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
EC 1.1.1.301 to EC 1.1.1.350

Contents

EC 1.1.1.351 phosphogluconate dehydrogenase [NAD(P)+-dependent, decarboxylating]
EC 1.1.1.352 5'-hydroxyaverantin dehydrogenase
EC 1.1.1.353 versiconal hemiacetal acetate reductase
EC 1.1.1.354 farnesol dehydrogenase (NAD+)
EC 1.1.1.355 2'-dehydrokanamycin reductase
EC 1.1.1.356 GDP-L-colitose synthase
EC 1.1.1.357 3α-hydroxysteroid 3-dehydrogenase
EC 1.1.1.358 2-dehydropantolactone reductase
EC 1.1.1.359 aldose 1-dehydrogenase [NAD(P)+]
EC 1.1.1.360 glucose/galactose 1-dehydrogenase
EC 1.1.1.361 glucose-6-phosphate 3-dehydrogenase
EC 1.1.1.362 aklaviketone reductase
EC 1.1.1.363 glucose-6-phosphate dehydrogenase [NAD(P)+]
EC 1.1.1.364 dTDP-4-dehydro-6-deoxy-α-D-gulose 4-ketoreductase
EC 1.1.1.365 D-galacturonate reductase
EC 1.1.1.366 L-idonate 5-dehydrogenase (NAD+)
EC 1.1.1.367 UDP-2-acetamido-2,6-β-L-arabino-hexul-4-ose reductase
EC 1.1.1.368 6-hydroxycyclohex-1-ene-1-carbonyl-CoA dehydrogenase
EC 1.1.1.369 D-chiro-inositol 1-dehydrogenase
EC 1.1.1.370 scyllo-inositol 2-dehydrogenase (NAD+)
EC 1.1.1.371 scyllo-inositol 2-dehydrogenase (NADP+)
EC 1.1.1.372 D/L-glyceraldehyde reductase
EC 1.1.1.373 sulfolactaldehyde 3-reductase
EC 1.1.1.374 UDP-N-acetylglucosamine 3-dehydrogenase
EC 1.1.1.375 L-2-hydroxycarboxylate dehydrogenase [NAD(P)+]
EC 1.1.1.376 L-arabinose 1-dehydrogenase [NAD(P)+]
EC 1.1.1.377 L-rhamnose 1-dehydrogenase (NADP+)
EC 1.1.1.378 L-rhamnose 1-dehydrogenase [NAD(P)+]
EC 1.1.1.379 (R)-mandelate dehydrogenase
EC 1.1.1.380 L-gulonate 5-dehydrogenase
EC 1.1.1.381 3-hydroxy acid dehydrogenase
EC 1.1.1.382 ketol-acid reductoisomerase (NAD+)
EC 1.1.1.383 ketol-acid reductoisomerase [NAD(P)+]
EC 1.1.1.384 dTDP-3,4-didehydro-2,6-dideoxy-α-D-glucose 3-reductase
EC 1.1.1.385 dihydroanticapsin dehydrogenase
EC 1.1.1.386 ipsdienol dehydrogenase
EC 1.1.1.387 L-serine 3-dehydrogenase (NAD+)
EC 1.1.1.388 glucose-6-phosphate dehydrogenase (NAD+)
EC 1.1.1.389 2-dehydro-3-deoxy-L-galactonate 5-dehydrogenase
EC 1.1.1.390 sulfoquinovose 1-dehydrogenase
EC 1.1.1.391 3β-hydroxycholanate 3-dehydrogenase (NAD+)
EC 1.1.1.392 3α-hydroxycholanate dehydrogenase (NADP+)
EC 1.1.1.393 3β-hydroxycholanate 3-dehydrogenase (NADP+)
EC 1.1.1.394 aurachin B dehydrogenase
EC 1.1.1.395 3α-hydroxy bile acid-CoA-ester 3-dehydrogenase
EC 1.1.1.396 bacteriochlorophyllide a dehydrogenase
EC 1.1.1.397 β-methylindole-3-pyruvate reductase
EC 1.1.1.398 2-glutathionyl-2-methylbut-3-en-1-ol dehydrogenase
EC 1.1.1.399 2-oxoglutarate reductase
EC 1.1.1.400 2-methyl-1,2-propanediol dehydrogenase
EC 1.1.1.401 2-dehydro-3-deoxy-L-rhamnonate dehydrogenase (NAD+)
EC 1.1.1.402 D-erythritol 1-phosphate dehydrogenase
EC 1.1.1.403 D-threitol dehydrogenase (NAD+)
EC 1.1.1.404 tetrachlorobenzoquinone reductase
EC 1.1.1.405 ribitol-5-phosphate 2-dehydrogenase (NADP+)
EC 1.1.1.406 galactitol 2-dehydrogenase (L-tagatose-forming)
EC 1.1.1.407 D-altritol 5-dehydrogenase
EC 1.1.1.408 4-phospho-D-threonate 3-dehydrogenase
EC 1.1.1.409 4-phospho-D-erythronate 3-dehydrogenase
EC 1.1.1.410 D-erythronate 2-dehydrogenase
EC 1.1.1.411 L-threonate 2-dehydrogenase
EC 1.1.1.412 2-alkyl-3-oxoalkanoate reductase
EC 1.1.1.413 A-factor type γ-butyrolactone 1'-reductase (1S-forming)

