oxidoreductase
Comments: The enzyme from the archaeon Methanocaldococcus jannaschii acts on multiple (S)-2-hydroxycarboxylates including (2R)-3-sulfolactate, (S)-malate, (S)-lactate, and (S)-2-hydroxyglutarate [3]. Note that (2R)-3-sulfolactate has the same stereo configuration as (2S)-2-hydroxycarboxylates.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 81210-65-3
References:
1.  Graupner, M., Xu, H. and White, R.H. Identification of an archaeal 2-hydroxy acid dehydrogenase catalyzing reactions involved in coenzyme biosynthesis in methanoarchaea. J. Bacteriol. 182 (2000) 3688–3692. [DOI] [PMID: 10850983]
2.  Graupner, M. and White, R.H. The first examples of (S)-2-hydroxyacid dehydrogenases catalyzing the transfer of the pro-4S hydrogen of NADH are found in the archaea. Biochim. Biophys. Acta 1548 (2001) 169–173. [DOI] [PMID: 11451450]
3.  Graham, D.E. and White, R.H. Elucidation of methanogenic coenzyme biosyntheses: from spectroscopy to genomics. Nat. Prod. Rep. 19 (2002) 133–147. [PMID: 12013276]
4.  Rein, U., Gueta, R., Denger, K., Ruff, J., Hollemeyer, K. and Cook, A.M. Dissimilation of cysteate via 3-sulfolactate sulfo-lyase and a sulfate exporter in Paracoccus pantotrophus NKNCYSA. Microbiology 151 (2005) 737–747. [DOI] [PMID: 15758220]
[EC 1.1.1.337 created 2012]
 
 
EC 1.1.1.350     
Accepted name: ureidoglycolate dehydrogenase (NAD+)
Reaction: (S)-ureidoglycolate + NAD+ = N-carbamoyl-2-oxoglycine + NADH + H+
For diagram of AMP catabolism, click here
Systematic name: (S)-ureidoglycolate:NAD+ oxidoreductase
Comments: Involved in catabolism of purines. The enzyme from the bacterium Escherichia coli is specific for NAD+ [2]. cf. EC 1.1.1.154, ureidoglycolate dehydrogenase [NAD(P)+].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Cusa, E., Obradors, N., Baldoma, L., Badia, J. and Aguilar, J. Genetic analysis of a chromosomal region containing genes required for assimilation of allantoin nitrogen and linked glyoxylate metabolism in Escherichia coli. J. Bacteriol. 181 (1999) 7479–7484. [PMID: 10601204]
2.  Kim, M.I., Shin, I., Cho, S., Lee, J. and Rhee, S. Structural and functional insights into (S)-ureidoglycolate dehydrogenase, a metabolic branch point enzyme in nitrogen utilization. PLoS One 7:e52066 (2012). [DOI] [PMID: 23284870]
[EC 1.1.1.350 created 2013]
 
 
EC 1.1.1.359     
Accepted name: aldose 1-dehydrogenase [NAD(P)+]
Reaction: an aldopyranose + NAD(P)+ = an aldono-1,5-lactone + NAD(P)H + H+
For diagram of L-fucose catabolism, click here
Systematic name: an aldopyranose:NAD(P)+ 1-oxidoreductase
Comments: The enzyme from the archaeon Sulfolobus solfataricus shows broad specificity towards aldoses (D-glucose, D-galactose, D-xylose, L-arabinose, 6-deoxy-D-glucose, D-fucose) and can utilize NAD+ and NADP+ with similar catalytic efficiency. It is involved in aldose catabolism via the branched variant of the Entner-Doudoroff pathway.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Giardina, P., de Biasi, M.G., de Rosa, M., Gambacorta, A. and Buonocore, V. Glucose dehydrogenase from the thermoacidophilic archaebacterium Sulfolobus solfataricus. Biochem. J. 239 (1986) 517–522. [PMID: 3827812]
2.  Smith, L.D., Budgen, N., Bungard, S.J., Danson, M.J. and Hough, D.W. Purification and characterization of glucose dehydrogenase from the thermoacidophilic archaebacterium Thermoplasma acidophilum. Biochem. J. 261 (1989) 973–977. [PMID: 2803257]
3.  Lamble, H.J., Heyer, N.I., Bull, S.D., Hough, D.W. and Danson, M.J. Metabolic pathway promiscuity in the archaeon Sulfolobus solfataricus revealed by studies on glucose dehydrogenase and 2-keto-3-deoxygluconate aldolase. J. Biol. Chem. 278 (2003) 34066–34072. [DOI] [PMID: 12824170]
4.  Theodossis, A., Milburn, C.C., Heyer, N.I., Lamble, H.J., Hough, D.W., Danson, M.J. and Taylor, G.L. Preliminary crystallographic studies of glucose dehydrogenase from the promiscuous Entner-Doudoroff pathway in the hyperthermophilic archaeon Sulfolobus solfataricus. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 61 (2005) 112–115. [DOI] [PMID: 16508107]
5.  Milburn, C.C., Lamble, H.J., Theodossis, A., Bull, S.D., Hough, D.W., Danson, M.J. and Taylor, G.L. The structural basis of substrate promiscuity in glucose dehydrogenase from the hyperthermophilic archaeon Sulfolobus solfataricus. J. Biol. Chem. 281 (2006) 14796–14804. [DOI] [PMID: 16556607]
6.  Haferkamp, P., Kutschki, S., Treichel, J., Hemeda, H., Sewczyk, K., Hoffmann, D., Zaparty, M. and Siebers, B. An additional glucose dehydrogenase from Sulfolobus solfataricus: fine-tuning of sugar degradation. Biochem. Soc. Trans. 39 (2011) 77–81. [DOI] [PMID: 21265750]
[EC 1.1.1.359 created 2013]
 
 
EC 1.1.1.430     
Accepted name: D-xylose reductase (NADH)
Reaction: xylitol + NAD+ = D-xylose + NADH + H+
Other name(s): XYL1 (gene name) (ambiguous)
Systematic name: xylitol:NAD+ oxidoreductase
Comments: Xylose reductases catalyse the reduction of xylose to xylitol, the initial reaction in the fungal D-xylose degradation pathway. Most of the enzymes exhibit a strict requirement for NADPH (cf. EC 1.1.1.431, D-xylose reductase (NADPH)). Some D-xylose reductases have dual cosubstrate specificity, though they still prefer NADPH to NADH (cf. EC 1.1.1.307, D-xylose reductase [NAD(P)H]). The enzyme from Candida parapsilosis is a rare example of a xylose reductase that significantly prefers NADH, with Km and Vmax values for NADH being 10-fold lower and 10-fold higher, respectively, than for NADPH.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Lee, J.K., Koo, B.S. and Kim, S.Y. Cloning and characterization of the xyl1 gene, encoding an NADH-preferring xylose reductase from Candida parapsilosis, and its functional expression in Candida tropicalis. Appl. Environ. Microbiol. 69 (2003) 6179–6188. [DOI] [PMID: 14532079]
[EC 1.1.1.430 created 2022]
 
 
EC 1.1.1.434     
Accepted name: 2-dehydro-3-deoxy-L-fuconate 4-dehydrogenase
Reaction: 2-dehydro-3-deoxy-L-fuconate + NAD+ = 2,4-didehydro-3-deoxy-L-fuconate + NADH + H+
For diagram of L-fucose catabolism, click here
Glossary: 2-dehydro-3-deoxy-L-fuconate = (4S,5S)-4,5-dihydroxy-2-oxohexanoate
2,4-didehydro-3-deoxy-L-fuconate = (5S)-5-hydroxy-2,4-dioxohexanoate
Systematic name: 2-dehydro-3-deoxy-L-fuconate:NAD+ 4-oxidoreductase
Comments: The enzyme, originally described from the bacterium Xanthomonas campestris pv. campestris, participates in an L-fucose degradation pathway. It can also act on 2-dehydro-3-deoxy-L-galactonate and 2-dehydro-3-deoxy-D-pentonate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Yew, W.S., Fedorov, A.A., Fedorov, E.V., Rakus, J.F., Pierce, R.W., Almo, S.C. and Gerlt, J.A. Evolution of enzymatic activities in the enolase superfamily: L-fuconate dehydratase from Xanthomonas campestris. Biochemistry 45 (2006) 14582–14597. [DOI] [PMID: 17144652]
2.  Watanabe, S., Fukumori, F., Nishiwaki, H., Sakurai, Y., Tajima, K. and Watanabe, Y. Novel non-phosphorylative pathway of pentose metabolism from bacteria. Sci. Rep. 9:155 (2019). [DOI] [PMID: 30655589]
[EC 1.1.1.434 created 2022]
 
