Enzyme Nomenclature

EC 1.1.1 (continued)

with NAD+ or NADP+ as acceptor

Continued from:
EC 1.1.1.1 to EC 1.1.1.50
EC 1.1.1.51 to EC 1.1.1.100
EC 1.1.1.101 to EC 1.1.1.150
EC 1.1.1.151 to EC 1.1.1.200
EC 1.1.1.201 to EC 1.1.1.250
EC 1.1.1.251 to EC 1.1.1.300
See separate file for EC 1.1.1.351 to EC 1.1.1.413,

Contents

EC 1.1.1.301 D-arabitol-phosphate dehydrogenase
EC 1.1.1.302 2,5-diamino-6-(ribosylamino)-4(3H)-pyrimidinone 5'-phosphate reductase
EC 1.1.1.303 diacetyl reductase [(R)-acetoin forming]
EC 1.1.1.304 diacetyl reductase [(S)-acetoin forming]
EC 1.1.1.305 UDP-glucuronic acid dehydrogenase (UDP-4-keto-hexauronic acid decarboxylating)
EC 1.1.1.306 S-(hydroxymethyl)mycothiol dehydrogenase
EC 1.1.1.307 D-xylose reductase
EC 1.1.1.308 sulfopropanediol 3-dehydrogenase
EC 1.1.1.309 phosphonoacetaldehyde reductase (NADH)
EC 1.1.1.310 (S)-sulfolactate dehydrogenase
EC 1.1.1.311 (S)-1-phenylethanol dehydrogenase
EC 1.1.1.312 2-hydroxy-4-carboxymuconate semialdehyde hemiacetal dehydrogenase
EC 1.1.1.313 sulfoacetaldehyde reductase
EC 1.1.1.314 germacrene A alcohol dehydrogenase
EC 1.1.1.315 11-cis-retinol dehydrogenase
EC 1.1.1.316 L-galactose 1-dehydrogenase
EC 1.1.1.317 perakine reductase
EC 1.1.1.318 eugenol synthase
EC 1.1.1.319 isoeugenol synthase
EC 1.1.1.320 benzil reductase [(S)-benzoin forming]
EC 1.1.1.321 benzil reductase [(R)-benzoin forming]
EC 1.1.1.322 (–)-endo-fenchol dehydrogenase
EC 1.1.1.323 (+)-thujan-3-ol dehydrogenase
EC 1.1.1.324 8-hydroxygeraniol dehydrogenase
EC 1.1.1.325 sepiapterin reductase (L-threo-7,8-dihydrobiopterin forming)
EC 1.1.1.326 zerumbone synthase
EC 1.1.1.327 5-exo-hydroxycamphor dehydrogenase
EC 1.1.1.328 nicotine blue oxidoreductase
EC 1.1.1.329 2-deoxy-scyllo-inosamine dehydrogenase
EC 1.1.1.330 very-long-chain 3-oxoacyl-CoA reductase
EC 1.1.1.331 secoisolariciresinol dehydrogenase
EC 1.1.1.332 chanoclavine-I dehydrogenase
EC 1.1.1.333 decaprenylphospho-β-D-erythro-pentofuranosid-2-ulose 2-reductase
EC 1.1.1.334 methylecgonone reductase
EC 1.1.1.335 UDP-N-acetyl-2-amino-2-deoxyglucuronate dehydrogenase
EC 1.1.1.336 UDP-N-acetyl-D-mannosamine dehydrogenase
EC 1.1.1.337 L-2-hydroxycarboxylate dehydrogenase (NAD+)
EC 1.1.1.338 (2R)-3-sulfolactate dehydrogenase (NADP+)
EC 1.1.1.339 dTDP-6-deoxy-L-talose 4-dehydrogenase (NAD+)
EC 1.1.1.340 1-deoxy-11β-hydroxypentalenate dehydrogenase
EC 1.1.1.341 CDP-abequose synthase
EC 1.1.1.342 CDP-paratose synthase
EC 1.1.1.343 phosphogluconate dehydrogenase (NAD+-dependent, decarboxylating)
EC 1.1.1.344 dTDP-6-deoxy-L-talose 4-dehydrogenase [NAD(P)+]
EC 1.1.1.345 D-2-hydroxyacid dehydrogenase (NAD+)
EC 1.1.1.346 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming)
EC 1.1.1.347 geraniol dehydrogenase (NAD+)
EC 1.1.1.348 (3R)-2'-hydroxyisoflavanone reductase
EC 1.1.1.349 norsolorinic acid ketoreductase
EC 1.1.1.350 ureidoglycolate dehydrogenase (NAD+)

See the following file for:
EC 1.1.1.351 to EC 1.1.1.413

Entries

When an enzyme can use either NAD+ or NADP+, the symbol NAD(P)+ is used.

EC 1.1.1.301

Accepted name: D-arabitol-phosphate dehydrogenase

Reaction: D-arabitol 1-phosphate + NAD+ = D-xylulose 5-phosphate + NADH + H+

Other name(s): APDH; D-arabitol 1-phosphate dehydrogenase; D-arabitol 5-phosphate dehydrogenase

Systematic name: D-arabitol-phosphate:NAD+ oxidoreductase

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

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

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. [PMID: 12467497]

[EC 1.1.1.301 created 2010]

EC 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 reaction 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: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:

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. [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. [PMID: 16730025]

[EC 1.1.1.302 created 2010, modified 2011]

EC 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: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

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. [PMID: 10938079]

[EC 1.1.1.303 created 2010 (EC 1.1.1.5 created 1961 part created 2010)]

EC 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: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:

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. [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. [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 part created 2010)]

EC 1.1.1.305

Accepted name: UDP-glucuronic acid dehydrogenase (UDP-4-keto-hexauronic acid decarboxylating)

Reaction: UDP-glucuronate + NAD+ = UDP-β-L-threo-pentapyranos-4-ulose + CO2 + NADH + H+

For diagram of reaction click here.

Other name(s): UDP-GlcUA decarboxylase; ArnADH

Systematic name: UDP-glucuronate:NAD+ oxidoreductase (decarboxylating)

Comments: The activity is part of a bifunctional enzyme also performing the reaction of EC 2.1.2.13 (UDP-4-amino-4-deoxy-L-arabinose formyltransferase).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:

References:

1. Breazeale, S.D., Ribeiro, A.A., McClerren, A.L. and Raetz, C.R.H. A formyltransferase required for polymyxin resistance in Escherichia coli and the modification of lipid A with 4-amino-4-deoxy-L-arabinose. Identification and function of UDP-4-deoxy-4-formamido-L-arabinose. J. Biol. Chem. 280 (2005) 14154-14167. [PMID: 15695810]

2. Gatzeva-Topalova, P.Z., May, A.P. and Sousa, M.C. Crystal structure of Escherichia coli ArnA (PmrI) decarboxylase domain. A key enzyme for lipid A modification with 4-amino-4-deoxy-L-arabinose and polymyxin resistance. Biochemistry 43 (2004) 13370-13379. [PMID: 15491143]

3. Williams, G.J., Breazeale, S.D., Raetz, C.R.H. and Naismith, J.H. Structure and function of both domains of ArnA, a dual function decarboxylase and a formyltransferase, involved in 4-amino-4-deoxy-L-arabinose biosynthesis. J. Biol. Chem. 280 (2005) 23000-23008. [PMID: 15809294]

4. Gatzeva-Topalova, P.Z., May, A.P. and Sousa, M.C. Structure and mechanism of ArnA: conformational change implies ordered dehydrogenase mechanism in key enzyme for polymyxin resistance. Structure 13 (2005) 929-942. [PMID: 15939024]

5. Yan, A., Guan, Z. and Raetz, C.R.H. An undecaprenyl phosphate-aminoarabinose flippase required for polymyxin resistance in Escherichia coli. J. Biol. Chem. 282 (2007) 36077-36089. [PMID: 17928292]

[EC 1.1.1.305 created 2010]

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-(N-acetyl-L-cysteinamido)-2-deoxy-α-D-glucopyranosyl]-D-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:

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. [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. [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. [PMID: 12809551]

4. Rawat, M. and Av-Gay, Y. Mycothiol-dependent proteins in actinomycetes. FEMS Microbiol. Rev. 31 (2007) 278-292. [PMID: 17286835]

[EC 1.1.1.306 created 2010 as EC 1.2.1.66, transferred 2010 to EC 1.1.1.306]

EC 1.1.1.307

Accepted name: D-xylose reductase

Reaction: xylitol + NAD(P)+ = D-xylose + NAD(P)H + H+

Other name(s): XylR; XyrA; msXR; dsXR; monospecific xylose reductase; dual specific xylose reductase; NAD(P)H-dependent xylose reductase; xylose reductase

Systematic name: xylitol:NAD(P)+ oxidoreductase

Comments: Xylose reductase catalyses the initial reaction in the xylose utilization pathway, the NAD(P)H dependent reduction of xylose to xylitol.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:

References:

1. Neuhauser, W., Haltrich, D., Kulbe, K.D. and Nidetzky, B. NAD(P)H-dependent aldose reductase from the xylose-assimilating yeast Candida tenuis. Isolation, characterization and biochemical properties of the enzyme. Biochem. J. 326 (1997) 683-692. [PMID: 9307017]