Entries

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

EC 1.1.1.351

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

Reaction: 6-phospho-D-gluconate + NAD(P)+ = D-ribulose 5-phosphate + CO2 + NAD(P)H + H+

For diagram of reaction click here.

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

Comments: The enzyme participates in the oxidative branch of the pentose phosphate pathway, whose main purpose is to produce reducing power and pentose for biosynthetic reactions. Unlike EC 1.1.1.44, phosphogluconate dehydrogenase (NADP+-dependent, decarboxylating), it is not specific for NADP+ and can accept both cofactors with similar efficiency. cf. EC 1.1.1.343, phosphogluconate dehydrogenase [NAD+-dependent, decarboxylating].

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

References:

1. Ben-Bassat, A. and Goldberg, I. Purification and properties of glucose-6-phosphate dehydrogenase (NADP+/NAD+) and 6-phosphogluconate dehydrogenase (NADP+/NAD+) from methanol-grown Pseudomonas C. Biochim. Biophys. Acta 611 (1980) 1-10. [PMID: 7350909]

2. Stournaras, C., Maurer, P. and Kurz, G. 6-phospho-D-gluconate dehydrogenase from Pseudomonas fluorescens. Properties and subunit structure. Eur. J. Biochem. 130 (1983) 391-396. [PMID: 6402366]

3. Levy, H.R., Vought, V.E., Yin, X. and Adams, M.J. Identification of an arginine residue in the dual coenzyme-specific glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides that plays a key role in binding NADP+ but not NAD+. Arch. Biochem. Biophys. 326 (1996) 145-151. [PMID: 8579362]

[EC 1.1.1.351 created 2013]

EC 1.1.1.352

Accepted name: 5'-hydroxyaverantin dehydrogenase

Reaction: (1) (1'S,5'S)-hydroxyaverantin + NAD+ = 5'-oxoaverantin + NADH + H+
(2) (1'S,5'R)-hydroxyaverantin + NAD+ = 5'-oxoaverantin + NADH + H+

For diagram of reaction click here.

Glossary: 5'-oxoaverantin = 1,3,6,8-tetrahydroxy-2-[(1S)-1-hydroxy-5-oxohexyl]anthracene-9,10-dione

Other name(s): HAVN dehydrogenase; adhA (gene name)

Systematic name: (1'S,5'S)-hydroxyaverantin:NAD+ oxidoreductase

Comments: Isolated from the aflatoxin-producing mold Aspergillus parasiticus [2]. Involved in aflatoxin biosynthesis. 5'-Oxoaverantin will spontaneously form averufin by intramolecular ketalisation. cf. EC 4.2.1.142, 5'-oxoaverantin cyclase.

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

References:

1. Chang, P.K., Yu, J., Ehrlich, K.C., Boue, S.M., Montalbano, B.G., Bhatnagar, D. and Cleveland, T.E. adhA in Aspergillus parasiticus is involved in conversion of 5'-hydroxyaverantin to averufin. Appl. Environ. Microbiol. 66 (2000) 4715-4719. [PMID: 11055914]

2. Sakuno, E., Yabe, K. and Nakajima, H. Involvement of two cytosolic enzymes and a novel intermediate, 5'-oxoaverantin, in the pathway from 5'-hydroxyaverantin to averufin in aflatoxin biosynthesis. Appl. Environ. Microbiol. 69 (2003) 6418-6426. [PMID: 14602595]

[EC 1.1.1.352 created 2013]

EC 1.1.1.353

Accepted name: versiconal hemiacetal acetate reductase

Reaction: (1) versicolorone + NADP+ = 1'-hydroxyversicolorone + NADPH + H+
(2) versiconol acetate + NADP+ = versiconal hemiacetal acetate + NADPH + H+
(3) versiconol + NADP+ = versiconal + NADPH + H+

For diagram of reaction click here.