 
EC 1.1.2.10     
Accepted name: lanthanide-dependent methanol dehydrogenase
Reaction: methanol + 2 oxidized cytochrome cL = formaldehyde + 2 reduced cytochrome cL
Other name(s): XoxF; XoxF-MDH; Ce-MDH; La3+-dependent MDH; Ce3+-induced methanol dehydrogenase; cerium dependent MDH
Systematic name: methanol:cytochrome cL oxidoreductase
Comments: Isolated from the bacterium Methylacidiphilum fumariolicum and many Methylobacterium species. Requires La3+, Ce3+, Pr3+ or Nd3+. The higher lanthanides show decreasing activity with Sm3+, Eu3+ and Gd3+. The lanthanide is coordinated by the enzyme and pyrroloquinoline quinone. Shows little activity with Ca2+, the required cofactor of EC 1.1.2.7, methanol dehydrogenase (cytochrome c).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Hibi, Y., Asai, K., Arafuka, H., Hamajima, M., Iwama, T. and Kawai, K. Molecular structure of La3+-induced methanol dehydrogenase-like protein in Methylobacterium radiotolerans. J. Biosci. Bioeng. 111 (2011) 547–549. [PMID: 21256798]
2.  Nakagawa, T., Mitsui, R., Tani, A., Sasa, K., Tashiro, S., Iwama, T., Hayakawa, T. and Kawai, K. A catalytic role of XoxF1 as La3+-dependent methanol dehydrogenase in Methylobacterium extorquens strain AM1. PLoS One 7:e50480 (2012). [PMID: 23209751]
3.  Pol, A., Barends, T.R., Dietl, A., Khadem, A.F., Eygensteyn, J., Jetten, M.S. and Op den Camp, H.J. Rare earth metals are essential for methanotrophic life in volcanic mudpots. Environ. Microbiol. 16 (2014) 255–264. [PMID: 24034209]
4.  Bogart, J.A., Lewis, A.J. and Schelter, E.J. DFT study of the active site of the XoxF-type natural, cerium-dependent methanol dehydrogenase enzyme. Chemistry Eur. J. 21 (2015) 1743–1748. [PMID: 25421364]
5.  Prejano, M., Marino, T. and Russo, N. How can methanol dehydrogenase from Methylacidiphilum fumariolicum work with the alien Ce(III) ion in the active center? A theoretical study. Chemistry 23 (2017) 8652–8657. [PMID: 28488399]
6.  Masuda, S., Suzuki, Y., Fujitani, Y., Mitsui, R., Nakagawa, T., Shintani, M. and Tani, A. Lanthanide-dependent regulation of methylotrophy in Methylobacterium aquaticum strain 22A. mSphere 3 (2018) e00462. [PMID: 29404411]
[EC 1.1.2.10 created 2019]
 
 
EC 1.1.3.40     
Accepted name: D-mannitol oxidase
Reaction: D-mannitol + O2 = D-mannose + H2O2
Other name(s): mannitol oxidase; D-arabitol oxidase
Systematic name: mannitol:oxygen oxidoreductase (cyclizing)
Comments: Also catalyses the oxidation of D-arabinitol and, to a lesser extent, D-glucitol (sorbitol), whereas L-arabinitol is not a good substrate. The enzyme from the snails Helix aspersa and Arion ater is found in a specialised tubular organelle that has been termed the mannosome.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 73562-29-5
References:
1.  Vorhaben, J.E., Scott, J.F., Smith, D.D. and Campbell, J.W. Mannitol oxidase: partial purification and characterisation of the membrane-bound enzyme from the snail Helix aspersa. Int. J. Biochem. 18 (1986) 337–344. [PMID: 3519307]
2.  Malik, Z., Jones, C.J.P. and Connock, M.J. Assay and subcellular localization of H2O2 generating mannitol oxidase in the terrestrial slug Arion ater. J. Exp. Zool. 242 (1987) 9–15.
3.  Large, A.T., Jones, C.J.P. and Connock, M.J. The association of mannitol oxidase with a distinct organelle in the digestive gland of the terrestrial slug Arion ater. Protoplasma 175 (1993) 93–101.
4.  Lobo-da-Cunha, A., Amaral-de-Carvalho, D., Oliveira, E., Alves, A., Costa, V. and Calado, G. Mannitol oxidase and polyol dehydrogenases in the digestive gland of gastropods: Correlations with phylogeny and diet. PLoS One 13:e0193078 (2018). [PMID: 29529078]
[EC 1.1.3.40 created 2001]
 
 
EC 1.1.5.3     
Accepted name: glycerol-3-phosphate dehydrogenase
Reaction: sn-glycerol 3-phosphate + a quinone = glycerone phosphate + a quinol
Glossary: glycerone phosphate = dihydroxyacetone phosphate = 3-hydroxy-2-oxopropyl phosphate
Other name(s): α-glycerophosphate dehydrogenase; α-glycerophosphate dehydrogenase (acceptor); anaerobic glycerol-3-phosphate dehydrogenase; DL-glycerol 3-phosphate oxidase (misleading); FAD-dependent glycerol-3-phosphate dehydrogenase; FAD-dependent sn-glycerol-3-phosphate dehydrogenase; FAD-GPDH; FAD-linked glycerol 3-phosphate dehydrogenase; FAD-linked L-glycerol-3-phosphate dehydrogenase; flavin-linked glycerol-3-phosphate dehydrogenase; flavoprotein-linked L-glycerol 3-phosphate dehydrogenase; glycerol 3-phosphate cytochrome c reductase (misleading); glycerol phosphate dehydrogenase; glycerol phosphate dehydrogenase (acceptor); glycerol phosphate dehydrogenase (FAD); glycerol-3-phosphate CoQ reductase; glycerol-3-phosphate dehydrogenase (flavin-linked); glycerol-3-phosphate:CoQ reductase; glycerophosphate dehydrogenase; L-3-glycerophosphate-ubiquinone oxidoreductase; L-glycerol-3-phosphate dehydrogenase (ambiguous); L-glycerophosphate dehydrogenase; mGPD; mitochondrial glycerol phosphate dehydrogenase; NAD+-independent glycerol phosphate dehydrogenase; pyridine nucleotide-independent L-glycerol 3-phosphate dehydrogenase; sn-glycerol 3-phosphate oxidase (misleading); sn-glycerol-3-phosphate dehydrogenase; sn-glycerol-3-phosphate:(acceptor) 2-oxidoreductase; sn-glycerol-3-phosphate:acceptor 2-oxidoreductase
Systematic name: sn-glycerol 3-phosphate:quinone oxidoreductase
Comments: This flavin-dependent dehydrogenase is an essential membrane enzyme, functioning at the central junction of glycolysis, respiration and phospholipid biosynthesis. In bacteria, the enzyme is localized to the cytoplasmic membrane [6], while in eukaryotes it is tightly bound to the outer surface of the inner mitochondrial membrane [2]. In eukaryotes, this enzyme, together with the cytosolic enzyme EC 1.1.1.8, glycerol-3-phosphate dehydrogenase (NAD+), forms the glycerol-3-phosphate shuttle by which NADH produced in the cytosol, primarily from glycolysis, can be reoxidized to NAD+ by the mitochondrial electron-transport chain [3]. This shuttle plays a critical role in transferring reducing equivalents from cytosolic NADH into the mitochondrial matrix [7,8]. Insect flight muscle uses only CoQ10 as the physiological quinone whereas hamster and rat mitochondria use mainly CoQ9 [4]. The enzyme is activated by calcium [3].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9001-49-4
References:
1.  Ringler, R.L. Studies on the mitochondrial α-glycerophosphate dehydrogenase. II. Extraction and partial purification of the dehydrogenase from pig brain. J. Biol. Chem. 236 (1961) 1192–1198. [PMID: 13741763]
2.  Schryvers, A., Lohmeier, E. and Weiner, J.H. Chemical and functional properties of the native and reconstituted forms of the membrane-bound, aerobic glycerol-3-phosphate dehydrogenase of Escherichia coli. J. Biol. Chem. 253 (1978) 783–788. [PMID: 340460]
3.  MacDonald, M.J. and Brown, L.J. Calcium activation of mitochondrial glycerol phosphate dehydrogenase restudied. Arch. Biochem. Biophys. 326 (1996) 79–84. [DOI] [PMID: 8579375]
4.  Rauchová, H., Fato, R., Drahota, Z. and Lenaz, G. Steady-state kinetics of reduction of coenzyme Q analogs by glycerol-3-phosphate dehydrogenase in brown adipose tissue mitochondria. Arch. Biochem. Biophys. 344 (1997) 235–241. [DOI] [PMID: 9244403]
5.  Shen, W., Wei, Y., Dauk, M., Zheng, Z. and Zou, J. Identification of a mitochondrial glycerol-3-phosphate dehydrogenase from Arabidopsis thaliana: evidence for a mitochondrial glycerol-3-phosphate shuttle in plants. FEBS Lett. 536 (2003) 92–96. [DOI] [PMID: 12586344]
6.  Walz, A.C., Demel, R.A., de Kruijff, B. and Mutzel, R. Aerobic sn-glycerol-3-phosphate dehydrogenase from Escherichia coli binds to the cytoplasmic membrane through an amphipathic α-helix. Biochem. J. 365 (2002) 471–479. [DOI] [PMID: 11955283]
7.  Ansell, R., Granath, K., Hohmann, S., Thevelein, J.M. and Adler, L. The two isoenzymes for yeast NAD+-dependent glycerol 3-phosphate dehydrogenase encoded by GPD1 and GPD2 have distinct roles in osmoadaptation and redox regulation. EMBO J. 16 (1997) 2179–2187. [DOI] [PMID: 9171333]
8.  Larsson, C., Påhlman, I.L., Ansell, R., Rigoulet, M., Adler, L. and Gustafsson, L. The importance of the glycerol 3-phosphate shuttle during aerobic growth of Saccharomyces cerevisiae. Yeast 14 (1998) 347–357. [DOI] [PMID: 9559543]
[EC 1.1.5.3 created 1961 as EC 1.1.2.1, transferred 1965 to EC 1.1.99.5, transferred 2009 to EC 1.1.5.3]
 