2. Nidetzky, B., Bruggler, K., Kratzer, R. and Mayr, P. Multiple forms of xylose reductase in Candida intermedia: comparison of their functional properties using quantitative structure-activity relationships, steady-state kinetic analysis, and pH studies. J. Agric. Food Chem. 51 (2003) 7930-7935. [PMID: 14690376]

3. Iablochkova, E.N., Bolotnikova, O.I., Mikhailova, N.P., Nemova, N.N. and Ginak, A.I. The activity of xylose reductase and xylitol dehydrogenase in yeasts. Mikrobiologiia 72 (2003) 466-469. [PMID: 14526534] (in Russian)

4. Chen, L.C., Huang, S.C., Chuankhayan, P., Chen, C.D., Huang, Y.C., Jeyakanthan, J., Pang, H.F., Men, L.C., Chen, Y.C., Wang, Y.K., Liu, M.Y., Wu, T.K. and Chen, C.J. Purification, crystallization and preliminary X-ray crystallographic analysis of xylose reductase from Candida tropicalis. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 65 (2009) 419-421. [PMID: 19342796]

5. Verduyn, C., Van Kleef, R., Frank, J., Schreuder, H., Van Dijken, J.P. and Scheffers, W.A. Properties of the NAD(P)H-dependent xylose reductase from the xylose-fermenting yeast Pichia stipitis. Biochem. J. 226 (1985) 669-677. [PMID: 3921014]

6. Fernandes, S., Tuohy, M.G. and Murray, P.G. Xylose reductase from the thermophilic fungus Talaromyces emersonii: cloning and heterologous expression of the native gene (Texr) and a double mutant (TexrK271R + N273D) with altered coenzyme specificity. J Biosci 34 (2009) 881-890. [PMID: 20093741]

7. 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. [PMID: 14532079]

8. Woodyer, R., Simurdiak, M., van der Donk, W.A. and Zhao, H. Heterologous expression, purification, and characterization of a highly active xylose reductase from Neurospora crassa. Appl. Environ. Microbiol. 71 (2005) 1642-1647. [PMID: 15746370]

[EC 1.1.1.307 created 2010]

EC 1.1.1.308

Accepted name: sulfopropanediol 3-dehydrogenase

Reaction: (R)-2,3-dihydroxypropane-1-sulfonate + 2 NAD+ + H2O = (R)-3-sulfolactate + 2 NADH + 2 H+

Other name(s): DHPS 3-dehydrogenase (sulfolactate forming); 2,3-dihydroxypropane-1-sulfonate 3-dehydrogenase (sulfolactate forming); dihydroxypropanesulfonate 3-dehydrogenase; hpsN (gene name)

Systematic name: (R)-2,3-dihydroxypropane-1-sulfonate:NAD+ 3-oxidoreductase

Comments: The enzyme is involved in degradation of (R)-2,3-dihydroxypropanesulfonate.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Mayer, J., Huhn, T., Habeck, M., Denger, K., Hollemeyer, K. and Cook, A.M. 2,3-Dihydroxypropane-1-sulfonate degraded by Cupriavidus pinatubonensis JMP134: purification of dihydroxypropanesulfonate 3-dehydrogenase. Microbiology 156 (2010) 1556-1564. [PMID: 20150239]

[EC 1.1.1.308 created 2011]

EC 1.1.1.309

Accepted name: phosphonoacetaldehyde reductase (NADH)

For diagram of reaction click here.

Reaction: 2-hydroxyethylphosphonate + NAD+ = phosphonoacetaldehyde + NADH + H+

Other name(s): PhpC

Systematic name: 2-hydroxyethylphosphonate:NAD+ oxidoreductase

Comments: The enzyme from Streptomyces viridochromogenes catalyses a step in the biosynthesis of phosphinothricin tripeptide, the reduction of phosphonoacetaldehyde to 2-hydroxyethylphosphonate. The preferred cofactor is NADH, lower activity with NADPH [1].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Blodgett, J.A., Thomas, P.M., Li, G., Velasquez, J.E., van der Donk, W.A., Kelleher, N.L. and Metcalf, W.W. Unusual transformations in the biosynthesis of the antibiotic phosphinothricin tripeptide. Nat. Chem. Biol. 3 (2007) 480-485. [PMID: 17632514]

[EC 1.1.1.309 created 2011]

EC 1.1.1.310

Accepted name: (S)-sulfolactate dehydrogenase

Reaction: (2S)-3-sulfolactate + NAD+ = 3-sulfopyruvate + NADH + H+

Other name(s): (2S)-3-sulfolactate dehydrogenase; SlcC

Systematic name: (2S)-sulfolactate:NAD+ oxidoreductase

Comments: This enzyme, isolated from the bacterium Chromohalobacter salexigens DSM 3043, acts only on the (S)-enantiomer of 3-sulfolactate. Combined with EC 1.1.1.338, (2R)-3-sulfolactate dehydrogenase (NADP+), it provides a racemase system that converts (2S)-3-sulfolactate to (2R)-3-sulfolactate, which is degraded further by EC 4.4.1.24, (2R)-sulfolactate sulfo-lyase. The enzyme is specific for NAD+.

Links to other databases: BRENDA, EXPASY, KEGG Metacyc, CAS registry number:

References:

1. Denger, K. and Cook, A.M. Racemase activity effected by two dehydrogenases in sulfolactate degradation by Chromohalobacter salexigens: purification of (S)-sulfolactate dehydrogenase. Microbiology 156 (2010) 967-974. [PMID: 20007648]

[EC 1.1.1.310 created 2011, modified 2013]

EC 1.1.1.311

Accepted name: (S)-1-phenylethanol dehydrogenase

Reaction: (S)-1-phenylethanol + NAD+ = acetophenone + NADH + H+

Other name(s): PED

Systematic name: (S)-1-phenylethanol:NAD+ oxidoreductase

Comments: The enzyme is involved in degradation of ethylbenzene.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number:

References:

1. Kniemeyer, O. and Heider, J. (S)-1-phenylethanol dehydrogenase of Azoarcus sp. strain EbN1, an enzyme of anaerobic ethylbenzene catabolism. Arch. Microbiol. 176 (2001) 129-135. [PMID: 11479712]

2. Hoffken, H.W., Duong, M., Friedrich, T., Breuer, M., Hauer, B., Reinhardt, R., Rabus, R. and Heider, J. Crystal structure and enzyme kinetics of the (S)-specific 1-phenylethanol dehydrogenase of the denitrifying bacterium strain EbN1. Biochemistry 45 (2006) 82-93. [PMID: 16388583]

[EC 1.1.1.311 created 2011]

EC 1.1.1.312

Accepted name: 2-hydroxy-4-carboxymuconate semialdehyde hemiacetal dehydrogenase

Reaction: 4-carboxy-2-hydroxymuconate semialdehyde hemiacetal + NADP+ = 2-oxo-2H-pyran-4,6-dicarboxylate + NADPH + H+

For diagram of reaction click here

Other name(s): 2-hydroxy-4-carboxymuconate 6-semialdehyde dehydrogenase; 4-carboxy-2-hydroxy-cis,cis-muconate-6-semialdehyde:NADP+ oxidoreductase; α-hydroxy-γ-carboxymuconic ε-semialdehyde dehydrogenase; 4-carboxy-2-hydroxymuconate-6-semialdehyde dehydrogenase; LigC; ProD

Systematic name: 4-carboxy-2-hydroxymuconate semialdehyde hemiacetal:NADP+ 2-oxidoreductase

Comments: The enzyme does not act on unsubstituted aliphatic or aromatic aldehydes or glucose; NAD+ can replace NADP+, but with lower affinity. The enzyme was initially believed to act on 4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde and produce 4-carboxy-2-hydroxy-cis,cis-muconate [1]. However, later studies showed that the substrate is the hemiacetal form [3], and the product is 2-oxo-2H-pyran-4,6-dicarboxylate [2,4].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 67272-39-3

References:

1. Maruyama, K., Ariga, N., Tsuda, M. and Deguchi, K. Purification and properties of α-hydroxy-γ-carboxymuconic ε-semialdehyde dehydrogenase. J. Biochem. (Tokyo) 83 (1978) 1125-1134. [PMID: 26671]

2. Maruyama, K. Isolation and identification of the reaction product of α-hydroxy-γ-carboxymuconic ε-semialdehyde dehydrogenase. J. Biochem. 86 (1979) 1671-1677. [PMID: 528534]

3. Maruyama, K. Purification and properties of 2-pyrone-4,6-dicarboxylate hydrolase. J. Biochem. (Tokyo) 93 (1983) 557-565. [PMID: 6841353]

4. Masai, E., Momose, K., Hara, H., Nishikawa, S., Katayama, Y. and Fukuda, M. Genetic and biochemical characterization of 4-carboxy-2-hydroxymuconate-6-semialdehyde dehydrogenase and its role in the protocatechuate 4,5-cleavage pathway in Sphingomonas paucimobilis SYK-6. J. Bacteriol. 182 (2000) 6651-6658. [PMID: 11073908]

[EC 1.1.1.312 created 1978 as EC 1.2.1.45, transferred 2011 to EC 1.1.1.312]

EC 1.1.1.313

Accepted name: sulfoacetaldehyde reductase

Reaction: isethionate + NADP+ = 2-sulfoacetaldehyde + NADPH + H+

Glossary: isethionate = 2-hydroxyethanesulfonate
2-sulfoacetaldehyde = 2-oxoethanesulfonate

Other name(s): isfD (gene name)

Systematic name: isethionate:NADP+ oxidoreductase

Comments: Catalyses the reaction only in the opposite direction. Involved in taurine degradation. The bacterium Chromohalobacter salexigens strain DSM 3043 possesses two enzymes that catalyse this reaction, a constitutive enzyme (encoded by isfD2) and an inducible enzyme (encoded by isfD). The latter is induced by taurine, and is responsible for most of the activity observed in taurine-grown cells.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Krejcik, Z., Hollemeyer, K., Smits, T.H. and Cook, A.M. Isethionate formation from taurine in Chromohalobacter salexigens: purification of sulfoacetaldehyde reductase. Microbiology 156 (2010) 1547-1555. [PMID: 20133363]

[EC 1.1.1.313 created 2011]

EC 1.1.1.314

Accepted name: germacrene A alcohol dehydrogenase

Reaction: germacra-1(10),4,11(13)-trien-12-ol + 2 NADP+ + H2O = germacra-1(10),4,11(13)-trien-12-oate + 2 NADPH + 3 H+ (overall reaction)
(1a) germacra-1(10),4,11(13)-trien-12-ol + NADP+ = germacra-1(10),4,11(13)-trien-12-al + NADPH + H+
(1b) germacra-1(10),4,11(13)-trien-12-al + NADP+ + H2O = germacra-1(10),4,11(13)-trien-12-oate + NADPH + 2 H+

For diagram of reaction click here.