Glossary: 1'-hydroxyversicolorone = (2S,3S)-2,4,6,8-tetrahydroxy-3-(3-oxobutyl)anthra[2,3-b]furan-5,10-dione
versiconal = (2S,3S)-2,4,6,8-tetrahydroxy-3-(2-hydroxyethyl)anthra[2,3-b]furan-5,10-dione
versiconal hemiacetal acetate = 2-[(2S,3S)-2,4,6,8-tetrahydroxy-5,10-dioxo-5,10-dihydroanthra[2,3-b]furan-3-yl]ethyl acetate
versiconol = 1,3,6,8-tetrahydroxy-3-[(2S)-1,4-dihydroxybutan-2-yl]anthracene-5,10-dione
versiconol acetate = (3S)-4-hydroxy-3-[1,3,6,8-tetrahydroxy-9,10-dioxo-9,10-dihydroanthracen-2-yl]butyl acetate
versicolorone = 1,3,6,8-tetrahydroxy-2-[(2S)-1-hydroxy-5-oxohexan-2-yl]anthracene-5,10-dione

Other name(s): VHA reductase; VHA reductase I; VHA reductase II; vrdA (gene name)

Systematic name: versiconol-acetate:NADP+ oxidoreductase

Comments: Isolated from the mold Aspergillus parasiticus. Involved in a metabolic grid that leads to aflatoxin biosynthesis.

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

References:

1. Matsushima, K., Ando, Y., Hamasaki, T. and Yabe, K. Purification and characterization of two versiconal hemiacetal acetate reductases involved in aflatoxin biosynthesis. Appl. Environ. Microbiol. 60 (1994) 2561-2567. [PMID: 16349333]

2. Shima, Y., Shiina, M., Shinozawa, T., Ito, Y., Nakajima, H., Adachi, Y. and Yabe, K. Participation in aflatoxin biosynthesis by a reductase enzyme encoded by vrdA gene outside the aflatoxin gene cluster. Fungal Genet. Biol. 46 (2009) 221-231. [PMID: 19211038]

[EC 1.1.1.353 created 2013]

EC 1.1.1.354

Accepted name: farnesol dehydrogenase (NAD+)

Reaction: (2E,6E)-farnesol + NAD+ = (2E,6E)-farnesal + NADH + H+

For diagram of reaction click here.

Other name(s): NAD+-farnesol dehydrogenase

Systematic name: (2E,6E)-farnesol:NAD+ 1-oxidoreductase

Comments: The enzyme from the prune mite Carpoglyphus lactis also acts on geraniol with greater activity [cf. EC 1.1.1.347, geraniol dehydrogenase (NAD+)]. Unlike EC 1.1.1.216, farnesol dehydrogenase (NADP+), this enzyme cannot use NADP+ as cofactor.

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]

[EC 1.1.1.354 created 2013]

EC 1.1.1.355

Accepted name: 2'-dehydrokanamycin reductase

Reaction: kanamycin A + NADP+ = 2'-dehydrokanamycin A + NADPH + H+

For diagram of reaction click here.

Glossary: kanamycin A = (1S,2R,3R,4S,6R)-4,6-diamino-3-(6-amino-6-deoxy-α-D-glucopyranosyloxy)-2-hydroxycyclohexyl 3-amino-3-deoxy-α-D-glucopyranoside (
2'-dehydrokanamycin A = (1S,2R,3R,4S,6R)-4,6-diamino-3-[(6-amino-6-deoxy-α-D-arabino-hexopyranosyl-2-ulose)oxy]-2-hydroxycyclohexyl 3-amino-3-deoxy-α-D-glucopyranoside

Other name(s): kanK (gene name, ambiguous)

Systematic name: kanamycin A:NADP+ oxidoreductase

Comments: Found in the bacterium Streptomyces kanamyceticus where it is involved in the conversion of kanamycin B to kanamycin A.