 
EC 1.1.99.3     
Accepted name: gluconate 2-dehydrogenase (acceptor)
Reaction: D-gluconate + acceptor = 2-dehydro-D-gluconate + reduced acceptor
Other name(s): gluconate oxidase; gluconate dehydrogenase; gluconic dehydrogenase; D-gluconate dehydrogenase; gluconic acid dehydrogenase; 2-ketogluconate reductase; D-gluconate dehydrogenase, 2-keto-D-gluconate-yielding; D-gluconate:(acceptor) 2-oxidoreductase
Systematic name: D-gluconate:acceptor 2-oxidoreductase
Comments: A flavoprotein (FAD).
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 9028-81-3
References:
1.  Matsushita, K., Shinagawa, E. and Ameyama, M. D-Gluconate dehydrogenases from bacteria, 2-keto-D-gluconate-yielding membrane-bound. Methods Enzymol. 89 (1982) 187–193. [PMID: 6815420]
2.  Ramakrishnan, T. and Campbell, J.J.R. Gluconic dehydrogenase of Pseudomonas aeruginosa. Biochim. Biophys. Acta 17 (1955) 122–127. [DOI] [PMID: 13239635]
[EC 1.1.99.3 created 1961, modified 1976, modified 1989]
 
 
EC 1.1.99.13     
Accepted name: glucoside 3-dehydrogenase (acceptor)
Reaction: sucrose + acceptor = 3-dehydro-α-D-glucosyl-β-D-fructofuranoside + reduced acceptor
Other name(s): D-glucoside 3-dehydrogenase (ambiguous); D-aldohexopyranoside dehydrogenase (ambiguous); D-aldohexoside:(acceptor) 3-oxidoreductase; thuA (gene name); thuB (gene name); glucoside 3-dehydrogenase
Systematic name: D-aldohexoside:acceptor 3-oxidoreductase
Comments: The enzymes from members of the Rhizobiaceae family (such as Agrobacterium tumefaciens) act on disaccharides that contain a glucose moiety at the non-reducing end, such as sucrose, trehalose, leucrose, palatinose, trehalulose, and maltitol, forming the respective 3′-keto derivatives. cf. EC 1.1.2.11, glucoside 3-dehydrogenase (cytochrome c).
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 9031-74-7
References:
1.  Jensen, J.B., Ampomah, O.Y., Darrah, R., Peters, N.K. and Bhuvaneswari, T.V. Role of trehalose transport and utilization in Sinorhizobium meliloti-alfalfa interactions. Mol. Plant Microbe Interact. 18 (2005) 694–702. [DOI] [PMID: 16042015]
2.  Ampomah, O.Y., Avetisyan, A., Hansen, E., Svenson, J., Huser, T., Jensen, J.B. and Bhuvaneswari, T.V. The thuEFGKAB operon of Rhizobia and Agrobacterium tumefaciens codes for transport of trehalose, maltitol, and isomers of sucrose and their assimilation through the formation of their 3-keto derivatives. J. Bacteriol. 195 (2013) 3797–3807. [DOI] [PMID: 23772075]
3.  Ampomah, O.Y. and Jensen, J.B. The trehalose utilization gene thuA ortholog in Mesorhizobium loti does not influence competitiveness for nodulation on Lotus spp. World J. Microbiol. Biotechnol. 30 (2014) 1129–1134. [DOI] [PMID: 24142427]
[EC 1.1.99.13 created 1972, modified 2022]
 
 
EC 1.2.1.19     
Accepted name: aminobutyraldehyde dehydrogenase
Reaction: 4-aminobutanal + NAD+ + H2O = 4-aminobutanoate + NADH + 2 H+
For diagram of arginine catabolism, click here
Glossary: 4-aminobutanoate = γ-aminobutyrate = GABA
Other name(s): γ-guanidinobutyraldehyde dehydrogenase (ambiguous); ABAL dehydrogenase; 4-aminobutyraldehyde dehydrogenase; 4-aminobutanal dehydrogenase; γ-aminobutyraldehyde dehydroganase; 1-pyrroline dehydrogenase; ABALDH; YdcW
Systematic name: 4-aminobutanal:NAD+ 1-oxidoreductase
Comments: The enzyme from some species exhibits broad substrate specificity and has a marked preference for straight-chain aldehydes (up to 7 carbon atoms) as substrates [9]. The plant enzyme also acts on 4-guanidinobutanal (cf. EC 1.2.1.54 γ-guanidinobutyraldehyde dehydrogenase). As 1-pyrroline and 4-aminobutanal are in equilibrium and can be interconverted spontaneously, 1-pyrroline may act as the starting substrate. The enzyme forms part of the arginine-catabolism pathway [8] and belongs in the aldehyde dehydrogenase superfamily [9].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9028-98-2
References:
1.  Callewaert, D.M., Rosemblatt, M.S. and Tchen, T.T. Purification and properties of 4-aminobutanal dehydrogenase from a Pseudomonas species. J. Biol. Chem. 249 (1974) 1737–1741. [PMID: 4817964]
2.  Jakoby, W.B. Aldehyde dehydrogenases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 7, Academic Press, New York, 1963, pp. 203–221.
3.  Jakoby, W.B. and Fredericks, J. Pyrrolidine and putrescine metabolism: γ-aminobutyraldehyde dehydrogenase. J. Biol. Chem. 234 (1959) 2145–2150. [PMID: 13673029]
4.  Matsuda, H. and Suzuki, Y. γ-Guanidinobutyraldehyde dehydrogenase of Vicia faba leaves. Plant Physiol. 76 (1984) 654–657. [PMID: 16663901]
5.  Yorifuji, T., Koike, K., Sakurai, T. and Yokoyama, K. 4-Aminobutyraldehyde and 4-guanidinobutyraldehyde dehydrogenases for arginine degradation in Pseudomonas putida. Agric. Biol. Chem. 50 (1986) 2009–2016.
6.  Prieto-Santos, M.I., Martin-Checa, J., Balaña-Fouce, R. and Garrido-Pertierra, A. A pathway for putrescine catabolism in Escherichia coli. Biochim. Biophys. Acta 880 (1986) 242–244. [DOI] [PMID: 3510672]
7.  Prieto, M.I., Martin, J., Balaña-Fouce, R. and Garrido-Pertierra, A. Properties of γ-aminobutyraldehyde dehydrogenase from Escherichia coli. Biochimie 69 (1987) 1161–1168. [DOI] [PMID: 3129020]
8.  Samsonova, N.N., Smirnov, S.V., Novikova, A.E. and Ptitsyn, L.R. Identification of Escherichia coli K12 YdcW protein as a γ-aminobutyraldehyde dehydrogenase. FEBS Lett. 579 (2005) 4107–4112. [DOI] [PMID: 16023116]
9.  Gruez, A., Roig-Zamboni, V., Grisel, S., Salomoni, A., Valencia, C., Campanacci, V., Tegoni, M. and Cambillau, C. Crystal structure and kinetics identify Escherichia coli YdcW gene product as a medium-chain aldehyde dehydrogenase. J. Mol. Biol. 343 (2004) 29–41. [DOI] [PMID: 15381418]
[EC 1.2.1.19 created 1965, modified 1989 (EC 1.5.1.35 created 2006, incorporated 2007)]
 
 
EC 1.2.1.30     
Accepted name: carboxylate reductase (NADP+)
Reaction: an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
Other name(s): aromatic acid reductase; aryl-aldehyde dehydrogenase (NADP+)
Systematic name: aryl-aldehyde:NADP+ oxidoreductase (ATP-forming)
Comments: The enzyme contains an adenylation domain, a phosphopantetheinyl binding domain, and a reductase domain, and requires activation by attachment of a phosphopantetheinyl group. The enzyme activates its substrate to an adenylate form, followed by a transfer to the phosphopantetheinyl binding domain. The resulting thioester is subsequently transferred to the reductase domain, where it is reduced to an aldehyde and released.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9074-94-6
References:
1.  Gross, G.G. and Zenk, M.H. Reduktion aromatischer Säuer zu Aldehyden und Alkoholen im zellfreien System. 1. Reinigung und Eigenschaften von Aryl-Aldehyd:NADP-Oxidoreduktase aus Neurospora crassa. Eur. J. Biochem. 8 (1969) 413–419. [DOI] [PMID: 4389863]
2.  Gross, G.G. Formation and reduction of intermediate acyladenylate by aryl-aldehyde. NADP oxidoreductase from Neurospora crassa. Eur. J. Biochem. 31 (1972) 585–592. [DOI] [PMID: 4405494]
3.  Venkitasubramanian, P., Daniels, L. and Rosazza, J.P. Reduction of carboxylic acids by Nocardia aldehyde oxidoreductase requires a phosphopantetheinylated enzyme. J. Biol. Chem. 282 (2007) 478–485. [PMID: 17102130]
4.  Stolterfoht, H., Schwendenwein, D., Sensen, C.W., Rudroff, F. and Winkler, M. Four distinct types of E.C. 1.2.1.30 enzymes can catalyze the reduction of carboxylic acids to aldehydes. J. Biotechnol. 257 (2017) 222–232. [PMID: 28223183]
[EC 1.2.1.30 created 1972, modified 2019]
 