Systematic name: germacra-1(10),4,11(13)-trien-12-ol:NADP+ oxidoreductase

Comments: In Lactuca sativa EC 1.1.1.314 is a mutifunctional enzyme with EC 1.14.13.123, germacrene A hydroxylase [2].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. de Kraker, J.W., Franssen, M.C., Dalm, M.C., de Groot, A. and Bouwmeester, H.J. Biosynthesis of germacrene A carboxylic acid in chicory roots. Demonstration of a cytochrome P450 (+)-germacrene A hydroxylase and NADP+-dependent sesquiterpenoid dehydrogenase(s) involved in sesquiterpene lactone biosynthesis. Plant Physiol. 125 (2001) 1930-1940. [PMID: 11299372]

2. Nguyen, D.T., Gopfert, J.C., Ikezawa, N., Macnevin, G., Kathiresan, M., Conrad, J., Spring, O. and Ro, D.K. Biochemical conservation and evolution of germacrene A oxidase in Asteraceae. J. Biol. Chem. 285 (2010) 16588-16598. [PMID: 20351109]

[EC 1.1.1.314 created 2011]

EC 1.1.1.315

Accepted name: 11-cis-retinol dehydrogenase

Reaction: 11-cis-retinol—[retinal-binding-protein] + NAD+ = 11-cis-retinal—[retinol-binding-protein] + NADH + H+

For diagram of reaction click here

Glossary: 11-cis-retinal = 11-cis-retinaldehyde

Other name(s): RDH5 (gene name)

Systematic name: 11-cis-retinol:NAD+ oxidoreductase

Comments: This enzyme, abundant in the retinal pigment epithelium, catalyses the reduction of 11-cis-retinol to 11-cis-retinal [1] while the substrate is bound to the retinal-binding protein [4]. This is a crucial step in the regeneration of 11-cis-retinal, the chromophore of rhodopsin. The enzyme can also accept other cis forms of retinol [2].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Simon, A., Hellman, U., Wernstedt, C. and Eriksson, U. The retinal pigment epithelial-specific 11-cis retinol dehydrogenase belongs to the family of short chain alcohol dehydrogenases. J. Biol. Chem. 270 (1995) 1107-1112. [PMID: 7836368]

2. Wang, J., Chai, X., Eriksson, U. and Napoli, J.L. Activity of human 11-cis-retinol dehydrogenase (Rdh5) with steroids and retinoids and expression of its mRNA in extra-ocular human tissue. Biochem. J. 338 (1999) 23-27. [PMID: 9931293]

3. Liden, M., Romert, A., Tryggvason, K., Persson, B. and Eriksson, U. Biochemical defects in 11-cis-retinol dehydrogenase mutants associated with fundus albipunctatus. J. Biol. Chem. 276 (2001) 49251-49257. [PMID: 11675386]

4. Wu, Z., Yang, Y., Shaw, N., Bhattacharya, S., Yan, L., West, K., Roth, K., Noy, N., Qin, J. and Crabb, J.W. Mapping the ligand binding pocket in the cellular retinaldehyde binding protein. J. Biol. Chem. 278 (2003) 12390-12396. [PMID: 12536149]

[EC 1.1.1.315 created 2011]

EC 1.1.1.316

Accepted name: L-galactose 1-dehydrogenase

Reaction: L-galactose + NAD+ = L-galactono-1,4-lactone + NADH + H+

Other name(s): L-GalDH; L-galactose dehydrogenase

Systematic name: L-galactose:NAD+ 1-oxidoreductase

Comments: The enzyme catalyses a step in the ascorbate biosynthesis in higher plants (Smirnoff-Wheeler pathway). The activity with NADP+ is less than 10% of the activity with NAD+.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Mieda, T., Yabuta, Y., Rapolu, M., Motoki, T., Takeda, T., Yoshimura, K., Ishikawa, T. and Shigeoka, S. Feedback inhibition of spinach L-galactose dehydrogenase by L-ascorbate. Plant Cell Physiol. 45 (2004) 1271-1279. [PMID: 15509850]

2. Gatzek, S., Wheeler, G.L. and Smirnoff, N. Antisense suppression of L-galactose dehydrogenase in Arabidopsis thaliana provides evidence for its role in ascorbate synthesis and reveals light modulated L-galactose synthesis. Plant J. 30 (2002) 541-553. [PMID: 12047629]

3. Wheeler, G.L., Jones, M.A. and Smirnoff, N. The biosynthetic pathway of vitamin C in higher plants. Nature 393 (1998) 365-369. [PMID: 9620799]

4. Oh, M.M., Carey, E.E. and Rajashekar, C.B. Environmental stresses induce health-promoting phytochemicals in lettuce. Plant Physiol. Biochem. 47 (2009) 578-583. [PMID: 19297184]

[EC 1.1.1.316 created 2011]

EC 1.1.1.317

Accepted name: perakine reductase

Reaction: raucaffrinoline + NADP+ = perakine + NADPH + H+

For diagram of reaction 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, CAS registry number:

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. [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. [PMID: 17142919]

[EC 1.1.1.317 created 2011]

EC 1.1.1.318

Accepted name: eugenol synthase

Reaction: eugenol + a carboxylate + NADP+ = a coniferyl ester + NADPH + H+

For diagram of reaction click here.

Other name(s): LtCES1; EGS1; EGS2

Systematic name: eugenol:NADP+ oxidoreductase (coniferyl ester reducing)

Comments: The enzyme acts in the opposite direction. The enzymes from the plants Ocimum basilicum (sweet basil) [1,3], Clarkia breweri and Petunia hybrida [4] only accept coniferyl acetate and form eugenol. The enzyme from Pimpinella anisum (anise) forms anol (from 4-coumaryl acetate) in vivo, although the recombinant enzyme can form eugenol from coniferyl acetate [5]. The enzyme from Larrea tridentata (creosote bush) also forms chavicol from a coumaryl ester and can use NADH [2].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:

References:

1. Koeduka, T., Fridman, E., Gang, D.R., Vassão, D.G., Jackson, B.L., Kish, C.M., Orlova, I., Spassova, S.M., Lewis, N.G., Noel, J.P., Baiga, T.J., Dudareva, N. and Pichersky, E. Eugenol and isoeugenol, characteristic aromatic constituents of spices, are biosynthesized via reduction of a coniferyl alcohol ester. Proc. Natl. Acad. Sci. USA 103 (2006) 10128-10133. [PMID: 16782809]

2. Vassão, D.G., Kim, S.J., Milhollan, J.K., Eichinger, D., Davin, L.B. and Lewis, N.G. A pinoresinol-lariciresinol reductase homologue from the creosote bush (Larrea tridentata) catalyzes the efficient in vitro conversion of p-coumaryl/coniferyl alcohol esters into the allylphenols chavicol/eugenol, but not the propenylphenols p-anol/isoeugenol. Arch. Biochem. Biophys. 465 (2007) 209-218. [PMID: 17624297]

3. Louie, G.V., Baiga, T.J., Bowman, M.E., Koeduka, T., Taylor, J.H., Spassova, S.M., Pichersky, E. and Noel, J.P. Structure and reaction mechanism of basil eugenol synthase. PLoS One 2 (2007) e993. [PMID: 17912370]

4. Koeduka, T., Louie, G.V., Orlova, I., Kish, C.M., Ibdah, M., Wilkerson, C.G., Bowman, M.E., Baiga, T.J., Noel, J.P., Dudareva, N. and Pichersky, E. The multiple phenylpropene synthases in both Clarkia breweri and Petunia hybrida represent two distinct protein lineages. Plant J. 54 (2008) 362-374. [PMID: 18208524]

5. Koeduka, T., Baiga, T.J., Noel, J.P. and Pichersky, E. Biosynthesis of t-anethole in anise: characterization of t-anol/isoeugenol synthase and an O-methyltransferase specific for a C7-C8 propenyl side chain. Plant Physiol. 149 (2009) 384-394. [PMID: 18987218]

[EC 1.1.1.318 created 2012]

EC 1.1.1.319

Accepted name: isoeugenol synthase

Reaction: isoeugenol + acetate + NADP+ = coniferyl acetate + NADPH + H+

For diagram of reaction click here.