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

References:

1. Sucipto, H., Kudo, F. and Eguchi, T. The last step of kanamycin biosynthesis: unique deamination reaction catalyzed by the α-ketoglutarate-dependent nonheme iron dioxygenase KanJ and the NADPH-dependent reductase KanK. Angew. Chem. Int. Ed. Engl. 51 (2012) 3428-3431. [PMID: 22374809]

[EC 1.1.1.355 created 2013]

EC 1.1.1.356

Accepted name: GDP-L-colitose synthase

Reaction: GDP-β-L-colitose + NAD(P)+ = GDP-4-dehydro-3,6-dideoxy-α-D-mannose + NAD(P)H + H+

Glossary: L-colitose = 3,6-dideoxy-L-xylo-hexopyranose
GDP-4-dehydro-3,6-dideoxy-α-D-mannose = GDP-3,6-dideoxy-α-D-threo-hexopyranos-4-ulose

Other name(s): ColC

Systematic name: GDP-β-L-colitose:NAD(P)+ 4-oxidoreductase (5-epimerizing)

Comments: The enzyme is involved in biosynthesis of L-colitose, a 3,6-dideoxyhexose found in the O-antigen of Gram-negative lipopolysaccharides, where it catalyses the reaction in the reverse direction. The enzyme also performs the NAD(P)H-dependent epimerisation at C-5 of the sugar. The enzyme from Yersinia pseudotuberculosis is Si-specific with respect to NAD(P)H [1].

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

References:

1. Alam, J., Beyer, N. and Liu, H.W. Biosynthesis of colitose: expression, purification, and mechanistic characterization of GDP-4-keto-6-deoxy-D-mannose-3-dehydrase (ColD) and GDP-L-colitose synthase (ColC). Biochemistry 43 (2004) 16450-16460. [PMID: 15610039]

[EC 1.1.1.356 created 2013]

EC 1.1.1.357

Accepted name: 3α-hydroxysteroid 3-dehydrogenase

Reaction: a 3α-hydroxysteroid + NAD(P)+ = a 3-oxosteroid + NAD(P)H + H+

Other name(s): 3α-hydroxysteroid dehydrogenase; AKR1C4 (gene name); AKR1C2 (gene name); hsdA (gene name)

Systematic name: 3α-hydroxysteroid:NAD(P)+ 3-oxidoreductase

Comments: The enzyme acts on multiple 3α-hydroxysteroids, such as androsterone and 5 α-dihydrotestosterone. The mammalian enzymes are involved in inactivation of steroid hormones, while the bacterial enzymes are involved in steroid degradation. This entry stands for enzymes whose stereo-specificity with respect to NAD+ or NADP+ is not known. [cf. EC 1.1.1.50, 3α-hydroxysteroid 3-dehydrogenase (Si-specific) and EC 1.1.1.213, 3α-hydroxysteroid 3-dehydrogenase (Re-specific)].

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

References:

1. Deyashiki, Y., Ogasawara, A., Nakayama, T., Nakanishi, M., Miyabe, Y., Sato, K. and Hara, A. Molecular cloning of two human liver 3 α-hydroxysteroid/dihydrodiol dehydrogenase isoenzymes that are identical with chlordecone reductase and bile-acid binder. Biochem. J. 299 (1994) 545-552. [PMID: 8172617]

2. Khanna, M., Qin, K.N., Wang, R.W. and Cheng, K.C. Substrate specificity, gene structure, and tissue-specific distribution of multiple human 3 α-hydroxysteroid dehydrogenases. J. Biol. Chem. 270 (1995) 20162-20168. [PMID: 7650035]

3. Oppermann, U.C. and Maser, E. Characterization of a 3 α-hydroxysteroid dehydrogenase/carbonyl reductase from the gram-negative bacterium Comamonas testosteroni. Eur. J. Biochem. 241 (1996) 744-749. [PMID: 8944761]

4. Mobus, E. and Maser, E. Molecular cloning, overexpression, and characterization of steroid-inducible 3α-hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni. A novel member of the short-chain dehydrogenase/reductase superfamily. J. Biol. Chem. 273 (1998) 30888-30896. [PMID: 9812981]

5. Nahoum, V., Gangloff, A., Legrand, P., Zhu, D.W., Cantin, L., Zhorov, B.S., Luu-The, V., Labrie, F., Breton, R. and Lin, S.X. Structure of the human 3α-hydroxysteroid dehydrogenase type 3 in complex with testosterone and NADP at 1.25-Å resolution. J. Biol. Chem. 276 (2001) 42091-42098. [PMID: 11514561]