 
EC 1.2.1.59     
Accepted name: glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) (phosphorylating)
Reaction: D-glyceraldehyde 3-phosphate + phosphate + NAD(P)+ = 3-phospho-D-glyceroyl phosphate + NAD(P)H + H+
Other name(s): triosephosphate dehydrogenase (NAD(P)); glyceraldehyde-3-phosphate dehydrogenase (NAD(P)) (phosphorylating)
Systematic name: D-glyceraldehyde 3-phosphate:NAD(P)+ oxidoreductase (phosphorylating)
Comments: NAD+ and NADP+ can be used as cofactors with similar efficiency, unlike EC 1.2.1.12 glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) and EC 1.2.1.13 glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating), which are NAD+- and NADP+-dependent, respectively.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 39369-25-0
References:
1.  Valverde, F., Losada, M. and Serrano, A. Cloning by functional complementation in E. coli of the gap2 gene of Synechocystis PCC 6803 supports an amphibolic role for cyanobacterial NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase. In: P. Mathis (Ed.), Photosynthesis: From Light to Biosphere, vol. 1, Kluwer Academic Publishers, 1995, pp. 959–962.
2.  Valverde, F., Losada, M. and Serrano, A. Functional complementation of an Escherichia coli gap mutant supports an amphibolic role for NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase of Synechocystis sp. strain PCC 6803. J. Bacteriol. 179 (1997) 4513–4522. [DOI] [PMID: 9226260]
[EC 1.2.1.59 created 1999]
 
 
EC 1.2.1.70     
Accepted name: glutamyl-tRNA reductase
Reaction: L-glutamate 1-semialdehyde + NADP+ + tRNAGlu = L-glutamyl-tRNAGlu + NADPH + H+
For diagram of the early stages of porphyrin biosynthesis, click here
Systematic name: L-glutamate-semialdehyde:NADP+ oxidoreductase (L-glutamyl-tRNAGlu-forming)
Comments: This enzyme forms part of the pathway for the biosynthesis of 5-aminolevulinate from glutamate, known as the C5 pathway. The route shown in the diagram is used in most eubacteria, and in all archaebacteria, algae and plants. However, in the α-proteobacteria, EC 2.3.1.37, 5-aminolevulinate synthase, is used in an alternative route to produce the product 5-aminolevulinate from succinyl-CoA and glycine. This route is found in the mitochondria of fungi and animals, organelles that are considered to be derived from an endosymbiotic α-proteobacterium. Although higher plants do not possess EC 2.3.1.37, the protistan Euglena gracilis possesses both the C5 pathway and EC 2.3.1.37.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 119940-26-0
References:
1.  von Wettstein, D., Gough, S. and Kannangara, C.G. Chlorophyll biosynthesis. Plant Cell 7 (1995) 1039–1057. [DOI] [PMID: 12242396]
2.  Pontoppidan, B. and Kannangara, C.G. Purification and partial characterisation of barley glutamyl-tRNAGlu reductase, the enzyme that directs glutamate to chlorophyll biosynthesis. Eur. J. Biochem. 225 (1994) 529–537. [DOI] [PMID: 7957167]
3.  Schauer, S., Chaturvedi, S., Randau, L., Moser, J., Kitabatake, M., Lorenz, S., Verkamp, E., Schubert, W.D., Nakayashiki, T., Murai, M., Wall, K., Thomann, H.-U., Heinz, D.W., Inokuchi, H, Söll, D. and Jahn, D. Escherichia coli glutamyl-tRNA reductase. Trapping the thioester intermediate. J. Biol. Chem. 277 (2002) 48657–48663. [DOI] [PMID: 12370189]
[EC 1.2.1.70 created 2004]
 
 
EC 1.2.1.94     
Accepted name: farnesal dehydrogenase
Reaction: (2E,6E)-farnesal + NAD+ + H2O = (2E,6E)-farnesoate + NADH + 2 H+
For diagram of juvenile hormone biosynthesis, click here
Glossary: farnesal = 3,7,11-trimethyldodeca-2,6,10-trienal
farnesoate = 3,7,11-trimethyldodeca-2,6,10-trienoate
Other name(s): AaALDH3
Systematic name: farnesal:NAD+ oxidoreductase
Comments: Invoved in juvenile hormone production in insects. The enzyme was described from the corpora allata of Drosophila melanogaster (fruit fly), Manduca sexta (tobacco hornworm) and Aedes aegypti (dengue mosquito).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Madhavan, K., Conscience-Egli, M., Sieber, F. and Ursprung, H. Farnesol metabolism in Drosophila melanogaster: ontogeny and tissue distribution of octanol dehydrogenase and aldehyde oxidase. J. Insect Physiol. 19 (1973) 235–241. [DOI] [PMID: 4631837]
2.  Baker, F.C., Mauchamp, B., Tsai, L.W. and Schooley, D.A. Farnesol and farnesal dehydrogenase(s) in corpora allata of the tobacco hornworm moth, Manduca sexta. J. Lipid Res. 24 (1983) 1586–1594. [PMID: 6366103]
3.  Rivera-Perez, C., Nouzova, M., Clifton, M.E., Garcia, E.M., LeBlanc, E. and Noriega, F.G. Aldehyde dehydrogenase 3 converts farnesal into farnesoic acid in the corpora allata of mosquitoes. Insect Biochem. Mol. Biol. 43 (2013) 675–682. [DOI] [PMID: 23639754]
[EC 1.2.1.94 created 2015]
 
 
EC 1.2.1.95     
Accepted name: L-2-aminoadipate reductase
Reaction: (S)-2-amino-6-oxohexanoate + NADP+ + AMP + diphosphate = L-2-aminoadipate + NADPH + H+ + ATP (overall reaction)
(1a) L-2-aminoadipyl-[LYS2 peptidyl-carrier-protein] + AMP + diphosphate = L-2-aminoadipate + holo-[LYS2 peptidyl-carrier-protein] + ATP
(1b) (S)-2-amino-6-oxohexanoate + holo-[LYS2 peptidyl-carrier-protein] + NADP+ = L-2-aminoadipyl-[LYS2 peptidyl-carrier-protein] + NADPH + H+
Glossary: L-2-aminoadipate = (2S)-2-aminohexanedioate
Other name(s): LYS2; α-aminoadipate reductase
Systematic name: (S)-2-amino-6-oxohexanoate:NADP+ oxidoreductase (ATP-forming)
Comments: This enzyme, characterized from the yeast Saccharomyces cerevisiae, catalyses the reduction of L-2-aminoadipate to (S)-2-amino-6-oxohexanoate during L-lysine biosynthesis. An adenylation domain activates the substrate at the expense of ATP hydrolysis, and forms L-2-aminoadipate adenylate, which is attached to a peptidyl-carrier protein (PCP) domain. Binding of NADPH results in reductive cleavage of the acyl-S-enzyme intermediate, releasing (S)-2-amino-6-oxohexanoate. Different from EC 1.2.1.31, L-aminoadipate-semialdehyde dehydrogenase, which catalyses a similar transformation in the opposite direction without ATP hydrolysis.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Ehmann, D.E., Gehring, A.M. and Walsh, C.T. Lysine biosynthesis in Saccharomyces cerevisiae: mechanism of α-aminoadipate reductase (Lys2) involves posttranslational phosphopantetheinylation by Lys5. Biochemistry 38 (1999) 6171–6177. [DOI] [PMID: 10320345]
[EC 1.2.1.95 created 2015]
 
 
EC 1.2.1.101     
Accepted name: L-tyrosine reductase
Reaction: L-tyrosinal + NADP+ + AMP + diphosphate = L-tyrosine + NADPH + H+ + ATP
Glossary: L-tyrosinal = (2S)-2-amino-3-(4-hydroxyphenyl)propanal
Other name(s): lnaA (gene name); lnbA (gene name)
Systematic name: (2S)-2-amino-3-(4-hydroxyphenyl)propanal:NADP+ oxidoreductase (ATP-forming)
Comments: The enzyme, characterized from the ascomycete fungus Aspergillus flavus, is specific for L-tyrosine. It contains three domains - an adenylation domain, a peptidyl-carrier protein (PCP) domain, and a reductase domain, and requires activation by attachment of a phosphopantetheinyl group. The enzyme activates its substrate to an adenylate form, followed by a transfer to the PCP domain. The resulting thioester is subsequently transferred to the reductase domain, where it is reduced to the aldehyde.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9074-94-6
References:
1.  Forseth, R.R., Amaike, S., Schwenk, D., Affeldt, K.J., Hoffmeister, D., Schroeder, F.C. and Keller, N.P. Homologous NRPS-like gene clusters mediate redundant small-molecule biosynthesis in Aspergillus flavus. Angew. Chem. Int. Ed. Engl. 52 (2013) 1590–1594. [PMID: 23281040]
[EC 1.2.1.101 created 2018]
 