Other name(s): IGS1; t-anol/isoeugenol synthase 1

Systematic name: eugenol:NADP+ oxidoreductase (coniferyl acetate reducing)

Comments: The enzyme acts in the opposite direction. In Ocimum basilicum (sweet basil), Clarkia breweri, and Petunia hybrida only isoeugenol is formed [1,2]. However in Pimpinella anisum (anise) only anol is formed in vivo, although the cloned enzyme does produce isoeugenol [3].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Koeduka, T., Fridman, E., Gang, D.R., Vassão, D.G., Jackson, B.L., Kish, C.M., Orlova, I., Spassova, S.M., Lewis, N.G., Noel, J.P., Baiga, T.J., Dudareva, N. and Pichersky, E. Eugenol and isoeugenol, characteristic aromatic constituents of spices, are biosynthesized via reduction of a coniferyl alcohol ester. Proc. Natl. Acad. Sci. USA 103 (2006) 10128-10133. [PMID: 16782809]

2. Koeduka, T., Louie, G.V., Orlova, I., Kish, C.M., Ibdah, M., Wilkerson, C.G., Bowman, M.E., Baiga, T.J., Noel, J.P., Dudareva, N. and Pichersky, E. The multiple phenylpropene synthases in both Clarkia breweri and Petunia hybrida represent two distinct protein lineages. Plant J. 54 (2008) 362-374. [PMID: 18208524]

3. Koeduka, T., Baiga, T.J., Noel, J.P. and Pichersky, E. Biosynthesis of t-anethole in anise: characterization of t-anol/isoeugenol synthase and an O-methyltransferase specific for a C7-C8 propenyl side chain. Plant Physiol. 149 (2009) 384-394. [PMID: 18987218]

[EC 1.1.1.319 created 2012]

EC 1.1.1.320

Accepted name: benzil reductase [(S)-benzoin forming]

Reaction: (S)-benzoin + NADP+ = benzil + NADPH + H+

Glossary: (S)-benzoin = (2S)-2-hydroxy-1,2-diphenylethanone
benzil = 1,2-diphenylethane-1,2-dione

Other name(s): YueD

Systematic name: (S)-benzoin:NADP+ oxidoreductase

Comments: The enzyme also reduces 1-phenylpropane-1,2-dione. The enzyme from Bacillus cereus in addition reduces 1,4-naphthoquinone and 1-(4-methylphenyl)-2-phenylethane-1,2-dione with high efficiency [2].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Maruyama, R., Nishizawa, M., Itoi, Y., Ito, S. and Inoue, M. Isolation and expression of a Bacillus cereus gene encoding benzil reductase. Biotechnol. Bioeng. 75 (2001) 630-633. [PMID: 11745140]

2. Maruyama, R., Nishizawa, M., Itoi, Y., Ito, S. and Inoue, M. The enzymes with benzil reductase activity conserved from bacteria to mammals. J. Biotechnol. 94 (2002) 157-169. [PMID: 11796169]

[EC 1.1.1.320 created 2012]

EC 1.1.1.321

Accepted name: benzil reductase [(R)-benzoin forming]

Reaction: (R)-benzoin + NADP+ = benzil + NADPH + H+

Glossary: (R)-benzoin = (2R)-2-hydroxy-1,2-diphenylethanone
benzil = 1,2-diphenylethane-1,2-dione

Systematic name: (R)-benzoin:NADP+ oxidoreductase

Comments: The enzyme from the bacterium Xanthomonas oryzae is able to reduce enantioselectively only one of the two carbonyl groups of benzil to give optically active (R)-benzoin.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Konishi, J., Ohta, H. and Tuchihashi, G. Asymmetric reduction of benzil to benzoin catalyzed by the enzyme system of a microorganism. Chem. Lett. 14 (1985) 1111-1112.

[EC 1.1.1.321 created 2012]

EC 1.1.1.322

Accepted name: (–)-endo-fenchol dehydrogenase

Reaction: (–)-endo-fenchol + NAD(P)+ = (+)-fenchone + NAD(P)H + H+

For diagram of reaction click here.

Other name(s): l-endo-fenchol dehydrogenase; FDH

Systematic name: (–)-endo-fenchol:NAD(P)+ oxidoreductase

Comments: Isolated from the plant Foeniculum vulgare (fennel). NADH is slightly preferred to NADPH.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Croteau, R. and Felton, N.M. Substrate specificity of monoterpenol dehydrogenases from Foeniculum vulgare and Tanacetum vulgare. Phytochemistry 19 (1980) 1343-1347.

[EC 1.1.1.322 created 2012]

EC 1.1.1.323

Accepted name: (+)-thujan-3-ol dehydrogenase

Reaction: (+)-thujan-3-ol + NAD(P)+ = (+)-thujan-3-one + NAD(P)H + H+

Other name(s): d-3-thujanol dehydrogenase; TDH

Systematic name: (+)-thujan-3-ol:NAD(P)+ oxidoreductase

Comments: Isolated from the plant Tanacetum vulgare (tansy). NADH is preferred to NADPH.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Croteau, R. and Felton, N.M. Substrate specificity of monoterpenol dehydrogenases from Foeniculum vulgare and Tanacetum vulgare. Phytochemistry 19 (1980) 1343-1347.

[EC 1.1.1.323 created 2012]

EC 1.1.1.324

Accepted name: 8-hydroxygeraniol dehydrogenase

Reaction: (6E)-8-hydroxygeraniol + 2 NADP+ = (6E)-8-oxogeranial + 2 NADPH + 2 H+ (overall reaction)
(1a) (6E)-8-hydroxygeraniol + NADP+ = (6E)-8-hydroxygeranial + NADPH + H+
(1b) (6E)-8-hydroxygeraniol + NADP+ = (6E)-8-oxogeraniol + NADPH + H+
(1c) (6E)-8-hydroxygeranial+ NADP+ = (6E)-8-oxogeranial + NADPH + H+
(1d) (6E)-8-oxogeraniol + NADP+ = (6E)-8-oxogeranial + NADPH + H+

For diagram of reaction click here.

Other name(s): 8-hydroxygeraniol oxidoreductase; CYP76B10; G10H; CrG10H; SmG10H; acyclic monoterpene primary alcohol:NADP+ oxidoreductase

Systematic name: (6E)-8-hydroxygeraniol:NADP+ oxidoreductase

Comments: Contains Zn2+. The enzyme catalyses the oxidation of (6E)-8-hydroxygeraniol to (6E)-8-oxogeranial via either (6E)-8-hydroxygeranial or (6E)-8-oxogeraniol. Also acts on geraniol, nerol and citronellol. May be identical to EC 1.1.1.183 geraniol dehydrogenase. The recommended numbering of geraniol gives 8-hydroxygeraniol as the substrate rather than 10-hydroxygeraniol as used by references 1 and 2. See prenol nomenclature Pr-1.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Ikeda, H., Esaki, N., Nakai, S., Hashimoto, K., Uesato, S., Soda, K. and Fujita, T. Acyclic monoterpene primary alcohol:NADP+ oxidoreductase of Rauwolfia serpentina cells: the key enzyme in biosynthesis of monoterpene alcohols. J. Biochem. 109 (1991) 341-347. [PMID: 1864846]

2. Hallahan, D.L., West, J.M., Wallsgrove, R.M., Smiley, D.W., Dawson, G.W., Pickett, J.A. and Hamilton, J.G. Purification and characterization of an acyclic monoterpene primary alcohol:NADP+ oxidoreductase from catmint (Nepeta racemosa). Arch. Biochem. Biophys. 318 (1995) 105-112. [PMID: 7726550]

[EC 1.1.1.324 created 2012]

EC 1.1.1.325

Accepted name: sepiapterin reductase (L-threo-7,8-dihydrobiopterin forming)

Reaction: (1) L-threo-7,8-dihydrobiopterin + NADP+ = sepiapterin + NADPH + H+
(2) L-threo-tetrahydrobiopterin + 2 NADP+ = 6-pyruvoyl-5,6,7,8-tetrahydropterin + 2 NADPH + 2 H+

Glossary: sepiapterin = 2-amino-6-lactoyl-7,8-dihydropteridin-4(3H)-one
tetrahydrobiopterin = 5,6,7,8-tetrahydrobiopterin = 2-amino-6-(1,2-dihydroxypropyl)-5,6,7,8-tetrahydropteridin-4(3H)-one

Systematic name: L-threo-7,8-dihydrobiopterin:NADP+ oxidoreductase

Comments: This enzyme, isolated from the bacterium Chlorobium tepidum, catalyses the final step in the de novo synthesis of tetrahydrobiopterin from GTP. cf. EC 1.1.1.153, sepiapterin reductase (L-erythro-7,8-dihydrobiopterin forming).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Cho, S.H., Na, J.U., Youn, H., Hwang, C.S., Lee, C.H. and Kang, S.O. Sepiapterin reductase producing L-threo-dihydrobiopterin from Chlorobium tepidum. Biochem. J. 340 (1999) 497-503. [PMID: 10333495]

2. Supangat, S., Choi, Y.K., Park, Y.S., Son, D., Han, C.D. and Lee, K.H. Expression, purification, crystallization and preliminary X-ray analysis of sepiapterin reductase from Chlorobium tepidum. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 61 (2005) 202-204. [PMID: 16510994]

[EC 1.1.1.325 created 2012]

EC 1.1.1.326

Accepted name: zerumbone synthase

Reaction: 10-hydroxy-α-humulene + NAD+ = zerumbone + NADH + H+

For diagram of reaction 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, CAS registry number:

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. [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 reaction click here.