[EC 1.1.1.357 created 2013]

EC 1.1.1.358

Accepted name: 2-dehydropantolactone reductase

Reaction: (R)-pantolactone + NADP+ = 2-dehydropantolactone + NADPH + H+

Other name(s): 2-oxopantoyl lactone reductase; 2-ketopantoyl lactone reductase; ketopantoyl lactone reductase; 2-dehydropantoyl-lactone reductase

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

Comments: The enzyme participates in an alternative pathway for biosynthesis of (R)-pantothenate (vitamin B5). This entry covers enzymes whose stereo specificity for NADP+ is not known. cf. EC 1.1.1.168 2-dehydropantolactone reductase (Re-specific) and EC 1.1.1.214, 2-dehydropantolactone reductase (Si-specific).

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

References:

1. Hata, H., Shimizu, S., Hattori, S. and Yamada, H. Ketopantoyl-lactone reductase from Candida parapsilosis: purification and characterization as a conjugated polyketone reductase. Biochim. Biophys. Acta 990 (1989) 175-181. [PMID: 2644973]

[EC 1.1.1.358 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+

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, CAS registry number:

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. [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. [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. [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. [PMID: 21265750]

[EC 1.1.1.359 created 2013]

EC 1.1.1.360

Accepted name: glucose/galactose 1-dehydrogenase

Reaction: (1) D-glucopyranose + NADP+ = D-glucono-1,5-lactone + NADPH + H+
(2) D-galactopyranose + NADP+ = D-galactono-1,5-lactone + NADPH + H+

For diagram of reaction click here.

Other name(s): GdhA; dual-specific glucose/galactose dehydrogenase; glucose (galactose) dehydrogenase; glucose/galactose dehydrogenase

Systematic name: D-glucose/D-galactose 1-dehydrogenase (NADPH)

Comments: A zinc protein. The enzyme from the archaeon Picrophilus torridus is involved in glucose and galactose catabolism via the nonphosphorylative variant of the Entner-Doudoroff pathway. It shows 20-fold higher activity with NADP+ compared tor NAD+. The oxidation of D-glucose and D-galactose is catalysed at a comparable rate (cf. EC 1.1.1.119, glucose 1-dehydrogenase (NADP+) and EC 1.1.1.120, galactose 1-dehydrogenase (NADP+)).

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

References:

1. Angelov, A., Futterer, O., Valerius, O., Braus, G.H. and Liebl, W. Properties of the recombinant glucose/galactose dehydrogenase from the extreme thermoacidophile, Picrophilus torridus. FEBS J. 272 (2005) 1054-1062. [PMID: 15691337]

2. 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. [PMID: 16556607]

[EC 1.1.1.360 created 2013]

EC 1.1.1.361

Accepted name: glucose-6-phosphate 3-dehydrogenase

Reaction: D-glucose 6-phosphate + NAD+ = 3-dehydro-D-glucose 6-phosphate + NADH + H+

For diagram of reaction click here.

Glossary: kanosamine = 3-amino-3-deoxy-D-glucose

Other name(s): ntdC (gene name)

Systematic name: D-glucose-6-phosphate:NAD+ oxidoreductase

Comments: The enzyme, found in the bacterium Bacillus subtilis, is involved in a kanosamine biosynthesis pathway.

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

References:

1. Vetter, N.D., Langill, D.M., Anjum, S., Boisvert-Martel, J., Jagdhane, R.C., Omene, E., Zheng, H., van Straaten, K.E., Asiamah, I., Krol, E.S., Sanders, D.A. and Palmer, D.R. A previously unrecognized kanosamine biosynthesis pathway in Bacillus subtilis. J. Am. Chem. Soc. 135 (2013) 5970-5973. [PMID: 23586652]

[EC 1.1.1.361 created 2013]

EC 1.1.1.362

Accepted name: aklaviketone reductase

Reaction: aklavinone + NADP+ = aklaviketone + NADPH + H+

For diagram of reaction click here.