 
EC 1.2.7.1     
Accepted name: pyruvate synthase
Reaction: pyruvate + CoA + 2 oxidized ferredoxin = acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
For diagram of the 3-hydroxypropanoate/4-hydroxybutanoate cycle and dicarboxylate/4-hydroxybutanoate cycle in archaea, click here
Other name(s): pyruvate oxidoreductase; pyruvate synthetase; pyruvate:ferredoxin oxidoreductase; pyruvic-ferredoxin oxidoreductase; 2-oxobutyrate synthase; α-ketobutyrate-ferredoxin oxidoreductase; 2-ketobutyrate synthase; α-ketobutyrate synthase; 2-oxobutyrate-ferredoxin oxidoreductase; 2-oxobutanoate:ferredoxin 2-oxidoreductase (CoA-propionylating); 2-oxobutanoate:ferredoxin 2-oxidoreductase (CoA-propanoylating)
Systematic name: pyruvate:ferredoxin 2-oxidoreductase (CoA-acetylating)
Comments: Contains thiamine diphosphate and [4Fe-4S] clusters. The enzyme also decarboxylates 2-oxobutyrate with lower efficiency, but shows no activity with 2-oxoglutarate. 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 examples of other members of this family, 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, KEGG, MetaCyc, PDB, CAS registry number: 9082-51-3
References:
1.  Evans, M.C.W. and Buchanan, B.B. Photoreduction of ferredoxin and its use in carbon dioxide fixation by a subcellular system from a photosynthetic bacterium. Proc. Natl. Acad. Sci. USA 53 (1965) 1420–1425. [DOI] [PMID: 5217644]
2.  Gehring, U. and Arnon, D.I. Purification and properties of α-ketoglutarate synthase from a photosynthetic bacterium. J. Biol. Chem. 247 (1972) 6963–6969. [PMID: 4628267]
3.  Uyeda, K. and Rabinowitz, J.C. Pyruvate-ferredoxin oxidoreductase. 3. Purification and properties of the enzyme. J. Biol. Chem. 246 (1971) 3111–3119. [PMID: 5574389]
4.  Uyeda, K. and Rabinowitz, J.C. Pyruvate-ferredoxin oxidoreductase. IV. Studies on the reaction mechanism. J. Biol. Chem. 246 (1971) 3120–3125. [PMID: 4324891]
5.  Charon, M.-H., Volbeda, A., Chabriere, E., Pieulle, L. and Fontecilla-Camps, J.C. Structure and electron transfer mechanism of pyruvate:ferredoxin oxidoreductase. Curr. Opin. Struct. Biol. 9 (1999) 663–669. [DOI] [PMID: 10607667]
[EC 1.2.7.1 created 1972, modified 2003, modified 2013]
 
 
EC 1.2.7.3     
Accepted name: 2-oxoglutarate synthase
Reaction: 2-oxoglutarate + CoA + 2 oxidized ferredoxin = succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
Other name(s): 2-ketoglutarate ferredoxin oxidoreductase; 2-oxoglutarate:ferredoxin oxidoreductase; KGOR; 2-oxoglutarate ferredoxin oxidoreductase; 2-oxoglutarate:ferredoxin 2-oxidoreductase (CoA-succinylating)
Systematic name: 2-oxoglutarate:ferredoxin oxidoreductase (decarboxylating)
Comments: The enzyme contains thiamine diphosphate and two [4Fe-4S] clusters. Highly specific for 2-oxoglutarate. 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 examples of other members of this family, see EC 1.2.7.1, pyruvate synthase and EC 1.2.7.7, 3-methyl-2-oxobutanoate dehydrogenase (ferredoxin).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37251-05-1
References:
1.  Buchanan, B.B. and Evans, M.C.W. The synthesis of α-ketoglutarate from succinate and carbon dioxide by a subcellular preparation of a photosynthetic bacterium. Proc. Natl. Acad. Sci. USA 54 (1965) 1212–1218. [DOI] [PMID: 4286833]
2.  Gehring, U. and Arnon, D.I. Purification and properties of α-ketoglutarate synthase from a photosynthetic bacterium. J. Biol. Chem. 247 (1972) 6963–6969. [PMID: 4628267]
3.  Dorner, E. and Boll, M. Properties of 2-oxoglutarate:ferredoxin oxidoreductase from Thauera aromatica and its role in enzymatic reduction of the aromatic ring. J. Bacteriol. 184 (2002) 3975–3983. [DOI] [PMID: 12081970]
4.  Mai, X. and Adams, M.W. Characterization of a fourth type of 2-keto acid-oxidizing enzyme from a hyperthermophilic archaeon: 2-ketoglutarate ferredoxin oxidoreductase from Thermococcus litoralis. J. Bacteriol. 178 (1996) 5890–5896. [DOI] [PMID: 8830683]
5.  Schut, G.J., Menon, A.L. and Adams, M.W.W. 2-Keto acid oxidoreductases from Pyrococcus furiosus and Thermococcus litoralis. Methods Enzymol. 331 (2001) 144–158. [DOI] [PMID: 11265457]
[EC 1.2.7.3 created 1972, modified 2005]
 
 
EC 1.2.7.7     
Accepted name: 3-methyl-2-oxobutanoate dehydrogenase (ferredoxin)
Reaction: 3-methyl-2-oxobutanoate + CoA + 2 oxidized ferredoxin = S-(2-methylpropanoyl)-CoA + CO2 + 2 reduced ferredoxin + H+
Other name(s): 2-ketoisovalerate ferredoxin reductase; 3-methyl-2-oxobutanoate synthase (ferredoxin); VOR; branched-chain ketoacid ferredoxin reductase; branched-chain oxo acid ferredoxin reductase; keto-valine-ferredoxin oxidoreductase; ketoisovalerate ferredoxin reductase; 2-oxoisovalerate ferredoxin reductase
Systematic name: 3-methyl-2-oxobutanoate:ferredoxin oxidoreductase (decarboxylating; CoA-2-methylpropanoylating)
Comments: The enzyme is CoA-dependent and contains thiamine diphosphate and iron-sulfur clusters. Preferentially utilizes 2-oxo-acid derivatives of branched chain amino acids, e.g. 3-methyl-2-oxopentanoate, 4-methyl-2-oxo-pentanoate, and 2-oxobutanoate. This enzyme is a member of the 2-oxoacid oxidoreductases, a family of enzymes that reversibly catalyse the oxidative decarboxylation of different 2-oxoacids to form their CoA derivatives, and are differentiated based on their substrate specificity. For examples of other members of this family, see EC 1.2.7.1, pyruvate synthase, and EC 1.2.7.3, 2-oxoglutarate synthase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Buchanan, B.B. Role of ferredoxin in the synthesis of α-ketobutyrate from propionyl coenzyme A and carbon dioxide by enzymes from photosynthetic and nonphotosynthetic bacteria. J. Biol. Chem. 244 (1969) 4218–4223. [PMID: 5800441]
2.  Heider, J., Mai, X.H. and Adams, M.W.W. Characterization of 2-ketoisovalerate ferredoxin oxidoreductase, a new and reversible coenzyme A-dependent enzyme involved in peptide fermentation by hyperthermophilic archaea. J. Bacteriol. 178 (1996) 780–787. [DOI] [PMID: 8550513]
3.  Tersteegen, A., Linder, D., Thauer, R.K. and Hedderich, R. Structures and functions of four anabolic 2-oxoacid oxidoreductases in Methanobacterium thermoautotrophicum. Eur. J. Biochem. 244 (1997) 862–868. [DOI] [PMID: 9108258]
4.  Schut, G.J., Menon, A.L. and Adams, M.W.W. 2-Keto acid oxidoreductases from Pyrococcus furiosus and Thermococcus litoralis. Methods Enzymol. 331 (2001) 144–158. [DOI] [PMID: 11265457]
[EC 1.2.7.7 created 2003]
 