Other name(s): F-dehydrogenase; FdeH

Systematic name: 5-exo-hydroxycamphor:NADP+ oxidoreductase

Comments: Contains Zn2+. Isolated from Pseudomonas putida, and involved in degradation of (+)-camphor.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number:

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. [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. [PMID: 8334169]

[EC 1.1.1.327 created 2012]

EC 1.1.1.328

Accepted name: nicotine blue oxidoreductase

Reaction: 3,3'-bipyridine-2,2',5,5',6,6'-hexol + NAD(P)+ = (E)-2,2',5,5'-tetrahydroxy-6H,6'H-[3,3'-bipyridinylidene]-6,6'-dione + NAD(P)H + H+

For diagram of reaction click here.

Glossary: 3,3'-bipyridine-2,2',5,5',6,6'-hexol = nicotine blue leuco form
(E)-2,2',5,5'-tetrahydroxy-6H,6'H-[3,3'-bipyridinylidene]-6,6'-dione = nicotine blue

Other name(s): nboR (gene name)

Systematic name: 3,3'-bipyridine-2,2',5,5',6,6'-hexol:NADP+ 11-oxidoreductase

Comments: The enzyme, characterized from the nicotine degrading bacterium Arthrobacter nicotinovorans, catalyses the reduction of "nicotine blue" to its hydroquinone form (the opposite direction from that shown). Nicotine blue is the name given to the compound formed by the autocatalytic condensation of two molecules of 2,3,6-trihydroxypyridine, an intermediate in the nicotine degradation pathway. The main role of the enzyme may be to prevent the intracellular formation of nicotine blue semiquinone radicals, which by redox cycling would lead to the formation of toxic reactive oxygen species. The enzyme possesses a slight preference for NADH over NADPH.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Mihasan, M., Chiribau, C.B., Friedrich, T., Artenie, V. and Brandsch, R. An NAD(P)H-nicotine blue oxidoreductase is part of the nicotine regulon and may protect Arthrobacter nicotinovorans from oxidative stress during nicotine catabolism. Appl. Environ. Microbiol. 73 (2007) 2479-2485. [PMID: 17293530]

[EC 1.1.1.328 created 2012]

EC 1.1.1.329

Accepted name: 2-deoxy-scyllo-inosamine dehydrogenase

Reaction: 2-deoxy-scyllo-inosamine + NAD(P)+ = 3-amino-2,3-dideoxy-scyllo-inosose + NAD(P)H + H+

For diagram of reaction click here.

Glossary: 2-deoxy-scyllo-inosamine = (1R,2S,3S,4R,5S)-5-aminocyclohexane-1,2,3,4-tetrol

Other name(s): neoA (gene name); kanK (gene name, ambiguous); kanE (gene name, ambiguous)

Systematic name: 2-deoxy-scyllo-inosamine:NAD(P)+ 1-oxidoreductase

Comments: Requires zinc. Involved in the biosynthetic pathways of several clinically important aminocyclitol antibiotics, including kanamycin, neomycin and ribostamycin. cf. EC 1.1.99.38, 2-deoxy-scyllo-inosamine dehydrogenase (SAM-dependent).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Kudo, F., Yamamoto, Y., Yokoyama, K., Eguchi, T. and Kakinuma, K. Biosynthesis of 2-deoxystreptamine by three crucial enzymes in Streptomyces fradiae NBRC 12773. J. Antibiot. (Tokyo) 58 (2005) 766-774. [PMID: 16506694]

2. Nepal, K.K., Oh, T.J. and Sohng, J.K. Heterologous production of paromamine in Streptomyces lividans TK24 using kanamycin biosynthetic genes from Streptomyces kanamyceticus ATCC12853. Mol. Cells 27 (2009) 601-608. [PMID: 19466609]

[EC 1.1.1.329 created 2012]

EC 1.1.1.330

Accepted name: very-long-chain 3-oxoacyl-CoA reductase

Reaction: a very-long-chain (3R)-3-hydroxyacyl-CoA + NADP+ = a very-long-chain 3-oxoacyl-CoA + NADPH + H+

Glossary: a very-long-chain acyl-CoA = an acyl-CoA thioester where the acyl chain contains 23 or more carbon atoms

Other name(s): very-long-chain 3-ketoacyl-CoA reductase; very-long-chain β-ketoacyl-CoA reductase; KCR (gene name); IFA38 (gene name)

Systematic name: (3R)-3-hydroxyacyl-CoA:NADP+ oxidoreductase

Comments: The second component of the elongase, a microsomal protein complex responsible for extending palmitoyl-CoA and stearoyl-CoA (and modified forms thereof) to very-long-chain acyl CoAs. The enzyme is active with substrates with chain length of C16 to C34, depending on the species. cf. EC 2.3.1.199, very-long-chain 3-oxoacyl-CoA synthase, EC 4.2.1.134, very-long-chain (3R)-3-hydroxyacyl-[acyl-carrier protein] dehydratase, and EC 1.3.1.93, very-long-chain enoyl-CoA reductase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Beaudoin, F., Gable, K., Sayanova, O., Dunn, T. and Napier, J.A. A Saccharomyces cerevisiae gene required for heterologous fatty acid elongase activity encodes a microsomal β-keto-reductase. J. Biol. Chem. 277 (2002) 11481-11488. [PMID: 11792704]

2. Han, G., Gable, K., Kohlwein, S.D., Beaudoin, F., Napier, J.A. and Dunn, T.M. The Saccharomyces cerevisiae YBR159w gene encodes the 3-ketoreductase of the microsomal fatty acid elongase. J. Biol. Chem. 277 (2002) 35440-35449. [PMID: 12087109]

3. Beaudoin, F., Wu, X., Li, F., Haslam, R.P., Markham, J.E., Zheng, H., Napier, J.A. and Kunst, L. Functional characterization of the Arabidopsis β-ketoacyl-coenzyme A reductase candidates of the fatty acid elongase. Plant Physiol. 150 (2009) 1174-1191. [PMID: 19439572]

[EC 1.1.1.330 created 2012]

EC 1.1.1.331

Accepted name: secoisolariciresinol dehydrogenase

Reaction: (–)-secoisolariciresinol + 2 NAD+ = (–)-matairesinol + 2 NADH + 2 H+

For diagram of reaction click here.

Systematic name: (–)-secoisolariciresinol:NAD+ oxidoreductase

Comments: Isolated from the plants Forsythia intermedia [1] and Podophyllum peltatum [1-3]. An intermediate lactol is detected in vitro.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Xia, Z.Q., Costa, M.A., Pelissier, H.C., Davin, L.B. and Lewis, N.G. Secoisolariciresinol dehydrogenase purification, cloning, and functional expression. Implications for human health protection. J. Biol. Chem. 276 (2001) 12614-12623. [PMID: 11278426]

2. Youn, B., Moinuddin, S.G., Davin, L.B., Lewis, N.G. and Kang, C. Crystal structures of apo-form and binary/ternary complexes of Podophyllum secoisolariciresinol dehydrogenase, an enzyme involved in formation of health-protecting and plant defense lignans. J. Biol. Chem. 280 (2005) 12917-12926. [PMID: 15653677]

3. Moinuddin, S.G., Youn, B., Bedgar, D.L., Costa, M.A., Helms, G.L., Kang, C., Davin, L.B. and Lewis, N.G. Secoisolariciresinol dehydrogenase: mode of catalysis and stereospecificity of hydride transfer in Podophyllum peltatum. Org. Biomol. Chem. 4 (2006) 808-816. [PMID: 16493463]

[EC 1.1.1.331 created 2012]

EC 1.1.1.332

Accepted name: chanoclavine-I dehydrogenase

Reaction: chanoclavine-I + NAD+ = chanoclavine-I aldehyde + NADH + H+

For diagram of reaction click here.

Glossary: chanoclavine-I = (1E)-2-methyl-3-[(4R,5R)-4-(methylamino)-1,3,4,5-tetrahydrobenz[cd]indol-5-yl]prop-2-en-1-ol
chanoclavine-I aldehyde = (1E)-2-methyl-3-[(4R,5R)-4-(methylamino)-1,3,4,5-tetrahydrobenz[cd]indol-5-yl]prop-2-enal

Other name(s): easD (gene name); fgaDH (gene name)

Systematic name: chanoclavine-I:NAD+ oxidoreductase

Comments: The enzyme catalyses a step in the pathway of ergot alkaloid biosynthesis in certain fungi.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Wallwey, C., Matuschek, M. and Li, S.M. Ergot alkaloid biosynthesis in Aspergillus fumigatus: conversion of chanoclavine-I to chanoclavine-I aldehyde catalyzed by a short-chain alcohol dehydrogenase FgaDH. Arch. Microbiol. 192 (2010) 127-134. [PMID: 20039019]

2. Wallwey, C., Heddergott, C., Xie, X., Brakhage, A.A. and Li, S.M. Genome mining reveals the presence of a conserved gene cluster for the biosynthesis of ergot alkaloid precursors in the fungal family Arthrodermataceae. Microbiology 158 (2012) 1634-1644. [PMID: 22403186]

[EC 1.1.1.332 created 2012]

EC 1.1.1.333

Accepted name: decaprenylphospho-β-D-erythro-pentofuranosid-2-ulose 2-reductase

Reaction: trans,octacis-decaprenylphospho-β-D-arabinofuranose + NAD+ = trans,octacis-decaprenylphospho-β-D-erythro-pentofuranosid-2-ulose + NADH + H+

For diagram of reaction click here.