 
EC 1.2.7.8     
Accepted name: indolepyruvate ferredoxin oxidoreductase
Reaction: (indol-3-yl)pyruvate + CoA + 2 oxidized ferredoxin = S-2-(indol-3-yl)acetyl-CoA + CO2 + 2 reduced ferredoxin + H+
Other name(s): 3-(indol-3-yl)pyruvate synthase (ferredoxin); IOR
Systematic name: 3-(indol-3-yl)pyruvate:ferredoxin oxidoreductase (decarboxylating, CoA-indole-acetylating)
Comments: Contains thiamine diphosphate and [4Fe-4S] clusters. Preferentially utilizes the transaminated forms of aromatic amino acids and can use phenylpyruvate and p-hydroxyphenylpyruvate as substrates. This enzyme, which is found in archaea, 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 examples of other members of this family, 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, KEGG, MetaCyc, CAS registry number: 158886-06-7
References:
1.  Mai, X.H. and Adams, M.W.W. Indolepyruvate ferredoxin oxidoreductase from the hyperthermophilic archaeon Pyrococcus furiosus - a new enzyme involved in peptide fermentation. J. Biol. Chem. 269 (1994) 16726–16732. [PMID: 8206994]
2.  Siddiqui, M.A., Fujiwara, S. and Imanaka, T. Indolepyruvate ferredoxin oxidoreductase from Pyrococcus sp. K0d1 possesses a mosaic: Structure showing features of various oxidoreductases. Mol. Gen. Genet. 254 (1997) 433–439. [PMID: 9180697]
3.  Tersteegen, A., Linder, D., Thauer, R.K. and Hedderich, R. Structures and functions of four anabolic 2-oxoacid oxidoreductases in Methanobacterium thermoautotrophicum. Eur. J. Biochem. 244 (1997) 862–868. [DOI] [PMID: 9108258]
4.  Schut, G.J., Menon, A.L. and Adams, M.W.W. 2-Keto acid oxidoreductases from Pyrococcus furiosus and Thermococcus litoralis. Methods Enzymol. 331 (2001) 144–158. [DOI] [PMID: 11265457]
[EC 1.2.7.8 created 2003]
 
 
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, KEGG, MetaCyc, PDB
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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [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 1.3.1.1     
Accepted name: dihydropyrimidine dehydrogenase (NAD+)
Reaction: (1) 5,6-dihydrouracil + NAD+ = uracil + NADH + H+
(2) 5,6-dihydrothymine + NAD+ = thymine + NADH + H+
Other name(s): dihydropyrimidine dehydrogenase; dihydrothymine dehydrogenase; pyrimidine reductase; thymine reductase; uracil reductase; dihydrouracil dehydrogenase (NAD+)
Systematic name: 5,6-dihydropyrimidine:NAD+ oxidoreductase
Comments: An iron-sulfur flavoenzyme. The enzyme was originally discovered in the uracil-fermenting bacterium, Clostridium uracilicum, which utilizes uracil and thymine as nitrogen and carbon sources for growth [1]. Since then the enzyme was found in additional organisms including Alcaligenes eutrophus [2], Pseudomonas strains [3,4] and Escherichia coli [5,6].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9026-89-5
References:
1.  Campbell, L.L. Reductive degradation of pyrimidines. III. Purificaion and properties of dihydrouracil dehydrogenase. J. Biol. Chem. 227 (1957) 693–700. [PMID: 13462991]
2.  Schmitt, U., Jahnke, K., Rosenbaum, K., Cook, P.F. and Schnackerz, K.D. Purification and characterization of dihydropyrimidine dehydrogenase from Alcaligenes eutrophus. Arch. Biochem. Biophys. 332 (1996) 175–182. [DOI] [PMID: 8806723]
3.  Kim, S. and West, T.P. Pyrimidine catabolism in Pseudomonas aeruginosa. FEMS Microbiol. Lett. 61 (1991) 175–179. [PMID: 1903745]
4.  West, T.P. Pyrimidine base catabolism in Pseudomonas putida biotype B. Antonie Van Leeuwenhoek 80 (2001) 163–167. [PMID: 11759049]
5.  West, T.P. Isolation and characterization of an Escherichia coli B mutant strain defective in uracil catabolism. Can. J. Microbiol. 44 (1998) 1106–1109. [PMID: 10030006]
6.  Hidese, R., Mihara, H., Kurihara, T. and Esaki, N. Escherichia coli dihydropyrimidine dehydrogenase is a novel NAD-dependent heterotetramer essential for the production of 5,6-dihydrouracil. J. Bacteriol. 193 (2011) 989–993. [DOI] [PMID: 21169495]
[EC 1.3.1.1 created 1961, modified 2011]
 
 
EC 1.3.1.22     
Accepted name: 3-oxo-5α-steroid 4-dehydrogenase (NADP+)
Reaction: a 3-oxo-5α-steroid + NADP+ = a 3-oxo-Δ4-steroid + NADPH + H+
Other name(s): cholestenone 5α-reductase; testosterone Δ4-5α-reductase; steroid 5α-reductase; 3-oxosteroid Δ4-dehydrogenase; 5α-reductase; steroid 5α-hydrogenase; 3-oxosteroid 5α-reductase; testosterone Δ4-hydrogenase; 4-ene-3-oxosteroid 5α-reductase; reduced nicotinamide adenine dinucleotide phosphate:Δ4-3-ketosteroid 5α-oxidoreductase; 4-ene-5α-reductase; Δ4-3-ketosteroid 5α-oxidoreductase; cholest-4-en-3-one 5α-reductase; testosterone 5α-reductase; 3-oxo-5α-steroid 4-dehydrogenase
Systematic name: 3-oxo-5α-steroid:NADP+ Δ4-oxidoreductase
Comments: The enzyme catalyses the conversion of assorted 3-oxo-Δ4 steroids into their corresponding 5α form. Substrates for the mammalian enzyme include testosterone, progesterone, and corticosterone. Substrates for the plant enzyme are brassinosteroids such as campest-4-en-3-one and (22α)-hydroxy-campest-4-en-3-one. cf. EC 1.3.99.5, 3-oxo-5α-steroid 4-dehydrogenase (acceptor).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37255-34-8
References:
1.  Levy, H.R. and Talalay, P. Bacterial oxidation of steroids. II. Studies on the enzymatic mechanisms of ring A dehydrogenation. J. Biol. Chem. 234 (1959) 2014–2021. [PMID: 13673006]
2.  Shefer, S., Hauser, S. and Mosbach, E.H. Studies on the biosynthesis of 5α-cholestan-3β-ol. I. Cholestenone 5α-reductase of rat liver. J. Biol. Chem. 241 (1966) 946–952. [PMID: 5907469]
3.  Cheng, Y.-J. and Karavolas, H.J. Properties and subcellular distribution of Δ4-steroid (progesterone) 5α-reductase in rat anterior pituitary. Steroids 26 (1975) 57–71. [DOI] [PMID: 1166484]
4.  Sargent, N.S. and Habib, F.K. Partial purification of human prostatic 5α-reductase (3-oxo-5α-steroid:NADP+ 4-ene-oxido-reductase; EC 1.3.1.22) in a stable and active form. J. Steroid Biochem. Mol. Biol. 38 (1991) 73–77. [DOI] [PMID: 1705142]
5.  Quemener, E., Amet, Y., di Stefano, S., Fournier, G., Floch, H.H. and Abalain, J.H. Purification of testosterone 5α-reductase from human prostate by a four-step chromatographic procedure. Steroids 59 (1994) 712–718. [DOI] [PMID: 7900170]
6.  Poletti, A., Celotti, F., Rumio, C., Rabuffetti, M. and Martini, L. Identification of type 1 5α-reductase in myelin membranes of male and female rat brain. Mol. Cell. Endocrinol. 129 (1997) 181–190. [DOI] [PMID: 9202401]
7.  Li, J., Biswas, M.G., Chao, A., Russell, D.W. and Chory, J. Conservation of function between mammalian and plant steroid 5α-reductases. Proc. Natl. Acad. Sci. USA 94 (1997) 3554–3559. [DOI] [PMID: 9108014]
8.  Rosati, F., Bardazzi, I., De Blasi, P., Simi, L., Scarpi, D., Guarna, A., Serio, M., Racchi, M.L. and Danza, G. 5α-Reductase activity in Lycopersicon esculentum: cloning and functional characterization of LeDET2 and evidence of the presence of two isoenzymes. J. Steroid Biochem. Mol. Biol. 96 (2005) 287–299. [DOI] [PMID: 15993049]
[EC 1.3.1.22 created 1972, modified 2012]
 
 
EC 1.3.1.121     
Accepted name: 4-amino-4-deoxyprephenate dehydrogenase
Reaction: 4-amino-4-deoxyprephenate + NAD+ = 3-(4-aminophenyl)pyruvate + CO2 + NADH + H+
Other name(s): cmlC (gene name); papC (gene name)
Systematic name: 4-amino-4-deoxyprephenate:NAD+ oxidoreductase (decarboxylating)
Comments: The enzyme, characterized from the bacteria Streptomyces venezuelae and Streptomyces pristinaespiralis, participates in the biosynthesis of the antibiotics chloramphenicol and pristinamycin IA, respectively. cf. EC 1.3.1.12, prephenate dehydrogenase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Blanc, V., Gil, P., Bamas-Jacques, N., Lorenzon, S., Zagorec, M., Schleuniger, J., Bisch, D., Blanche, F., Debussche, L., Crouzet, J. and Thibaut, D. Identification and analysis of genes from Streptomyces pristinaespiralis encoding enzymes involved in the biosynthesis of the 4-dimethylamino-L-phenylalanine precursor of pristinamycin I. Mol. Microbiol. 23 (1997) 191–202. [PMID: 9044253]
2.  He, J., Magarvey, N., Piraee, M. and Vining, L.C. The gene cluster for chloramphenicol biosynthesis in Streptomyces venezuelae ISP5230 includes novel shikimate pathway homologues and a monomodular non-ribosomal peptide synthetase gene. Microbiology 147 (2001) 2817–2829. [PMID: 11577160]
[EC 1.3.1.121 created 2019]
 