Other name(s): decaprenylphospho-β-D-ribofuranose 2'-epimerase; Rv3791; DprE2

Systematic name: trans,octacis-decaprenylphospho-β-D-arabinofuranose:NAD+ 2-oxidoreductase

Comments: The reaction is catalysed in the reverse direction. The enzyme, isolated from the bacterium Mycobacterium smegmatis, is involved, along with EC 1.1.98.3, decaprenylphospho-β-D-ribofuranose 2-oxidase, in the epimerization of trans,octacis-decaprenylphospho-β-D-ribofuranose to trans,octacis-decaprenylphospho-β-D-arabinoofuranose, the arabinosyl donor for the biosynthesis of mycobacterial cell wall arabinan polymers.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Trefzer, C., Škovierová, H., Buroni, S., Bobovská, A., Nenci, S., Molteni, E., Pojer, F., Pasca, M.R., Makarov, V., Cole, S.T., Riccardi, G., Mikušová, K. and Johnsson, K. Benzothiazinones are suicide inhibitors of mycobacterial decaprenylphosphoryl-β-D-ribofuranose 2'-oxidase DprE1. J. Am. Chem. Soc. 134 (2012) 912-915. [PMID: 22188377]

[EC 1.1.1.333 created 2012]

EC 1.1.1.334

Accepted name: methylecgonone reductase

Reaction: ecgonine methyl ester + NADP+ = ecgonone methyl ester + NADPH + H+

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
ecgonone methyl ester = 2β-carbomethoxy-3-tropinone = methyl (1R,2R,5S)-8-methyl-3-oxo-8-azabicyclo[3.2.1]octane-2-carboxylate

Other name(s): MecgoR (gene name)

Systematic name: ecgonine methyl ester:NADP+ oxidoreductase

Comments: The enzyme from the plant Erythroxylum coca catalyses the penultimate step in the biosynthesis of cocaine. In vivo the reaction proceeds in the opposite direction. With NADH instead of NADPH the reaction rate is reduced to 14%. The enzyme also reduces tropinone, nortropinone and 6-hydroxytropinone but with lower reaction rates.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Jirschitzka, J., Schmidt, G.W., Reichelt, M., Schneider, B., Gershenzon, J. and D'Auria, J.C. Plant tropane alkaloid biosynthesis evolved independently in the Solanaceae and Erythroxylaceae. Proc. Natl. Acad. Sci. USA 109 (2012) 10304-10309. [PMID: 22665766]

[EC 1.1.1.334 created 2012]

EC 1.1.1.335

Accepted name: UDP-N-acetyl-2-amino-2-deoxyglucuronate dehydrogenase

Reaction: UDP-2-acetamido-2-deoxy-α-D-glucuronate + NAD+ = UDP-2-acetamido-2-deoxy-α-D-ribo-hex-3-uluronate + NADH + H+

For diagram of reaction, click here

Other name(s): WlbA; WbpB

Systematic name: UDP-N-acetyl-2-amino-2-deoxy-α-D-glucuronate:NAD+ 3-oxidoreductase

Comments: This enzyme participates in the biosynthetic pathway for UDP-α-D-ManNAc3NAcA (UDP-2,3-diacetamido-2,3-dideoxy-α-D-mannuronic acid), an important precursor of B-band lipopolysaccharide. The enzymes from Pseudomonas aeruginosa serotype O5 and Thermus thermophilus form a complex with the the enzyme catalysing the next step the pathway (EC 2.6.1.98, UDP-2-acetamido-2-deoxy-ribo-hexuluronate aminotransferase). The enzyme also possesses an EC 1.1.99.2 (L-2-hydroxyglutarate dehydrogenase) activity, and utilizes the 2-oxoglutarate produced by EC 2.6.1.98 to regenerate the tightly bound NAD+. The enzymes from Bordetella pertussis and Chromobacterium violaceum do not bind NAD+ as tightly and do not require 2-oxoglutarate to function.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Westman, E.L., McNally, D.J., Charchoglyan, A., Brewer, D., Field, R.A. and Lam, J.S. Characterization of WbpB, WbpE, and WbpD and reconstitution of a pathway for the biosynthesis of UDP-2,3-diacetamido-2,3-dideoxy-D-mannuronic acid in Pseudomonas aeruginosa. J. Biol. Chem. 284 (2009) 11854-11862. [PMID: 19282284]

2. Larkin, A. and Imperiali, B. Biosynthesis of UDP-GlcNAc(3NAc)A by WbpB, WbpE, and WbpD: enzymes in the Wbp pathway responsible for O-antigen assembly in Pseudomonas aeruginosa PAO1. Biochemistry 48 (2009) 5446-5455. [PMID: 19348502]

3. Thoden, J.B. and Holden, H.M. Structural and functional studies of WlbA: A dehydrogenase involved in the biosynthesis of 2,3-diacetamido-2,3-dideoxy-D-mannuronic acid. Biochemistry 49 (2010) 7939-7948. [PMID: 20690587]

4. Thoden, J.B. and Holden, H.M. Biochemical and structural characterization of WlbA from Bordetella pertussis and Chromobacterium violaceum: enzymes required for the biosynthesis of 2,3-diacetamido-2,3-dideoxy-D-mannuronic acid. Biochemistry 50 (2011) 1483-1491. [PMID: 21241053]

[EC 1.1.1.335 created 2012]

EC 1.1.1.336

Accepted name: UDP-N-acetyl-D-mannosamine dehydrogenase

Reaction: UDP-N-acetyl-α-D-mannosamine + 2 NAD+ + H2O = UDP-N-acetyl-α-D-mannosaminuronate + 2 NADH + 2 H+

For diagram of reaction click here.

Other name(s): UDP-ManNAc 6-dehydrogenase; wecC (gene name)

Systematic name: UDP-N-acetyl-α-D-mannosamine:NAD+ 6-oxidoreductase

Comments: Part of the pathway for acetamido sugar biosynthesis in bacteria and archaea. The enzyme has no activity with NADP+.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Namboori, S.C. and Graham, D.E. Acetamido sugar biosynthesis in the Euryarchaea. J. Bacteriol. 190 (2008) 2987-2996. [PMID: 18263721]

[EC 1.1.1.336 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 L-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, CAS registry number:

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. [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. [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. [PMID: 15758220]

[EC 1.1.1.337 created 2012]

EC 1.1.1.338

Accepted name: (2R)-3-sulfolactate dehydrogenase (NADP+)

Reaction: (2R)-3-sulfolactate + NADP+ = 3-sulfopyruvate + NADPH + H+

For diagram of reaction click here

Other name(s): (R)-sulfolactate:NADP+ oxidoreductase; L-sulfolactate dehydrogenase; (R)-sulfolactate dehydrogenase; ComC

Systematic name: (2R)-3-sulfolactate:NADP+ oxidoreductase

Comments: The enzyme from the bacterium Chromohalobacter salexigens can only utilize NADP+. It functions both biosynthetically in coenzyme M biosynthesis and degradatively, in the degradation of sulfolactate. It can not use (S)-malate and (S)-lactate.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Denger, K. and Cook, A.M. Racemase activity effected by two dehydrogenases in sulfolactate degradation by Chromohalobacter salexigens: purification of (S)-sulfolactate dehydrogenase. Microbiology 156 (2010) 967-974. [PMID: 20007648]

[EC 1.1.1.338 created 2012]

EC 1.1.1.339

Accepted name: dTDP-6-deoxy-L-talose 4-dehydrogenase (NAD+)

Reaction: dTDP-6-deoxy-β-L-talose + NAD+ = dTDP-4-dehydro-β-L-rhamnose + NADH + H+

Glossary: dTDP-4-dehydro-β-L-rhamnose = dTDP-4-dehydro-6-deoxy-β-L-mannose
dTDP-6-deoxy-β-L-talose = dTDP-β-L-pneumose

Other name(s): tll (gene name)

Systematic name: dTDP-6-deoxy-β-L-talose:NAD+ 4-oxidoreductase

Comments: The enzyme has been characterized from the bacterium Aggregatibacter actinomycetemcomitans, in which it participates in the biosynthesis of the serotype c-specific polysaccharide antigen. Shows no activity with NADP+.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Nakano, Y., Suzuki, N., Yoshida, Y., Nezu, T., Yamashita, Y. and Koga, T. Thymidine diphosphate-6-deoxy-L-lyxo-4-hexulose reductase synthesizing dTDP-6-deoxy-L-talose from Actinobacillus actinomycetemcomitans. J. Biol. Chem. 275 (2000) 6806-6812. [PMID: 10702238]

[EC 1.1.1.339 created 2012]

EC 1.1.1.340

Accepted name: 1-deoxy-11β-hydroxypentalenate dehydrogenase

Reaction: 1-deoxy-11β-hydroxypentalenate + NAD+ = 1-deoxy-11-oxopentalenate + NADH + H+

For diagram of reaction click here.