 
EC 1.4.1.26     
Accepted name: 2,4-diaminopentanoate dehydrogenase (NAD+)
Reaction: (2R,4S)-2,4-diaminopentanoate + H2O + NAD+ = (2R)-2-amino-4-oxopentanoate + NH3 + NADH + H+
Other name(s): DAPDH (ambiguous)
Systematic name: (2R,4S)-2,4-diaminopentanoate:NADP+ oxidoreductase (deaminating)
Comments: The enzyme, characterized from an unknown bacterium in an environmental sample, has some activity with (2R,4R)-2,4-diaminopentanoate. It has very low activity with NADP+ (cf. EC 1.4.1.12, 2,4-diaminopentanoate dehydrogenase).
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc
References:
1.  Fonknechten, N., Perret, A., Perchat, N., Tricot, S., Lechaplais, C., Vallenet, D., Vergne, C., Zaparucha, A., Le Paslier, D., Weissenbach, J. and Salanoubat, M. A conserved gene cluster rules anaerobic oxidative degradation of L-ornithine. J. Bacteriol. 191 (2009) 3162–3167. [DOI] [PMID: 19251850]
[EC 1.4.1.26 created 2017]
 
 
EC 1.4.3.13     
Accepted name: protein-lysine 6-oxidase
Reaction: [protein]-L-lysine + O2 + H2O = [protein]-(S)-2-amino-6-oxohexanoate + NH3 + H2O2
Glossary: (S)-2-amino-6-oxohexanoate = L-allysine
Other name(s): lysyl oxidase
Systematic name: protein-L-lysine:oxygen 6-oxidoreductase (deaminating)
Comments: Also acts on protein 5-hydroxylysine. This enzyme catalyses the final known enzymic step required for collagen and elastin cross-linking in the biosynthesis of normal mature extracellular matrices [4]. These reactions play an important role for the development, elasticity and extensibility of connective tissue. The enzyme is also active on free amines, such as cadaverine or benzylamine [4,5]. Some isoforms can also use [protein]-N(6)-acetyl-L-lysine as substrate deacetamidating the substrate [6].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 99676-44-5
References:
1.  Harris, E.D., Gonnerman, W.A., Savage, J.E. and O'Dell, B.L. Connective tissue amine oxidase. II. Purification and partial characterization of lysyl oxidase from chick aorta. Biochim. Biophys. Acta 341 (1974) 332–344. [DOI] [PMID: 4838158]
2.  Rayton, J.K. and Harris, E.D. Induction of lysyl oxidase with copper. Properties of an in vitro system. J. Biol. Chem. 254 (1979) 621–626. [PMID: 33171]
3.  Stassen, F.L.H. Properties of highly purified lysyl oxidase from embryonic chick cartilage. Biochim. Biophys. Acta 438 (1976) 49–60. [DOI] [PMID: 7318]
4.  Palamakumbura, A.H. and Trackman, P.C. A fluorometric assay for detection of lysyl oxidase enzyme activity in biological samples. Anal. Biochem. 300 (2002) 245–251. [DOI] [PMID: 11779117]
5.  Kagan, H.M., Williams, M.A., Williamson, P.R. and Anderson, J.M. Influence of sequence and charge on the specificity of lysyl oxidase toward protein and synthetic peptide substrates. J. Biol. Chem. 259 (1984) 11203–11207. [PMID: 6147351]
6.  Rodriguez, H.M., Vaysberg, M., Mikels, A., McCauley, S., Velayo, A.C., Garcia, C. and Smith, V. Modulation of lysyl oxidase-like 2 enzymatic activity by an allosteric antibody inhibitor. J. Biol. Chem. 285 (2010) 20964–20974. [DOI] [PMID: 20439985]
7.  Kim, Y.M., Kim, E.C. and Kim, Y. The human lysyl oxidase-like 2 protein functions as an amine oxidase toward collagen and elastin. Mol. Biol. Rep. 38 (2011) 145–149. [DOI] [PMID: 20306300]
8.  Xu, L., Go, E.P., Finney, J., Moon, H., Lantz, M., Rebecchi, K., Desaire, H. and Mure, M. Post-translational modifications of recombinant human lysyl oxidase-like 2 (rhLOXL2) secreted from Drosophila S2 cells. J. Biol. Chem. 288 (2013) 5357–5363. [DOI] [PMID: 23319596]
9.  Ma, L., Huang, C., Wang, X.J., Xin, D.E., Wang, L.S., Zou, Q.C., Zhang, Y.S., Tan, M.D., Wang, Y.M., Zhao, T.C., Chatterjee, D., Altura, R.A., Wang, C., Xu, Y.S., Yang, J.H., Fan, Y.S., Han, B.H., Si, J., Zhang, X., Cheng, J., Chang, Z. and Chin, Y.E. Lysyl oxidase 3 is a dual-specificity enzyme involved in STAT3 deacetylation and deacetylimination modulation. Mol. Cell 65 (2017) 296–309. [PMID: 28065600]
[EC 1.4.3.13 created 1980, modified 1983]
 
 
EC 1.5.1.43     
Accepted name: carboxynorspermidine synthase
Reaction: (1) carboxynorspermidine + H2O + NADP+ = L-aspartate 4-semialdehyde + propane-1,3-diamine + NADPH + H+
(2) carboxyspermidine + H2O + NADP+ = L-aspartate 4-semialdehyde + putrescine + NADPH + H+
Other name(s): carboxynorspermidine dehydrogenase; carboxyspermidine dehydrogenase; CASDH; CANSDH; VC1624 (gene name)
Systematic name: carboxynorspermidine:NADP+ oxidoreductase
Comments: The reaction takes place in the opposite direction. Part of a bacterial polyamine biosynthesis pathway. L-aspartate 4-semialdehyde and propane-1,3-diamine/putrescine form a Schiff base that is reduced to form carboxynorspermidine/carboxyspermidine, respectively [1]. The enzyme from the bacterium Vibrio cholerae is essential for biofilm formation [2]. The enzyme from Campylobacter jejuni only produces carboxyspermidine in vivo even though it also can produce carboxynorspermidine in vitro [3].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Nakao, H., Shinoda, S. and Yamamoto, S. Purification and some properties of carboxynorspermidine synthase participating in a novel biosynthetic pathway for norspermidine in Vibrio alginolyticus. J. Gen. Microbiol. 137 (1991) 1737–1742. [DOI] [PMID: 1955861]
2.  Lee, J., Sperandio, V., Frantz, D.E., Longgood, J., Camilli, A., Phillips, M.A. and Michael, A.J. An alternative polyamine biosynthetic pathway is widespread in bacteria and essential for biofilm formation in Vibrio cholerae. J. Biol. Chem. 284 (2009) 9899–9907. [DOI] [PMID: 19196710]
3.  Hanfrey, C.C., Pearson, B.M., Hazeldine, S., Lee, J., Gaskin, D.J., Woster, P.M., Phillips, M.A. and Michael, A.J. Alternative spermidine biosynthetic route is critical for growth of Campylobacter jejuni and is the dominant polyamine pathway in human gut microbiota. J. Biol. Chem. 286 (2011) 43301–43312. [DOI] [PMID: 22025614]
[EC 1.5.1.43 created 2012]
 
 
EC 1.5.8.2     
Accepted name: trimethylamine dehydrogenase
Reaction: trimethylamine + H2O + electron-transfer flavoprotein = dimethylamine + formaldehyde + reduced electron-transfer flavoprotein
Systematic name: trimethylamine:electron-transfer flavoprotein oxidoreductase (demethylating)
Comments: A number of alkyl-substituted derivatives of trimethylamine can also act as electron donors; phenazine methosulfate and 2,6-dichloroindophenol can act as electron acceptors. Contains FAD and a [4Fe-4S] cluster.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 39307-09-0
References:
1.  Colby, J. and Zatman, L.J. The purification and properties of a bacterial trimethylamine dehydrogenase. Biochem. J. 121 (1971) 9P–10P. [PMID: 5116569]
2.  Steenkamp, D.J. and Singer, T.P. Participation of the iron-sulphur cluster and of the covalently bound coenzyme of trimethylamine dehydrogenase in catalysis. Biochem. J. 169 (1978) 361–369. [PMID: 204297]
3.  Huang, L.X., Rohlfs, R.J. and Hille, R. The reaction of trimethylamine dehydrogenase with electron transferring flavoprotein. J. Biol. Chem. 270 (1995) 23958–23965. [DOI] [PMID: 7592591]
4.  Jones, M., Talfournier, F., Bobrov, A., Grossmann, J.G., Vekshin, N., Sutcliffe, M.J. and Scrutton, N.S. Electron transfer and conformational change in complexes of trimethylamine dehydrogenase and electron transferring flavoprotein. J. Biol. Chem. 277 (2002) 8457–8465. [DOI] [PMID: 11756429]
5.  Scrutton, N.S. and Sutcliffe, M.J. Trimethylamine dehydrogenase and electron transferring flavoprotein. Subcell. Biochem. 35 (2000) 145–181. [PMID: 11192721]
[EC 1.5.8.2 created 1976 as EC 1.5.99.7, transferred 2002 to EC 1.5.8.2]
 