Glossary: 1-deoxy-11β-hydroxypentalenate = (1S,2R,3aR,5aS,8aR)-2-hydroxy-1,7,7-trimethyl-1,2,3,3a,5a,6,7,8-octahydrocyclopenta[c]pentalene-4-carboxylate
1-deoxy-11-oxopentalenate = (1S,3aR,5aS)-1,7,7-trimethyl-2-oxo-1,2,3,3a,5a,6,7,8-octahydrocyclopenta[c]pentalene-4-carboxylate

Other name(s): 1-deoxy-11β-hydroxypentalenic acid dehydrogenase; ptlF (gene name); penF (gene name)

Systematic name: 1-deoxy-11β-hydroxypentalenate:NAD+ oxidoreductase

Comments: Isolated from the bacterium Streptomyces avermitilis and present in many other Streptomyces species. Part of the pathway for pentalenolactone biosynthesis.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. You, Z., Omura, S., Ikeda, H. and Cane, D.E. Pentalenolactone biosynthesis: Molecular cloning and assignment of biochemical function to PtlF, a short-chain dehydrogenase from Streptomyces avermitilis, and identification of a new biosynthetic intermediate. Arch. Biochem. Biophys. 459 (2007) 233-240. [PMID: 17178094]

[EC 1.1.1.340 created 2012]

EC 1.1.1.341

Accepted name: CDP-abequose synthase

Reaction: CDP-α-D-abequose + NADP+ = CDP-4-dehydro-3,6-dideoxy-α-D-glucose + NADPH + H+

For diagram of reaction click here.

Glossary: CDP-α-D-abequose = CDP-3,6-dideoxy-α-D-xylo-hexose

Other name(s): rfbJ (gene name)

Systematic name: CDP-α-D-abequose:NADP+ 4-oxidoreductase

Comments: Isolated from Yersinia pseudotuberculosis [1,3] and Salmonella enterica [1,2].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Kessler, A.C., Brown, P.K., Romana, L.K. and Reeves, P.R. Molecular cloning and genetic characterization of the rfb region from Yersinia pseudotuberculosis serogroup IIA, which determines the formation of the 3,6-dideoxyhexose abequose. J. Gen. Microbiol. 137 (1991) 2689-2695. [PMID: 1724263]

2. Wyk, P. and Reeves, P. Identification and sequence of the gene for abequose synthase, which confers antigenic specificity on group B salmonellae: homology with galactose epimerase. J. Bacteriol. 171 (1989) 5687-5693. [PMID: 2793832]

3. Thorson, J.S., Lo, S.F., Ploux, O., He, X. and Liu, H.W. Studies of the biosynthesis of 3,6-dideoxyhexoses: molecular cloning and characterization of the asc (ascarylose) region from Yersinia pseudotuberculosis serogroup VA. J. Bacteriol. 176 (1994) 5483-5493. [PMID: 8071227]

[EC 1.1.1.341 created 2012]

EC 1.1.1.342

Accepted name: CDP-paratose synthase

Reaction: CDP-α-D-paratose + NADP+ = CDP-4-dehydro-3,6-dideoxy-α-D-glucose + NADPH + H+

For diagram of reaction click here.

Glossary: CDP-α-D-paratose = CDP-3,6-dideoxy-α-D-glucose = CDP-3,6-dideoxy-α-D-ribo-hexose

Other name(s): rfbS (gene name)

Systematic name: CDP-α-D-paratose:NADP+ 4-oxidoreductase

Comments: The enzyme is involved in synthesis of paratose and tyvelose, unusual 3,6-dideoxyhexose sugars that form part of the O-antigen in the lipopolysaccharides of several enteric bacteria. Isolated from Salmonella enterica subsp. enterica serovar Typhi (Salmonella typhi).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Verma, N. and Reeves, P. Identification and sequence of rfbS and rfbE, which determine antigenic specificity of group A and group D salmonellae. J. Bacteriol. 171 (1989) 5694-5701. [PMID: 2793833]

2. Hallis, T.M., Lei, Y., Que, N.L. and Liu, H. Mechanistic studies of the biosynthesis of paratose: purification and characterization of CDP-paratose synthase. Biochemistry 37 (1998) 4935-4945. [PMID: 9538012]

[EC 1.1.1.342 created 2012]

EC 1.1.1.343

Accepted name: phosphogluconate dehydrogenase (NAD+-dependent, decarboxylating)

Reaction: 6-phospho-D-gluconate + NAD+ = D-ribulose 5-phosphate + CO2 + NADH + H+

For diagram of reaction click here.

Other name(s): 6-PGDH (ambiguous); gntZ (gene name); GNDl

Systematic name: 6-phospho-D-gluconate:NAD+ 2-oxidoreductase (decarboxylating)

Comments: Highly specific for NAD+. The enzyme catalyses both the oxidation and decarboxylation of 6-phospho-D-gluconate. In the bacterium Methylobacillus flagellatus the enzyme participates in a formaldehyde oxidation pathway [4]. cf. EC 1.1.1.44, phosphogluconate dehydrogenase (NADP+-dependent, decarboxylating).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Kiriuchin, M. Y., Kletsova, L. V., Chistoserdov, A. Y. and Tsygankov, Y. D. Properties of glucose 6-phosphate and 6-phosphogluconate dehydrogenases of the obligate methylotroph Methylobacillus flagellatum KT. FEMS Microbiology Letters 52 (1988) 199-204.

2. Ohara, H., Russell, R.A., Uchida, K. and Kondo, H. Purification and characterization of NAD-specific 6-phosphogluconate dehydrogenase from Leuconostoc lactis SHO-54. J. Biosci. Bioeng. 98 (2004) 126-128. [PMID: 16233677]

3. Zamboni, N., Fischer, E., Laudert, D., Aymerich, S., Hohmann, H.P. and Sauer, U. The Bacillus subtilis yqjI gene encodes the NADP+-dependent 6-P-gluconate dehydrogenase in the pentose phosphate pathway. J. Bacteriol. 186 (2004) 4528-4534. [PMID: 15231785]

4. Chistoserdova, L., Gomelsky, L., Vorholt, J.A., Gomelsky, M., Tsygankov, Y.D. and Lidstrom, M.E. Analysis of two formaldehyde oxidation pathways in Methylobacillus flagellatus KT, a ribulose monophosphate cycle methylotroph. Microbiology 146 (2000) 233-238. [PMID: 10658669]

[EC 1.1.1.343 created 2013]

EC 1.1.1.344

Accepted name: dTDP-6-deoxy-L-talose 4-dehydrogenase [NAD(P)+]

Reaction: dTDP-6-deoxy-β-L-talose + NAD(P)+ = dTDP-4-dehydro-β-L-rhamnose + NAD(P)H + H+

Glossary: dTDP-4-dehydro-β-L-rhamnose = dTDP-4-dehydro-6-deoxy-β-L-mannose
dTDP-6-deoxy-β-L-talose = dTDP-β-L-pneumose

Other name(s): tal (gene name)

Systematic name: dTDP-6-deoxy-β-L-talose:NAD(P)+ 4-oxidoreductase

Comments: The enzyme works equally well with NAD+ and NADP+.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Karki, S., Yoo, H.G., Kwon, S.Y., Suh, J.W. and Kwon, H.J. Cloning and in vitro characterization of dTDP-6-deoxy-L-talose biosynthetic genes from Kitasatospora kifunensis featuring the dTDP-6-deoxy-L-lyxo-4-hexulose reductase that synthesizes dTDP-6-deoxy-L-talose. Carbohydr. Res. 345 (2010) 1958-1962. [PMID: 20667525]

[EC 1.1.1.344 created 2013]

EC 1.1.1.345

Reaction: an (R)-2-hydroxycarboxylate + NAD+ = a 2-oxocarboxylate + NADH + H+

Other name(s): LdhA; HdhD; D-2-hydroxyisocaproate dehydrogenase; R-HicDH; D-HicDH; (R)-2-hydroxy-4-methylpentanoate:NAD+ oxidoreductase; (R)-2-hydroxyisocaproate dehydrogenase; D-mandelate dehydrogenase (ambiguous)

Systematic name: (R)-2-hydroxycarboxylate:NAD+ oxidoreductase

Comments: The enzymes, characterized from bacteria (Peptoclostridium difficile, Enterococcus faecalis and from lactic acid bacteria) prefer substrates with a main chain of 5 carbons (such as 4-methyl-2-oxopentanoate) to those with a shorter chain. It also utilizes phenylpyruvate. The enzyme from the halophilic archaeon Haloferax mediterranei prefers substrates with a main chain of 3-4 carbons (pyruvate and 2-oxobutanoate). cf. EC 1.1.1.272, (D)-2-hydroxyacid dehydrogenase (NADP+).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Dengler, U., Niefind, K., Kiess, M. and Schomburg, D. Crystal structure of a ternary complex of D-2-hydroxyisocaproate dehydrogenase from Lactobacillus casei, NAD+ and 2-oxoisocaproate at 1.9 Å resolution. J. Mol. Biol. 267 (1997) 640-660. [PMID: 9126843]

2. Bonete, M.J., Ferrer, J., Pire, C., Penades, M. and Ruiz, J.L. 2-Hydroxyacid dehydrogenase from Haloferax mediterranei, a D-isomer-specific member of the 2-hydroxyacid dehydrogenase family. Biochimie 82 (2000) 1143-1150. [PMID: 11120357]