 
EC 1.5.8.3     
Accepted name: sarcosine dehydrogenase
Reaction: sarcosine + 5,6,7,8-tetrahydrofolate + oxidized [electron-transfer flavoprotein] = glycine + 5,10-methylenetetrahydrofolate + reduced [electron-transfer flavoprotein]
Other name(s): sarcosine N-demethylase; monomethylglycine dehydrogenase; sarcosine:(acceptor) oxidoreductase (demethylating); sarcosine:electron-transfer flavoprotein oxidoreductase (demethylating)
Systematic name: sarcosine, 5,6,7,8-tetrahydrofolate:electron-transferflavoprotein oxidoreductase (demethylating,5,10-methylenetetrahydrofolate-forming)
Comments: A flavoprotein (FMN) found in eukaryotes. In the absence of tetrahydrofolate the enzyme produces formaldehyde. cf. EC 1.5.3.1, sarcosine oxidase (formaldehyde-forming), and EC 1.5.3.24, sarcosine oxidase (5,10-methylenetetrahydrofolate-forming).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37228-65-2, 93389-49-2
References:
1.  Hoskins, D.D. and MacKenzie, C.G. Solubilization and electron transfer flavoprotein requirement of mitochondrial sarcosine dehydrogenase and dimethylglycine dehydrogenase. J. Biol. Chem. 236 (1961) 177–183. [DOI] [PMID: 13716069]
2.  Frisell, W.R. and MacKenzie, C.G. Separation and purification of sarcosine dehydrogenase and dimethylglycine dehydrogenase. J. Biol. Chem. 237 (1962) 94–98. [DOI] [PMID: 13895406]
3.  Wittwer, A.J. and Wagner, C. Identification of the folate-binding proteins of rat liver mitochondria as dimethylglycine dehydrogenase and sarcosine dehydrogenase. Flavoprotein nature and enzymatic properties of the purified proteins. J. Biol. Chem. 256 (1981) 4109–4115. [DOI] [PMID: 6163778]
4.  Steenkamp, D.J. and Husain, M. The effect of tetrahydrofolate on the reduction of electron transfer flavoprotein by sarcosine and dimethylglycine dehydrogenases. Biochem. J. 203 (1982) 707–715. [DOI] [PMID: 6180732]
[EC 1.5.8.3 created 1972 as EC 1.5.99.1, transferred 2012 to EC 1.5.8.3, modified 2022]
 
 
EC 1.6.5.11      
Deleted entry: NADH dehydrogenase (quinone). Identical to EC 1.6.5.9, NADH:quinone reductase (non-electrogenic)
[EC 1.6.5.11 created 1972 as EC 1.6.99.5, transferred 2015 to EC 1.6.5.11, deleted 2019]
 
 
EC 1.6.99.5      
Transferred entry: NADH dehydrogenase (quinone). Transferred to EC 1.6.5.11, NADH dehydrogenase (quinone)
[EC 1.6.99.5 created 1972, deleted 2014]
 
 
EC 1.7.1.2     
Accepted name: nitrate reductase [NAD(P)H]
Reaction: nitrite + NAD(P)+ + H2O = nitrate + NAD(P)H + H+
Other name(s): assimilatory nitrate reductase ( ambiguous); assimilatory NAD(P)H-nitrate reductase; NAD(P)H bispecific nitrate reductase; nitrate reductase (reduced nicotinamide adenine dinucleotide (phosphate)); nitrate reductase NAD(P)H; NAD(P)H-nitrate reductase; nitrate reductase [NAD(P)H2]; NAD(P)H2:nitrate oxidoreductase
Systematic name: nitrite:NAD(P)+ oxidoreductase
Comments: An iron-sulfur molybdenum flavoprotein.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9029-27-0
References:
1.  Nason, A. Nitrate reductases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 7, Academic Press, New York, 1963, pp. 587–607.
2.  Paneque, A., Del Campo, F.F., Ramirez, J.M. and Losada, M. Flavin nucleotide nitrate reductase from spinach. Biochim. Biophys. Acta 109 (1965) 79–85. [PMID: 5864033]
3.  Campbell, W.H. Structure and function of eukaryotic NAD(P)H:nitrate reductase. Cell. Mol. Life Sci. 58 (2001) 194–204. [DOI] [PMID: 11289301]
4.  Berks, B.C., Ferguson, S.J., Moir, J.W. and Richardson, D.J. Enzymes and associated electron transport systems that catalyse the respiratory reduction of nitrogen oxides and oxyanions. Biochim. Biophys. Acta 1232 (1995) 97–173. [DOI] [PMID: 8534676]
[EC 1.7.1.2 created 1961 as EC 1.6.6.2, transferred 2002 to EC 1.7.1.2]
 
 
EC 1.7.2.7     
Accepted name: hydrazine synthase
Reaction: hydrazine + H2O + 3 ferricytochrome c = nitric oxide + ammonium + 3 ferrocytochrome c
Glossary: nitric oxide = nitrogen monoxide = NO
Other name(s): HZS
Systematic name: hydrazine:ferricytochrome-c oxidoreductase
Comments: The enzyme, characterized from anaerobic ammonia oxidizers (anammox bacteria), is one of only a few enzymes that are known to form an N-N bond (other examples include EC 1.7.1.14, nitric oxide reductase [NAD(P)+, nitrous oxide-forming] and EC 4.8.1.1, L-piperazate synthase). The enzyme from the bacterium Candidatus Kuenenia stuttgartiensis is a dimer of heterotrimers and contains multiple c-type cytochromes.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Kartal, B., Maalcke, W.J., de Almeida, N.M., Cirpus, I., Gloerich, J., Geerts, W., Op den Camp, H.J., Harhangi, H.R., Janssen-Megens, E.M., Francoijs, K.J., Stunnenberg, H.G., Keltjens, J.T., Jetten, M.S. and Strous, M. Molecular mechanism of anaerobic ammonium oxidation. Nature 479 (2011) 127–130. [DOI] [PMID: 21964329]
2.  Dietl, A., Ferousi, C., Maalcke, W.J., Menzel, A., de Vries, S., Keltjens, J.T., Jetten, M.S., Kartal, B. and Barends, T.R. The inner workings of the hydrazine synthase multiprotein complex. Nature 527 (2015) 394–397. [DOI] [PMID: 26479033]
[EC 1.7.2.7 created 2016, modified 2021]
 
 
EC 1.7.2.8     
Accepted name: hydrazine dehydrogenase
Reaction: hydrazine + 4 ferricytochrome c = N2 + 4 ferrocytochrome c
Other name(s): HDH
Systematic name: hydrazine:ferricytochrome c oxidoreductase
Comments: The enzyme, which is involved in the pathway of anaerobic ammonium oxidation in anammox bacteria, has been purified from the bacterium Candidatus Kuenenia stuttgartiensis. The electrons derived from hydrazine are eventually transferred to the quinone pool.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9075-43-8
References:
1.  Schalk, J., de Vries, S., Kuenen, J.G. and Jetten, M.S. Involvement of a novel hydroxylamine oxidoreductase in anaerobic ammonium oxidation. Biochemistry 39 (2000) 5405–5412. [DOI] [PMID: 10820012]
2.  Jetten, M.S., Wagner, M., Fuerst, J., van Loosdrecht, M., Kuenen, G. and Strous, M. Microbiology and application of the anaerobic ammonium oxidation ('anammox') process. Curr. Opin. Biotechnol. 12 (2001) 283–288. [DOI] [PMID: 11404106]
3.  Kartal, B., Maalcke, W.J., de Almeida, N.M., Cirpus, I., Gloerich, J., Geerts, W., Op den Camp, H.J., Harhangi, H.R., Janssen-Megens, E.M., Francoijs, K.J., Stunnenberg, H.G., Keltjens, J.T., Jetten, M.S. and Strous, M. Molecular mechanism of anaerobic ammonium oxidation. Nature 479 (2011) 127–130. [DOI] [PMID: 21964329]
4.  Kartal, B., de Almeida, N.M., Maalcke, W.J., Op den Camp, H.J., Jetten, M.S. and Keltjens, J.T. How to make a living from anaerobic ammonium oxidation. FEMS Microbiol. Rev. 37 (2013) 428–461. [DOI] [PMID: 23210799]
[EC 1.7.2.8 created 2003 as EC 1.7.99.8, modified 2010, transferred 2016 to EC 1.7.2.8]
 
 
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, KEGG, MetaCyc, 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]
 
 


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