3. Kim, J., Darley, D., Selmer, T. and Buckel, W. Characterization of (R)-2-hydroxyisocaproate dehydrogenase and a family III coenzyme A transferase involved in reduction of L-leucine to isocaproate by Clostridium difficile. Appl. Environ. Microbiol. 72 (2006) 6062-6069. [PMID: 16957230]

4. Wada, Y., Iwai, S., Tamura, Y., Ando, T., Shinoda, T., Arai, K. and Taguchi, H. A new family of D-2-hydroxyacid dehydrogenases that comprises D-mandelate dehydrogenases and 2-ketopantoate reductases. Biosci. Biotechnol. Biochem. 72 (2008) 1087-1094. [PMID: 18391442]

5. Chambellon, E., Rijnen, L., Lorquet, F., Gitton, C., van Hylckama Vlieg, J.E., Wouters, J.A. and Yvon, M. The D-2-hydroxyacid dehydrogenase incorrectly annotated PanE is the sole reduction system for branched-chain 2-keto acids in Lactococcus lactis. J. Bacteriol. 191 (2009) 873-881. [PMID: 19047348]

6. Miyanaga, A., Fujisawa, S., Furukawa, N., Arai, K., Nakajima, M. and Taguchi, H. The crystal structure of D-mandelate dehydrogenase reveals its distinct substrate and coenzyme recognition mechanisms from those of 2-ketopantoate reductase. Biochem. Biophys. Res. Commun. 439 (2013) 109-114. [PMID: 23954635]

[EC 1.1.1.345 created 2013]

EC 1.1.1.346

Accepted name: 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming)

Reaction: 2-dehydro-L-gulonate + NADP+ = 2,5-didehydro-D-gluconate + NADPH + H+

Glossary: 2-dehydro-L-gulonate = 2-dehydro-L-idonate = 2-keto-L-gulonate

Other name(s): 2,5-diketo-D-gluconate-reductase (ambiguous); YqhE reductase; dkgA (gene name); dkgB (gene name)

Systematic name: 2-dehydro-D-gluconate:NADP+ 2-oxidoreductase (2-dehydro-L-gulonate-forming)

Comments: The enzyme is involved in ketogluconate metabolism, and catalyses the reaction in vivo in the reverse direction to that shown [1]. It is used in the commercial microbial production of ascorbate. cf. EC 1.1.1.274, 2,5-didehydrogluconate reductase (2-dehydro-D-gluconate-forming).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Sonoyama, T. and Kobayashi, K. Purification and properties of two 2,5-diketo-D-gluconate reductases from a mutant strain derived from Corynebacterium sp. J Ferment Technol. 65 (1987) 311-317.

2. Miller, J.V., Estell, D.A. and Lazarus, R.A. Purification and characterization of 2,5-diketo-D-gluconate reductase from Corynebacterium sp. J. Biol. Chem. 262 (1987) 9016-9020. [PMID: 3597405]

3. Yum, D.Y., Lee, B.Y. and Pan, J.G. Identification of the yqhE and yafB genes encoding two 2,5-diketo-D-gluconate reductases in Escherichia coli. Appl. Environ. Microbiol. 65 (1999) 3341-3346. [PMID: 10427017]

4. Maremonti, M., Greco, G. and Wichmann, R. Characterisation of 2,5-diketo-D-gluconic acid reductase from Corynebacterium sp. Biotechnology Letters 18 (1996) 845-850.

5. Khurana, S., Powers, D.B., Anderson, S. and Blaber, M. Crystal structure of 2,5-diketo-D-gluconic acid reductase A complexed with NADPH at 2.1-Å resolution. Proc. Natl. Acad. Sci. USA 95 (1998) 6768-6773. [PMID: 9618487]

[EC 1.1.1.346 created 2013]

EC 1.1.1.347

Accepted name: geraniol dehydrogenase (NAD+)

Reaction: geraniol + NAD+ = geranial + NADH + H+

For diagram of reaction click here.

Other name(s): GeDH; geoA (gene name)

Systematic name: geraniol:NAD+ oxidoreductase

Comments: The enzyme from the bacterium Castellaniella defragrans is most active in vitro with perillyl alcohol [2]. The enzyme from the prune mite Carpoglyphus lactis also acts (more slowly) on farnesol but not on nerol [1].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Noge, K., Kato, M., Mori, N., Kataoka, M., Tanaka, C., Yamasue, Y., Nishida, R. and Kuwahara, Y. Geraniol dehydrogenase, the key enzyme in biosynthesis of the alarm pheromone, from the astigmatid mite Carpoglyphus lactis (Acari: Carpoglyphidae). FEBS J. 275 (2008) 2807-2817. [PMID: 18422649]

2. Lüddeke, F., Wülfing, A., Timke, M., Germer, F., Weber, J., Dikfidan, A., Rahnfeld, T., Linder, D., Meyerdierks, A. and Harder, J. Geraniol and geranial dehydrogenases induced in anaerobic monoterpene degradation by Castellaniella defragrans. Appl. Environ. Microbiol. 78 (2012) 2128-2136. [PMID: 22286981]

[EC 1.1.1.347 created 2013]

EC 1.1.1.348

Accepted name: (3R)-2'-hydroxyisoflavanone reductase

Reaction: a (4R)-4,2'-dihydroxyisoflavan + NADP+ = a (3R)-2'-hydroxyisoflavanone + NADPH + H+

For diagram of reaction click here

Glossary: (3R)-vestitone = (3R)-2',7-dihydroxy-4'-methoxyisoflavanone

Other name(s): vestitone reductase; pterocarpin synthase (incorrect); pterocarpan synthase (incorrect)

Systematic name: (3R)-2'-hydroxyisoflavanone:NADP+ 4-oxidoreductase

Comments: This plant enzyme participates in the biosynthesis of the pterocarpan phytoalexins medicarpin, maackiain, and several forms of glyceollin. The ezyme has a strict stereo specificity for the 3R-isoflavanones.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 118477-70-6

References:

1. Bless, W. and Barz, W. Isolation of pterocarpan synthase, the terminal enzyme of pterocarpan phytoalexin biosynthesis in cell-suspension cultures of Cicer arietinum. FEBS Lett. 235 (1988) 47-50.

2. Guo, L., Dixon, R.A. and Paiva, N.L. Conversion of vestitone to medicarpin in alfalfa (Medicago sativa L.) is catalyzed by two independent enzymes. Identification, purification, and characterization of vestitone reductase and 7,2'-dihydroxy-4'-methoxyisoflavanol dehydratase. J. Biol. Chem. 269 (1994) 22372-22378. [PMID: 8071365]

3. Guo, L., Dixon, R.A. and Paiva, N.L. The ‘pterocarpan synthase’ of alfalfa: association and co-induction of vestitone reductase and 7,2'-dihydroxy-4'-methoxy-isoflavanol (DMI) dehydratase, the two final enzymes in medicarpin biosynthesis. FEBS Lett. 356 (1994) 221-225. [PMID: 7805842]

4. Guo, L. and Paiva, N.L. Molecular cloning and expression of alfalfa (Medicago sativa L.) vestitone reductase, the penultimate enzyme in medicarpin biosynthesis. Arch. Biochem. Biophys. 320 (1995) 353-360. [PMID: 7625843]

5. Shao, H., Dixon, R.A. and Wang, X. Crystal structure of vestitone reductase from alfalfa (Medicago sativa L.). J. Mol. Biol. 369 (2007) 265-276. [PMID: 17433362]

[EC 1.1.1.348 created 1992 as EC 1.1.1.246, part transferred 2013 to EC 1.1.1.348]

EC 1.1.1.349

Accepted name: norsolorinic acid ketoreductase

Reaction: (1'S)-averantin + NADP+ = norsolorinic acid + NADPH + H+

For diagram of reaction click here.

Glossary: norsolorinic acid = 2-hexanoyl-1,3,6,8-tetrahydroxy-9,10-anthraquinone
(1'S)-averantin = 1,3,6,8-tetrahydroxy-[(1S)-2-hydroxyhexyl]-9,10-anthraquinone

Other name(s): aflD (gene name); nor-1 (gene name)

Systematic name: (1'S)-averantin:NADP+ oxidoreductase

Comments: Involved in the synthesis of aflatoxins in the fungus Aspergillus parasiticus.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Yabe, K., Matsuyama, Y., Ando, Y., Nakajima, H. and Hamasaki, T. Stereochemistry during aflatoxin biosynthesis: conversion of norsolorinic acid to averufin. Appl. Environ. Microbiol. 59 (1993) 2486-2492. [PMID: 8368836]

2. Zhou, R. and Linz, J.E. Enzymatic function of the nor-1 protein in aflatoxin biosynthesis in Aspergillus parasiticus. Appl. Environ. Microbiol. 65 (1999) 5639-5641. [PMID: 10584035]

[EC 1.1.1.349 created 2013]

EC 1.1.1.350

Accepted name: ureidoglycolate dehydrogenase (NAD+)

Reaction: (S)-ureidoglycolate + NAD+ = oxalurate + NADH + H+

For diagram of reaction 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, CAS registry number:

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 (2012) e52066. [PMID: 23284870]

[EC 1.1.1.350 created 2013]


Continue with EC 1.1.1.351 to EC 1.1.1.413
Return to EC 1 home page
Return to Enzymes home page
Return to IUBMB Biochemical Nomenclature home page