Glossary: aklavinone = methyl (1R,2R,4S)-2-ethyl-2,4,5,7-tetrahydroxy-6,11-dioxo-1,2,3,4,6,11-hexahydrotetracene-1-carboxylate
aklaviketone = methyl (1R,2R)-2-ethyl-2,5,7-trihydroxy-4,6,11-trioxo-1,2,3,4,6,11-hexahydrotetracene-1-carboxylate

Other name(s): dauE (gene name); aknU (gene name)

Systematic name: aklavinone:NADP+ oxidoreductase

Comments: The enzyme is involved in the synthesis of the aklavinone aglycone, a common precursor for several anthracycline antibiotics including aclacinomycins, daunorubicin and doxorubicin. The enzyme from the Gram-negative bacterium Streptomyces sp. C5 produces daunomycin.

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

References:

1. Dickens, M.L., Ye, J. and Strohl, W.R. Cloning, sequencing, and analysis of aklaviketone reductase from Streptomyces sp. strain C5. J. Bacteriol. 178 (1996) 3384-3388. [PMID: 8655529]

[EC 1.1.1.362 created 2013]

EC 1.1.1.363

Accepted name: glucose-6-phosphate dehydrogenase [NAD(P)+]

Reaction: D-glucose 6-phosphate + NAD(P)+ = 6-phospho-D-glucono-1,5-lactone + NAD(P)H + H+

Other name(s): G6PDH; G6PD; Glc6PD

Systematic name: D-glucose-6-phosphate:NAD(P)+ 1-oxidoreductase

Comments: The enzyme catalyses a step of the pentose phosphate pathway. The enzyme from the Gram-positive bacterium Leuconostoc mesenteroides prefers NADP+ while the enzyme from the Gram-negative bacterium Gluconacetobacter xylinus prefers NAD+. cf. EC 1.1.1.49, glucose-6-phosphate dehydrogenase (NADP+) and EC 1.1.1.388, glucose-6-phosphate dehydrogenase (NAD+).

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

References:

1. Olive, C., Geroch, M.E. and Levy, H.R. Glucose 6-phosphate dehydrogenase from Leuconostoc mesenteroides. Kinetic studies. J. Biol. Chem. 246 (1971) 2047-2057. [PMID: 4396688]

2. Lee, W.T. and Levy, H.R. Lysine-21 of Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase participates in substrate binding through charge-charge interaction. Protein Sci. 1 (1992) 329-334. [PMID: 1304341]

3. Cosgrove, M.S., Naylor, C., Paludan, S., Adams, M.J. and Levy, H.R. On the mechanism of the reaction catalyzed by glucose 6-phosphate dehydrogenase. Biochemistry 37 (1998) 2759-2767. [PMID: 9485426]

4. Ragunathan, S. and Levy, H.R. Purification and characterization of the NAD-preferring glucose 6-phosphate dehydrogenase from Acetobacter hansenii (Acetobacter xylinum). Arch. Biochem. Biophys. 310 (1994) 360-366. [PMID: 8179320]

[EC 1.1.1.363 created 2013, modified 2015]

EC 1.1.1.364

Accepted name: dTDP-4-dehydro-6-deoxy-α-D-gulose 4-ketoreductase

Reaction: dTDP-6-deoxy-α-D-allose + NAD(P)+ = dTDP-4-dehydro-6-deoxy-α-D-gulose + NAD(P)H + H+

For diagram of reaction, click here

Glossary: dTDP-4-dehydro-6-deoxy-α-D-gulose = dTDP-4-dehydro-6-deoxy-α-D-allose

Other name(s): dTDP-4-dehydro-6-deoxygulose reductase; tylD (gene name); gerKI (gene name); chmD (gene name); mydI (gene name)

Systematic name: dTDP-6-deoxy-α-D-allose:NAD(P)+ oxidoreductase

Comments: The enzyme forms an activated deoxy-α-D-allose, which is converted to mycinose after attachment to the aglycones of several macrolide antibiotics, including tylosin, chalcomycin, dihydrochalcomycin, and mycinamicin II.

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

References:

1. Bate, N. and Cundliffe, E. The mycinose-biosynthetic genes of Streptomyces fradiae, producer of tylosin. J Ind Microbiol Biotechnol 23 (1999) 118-122. [PMID: 10510490]

2. Anzai, Y., Saito, N., Tanaka, M., Kinoshita, K., Koyama, Y. and Kato, F. Organization of the biosynthetic gene cluster for the polyketide macrolide mycinamicin in Micromonospora griseorubida. FEMS Microbiol. Lett. 218 (2003) 135-141. [PMID: 12583909]

3. Thuy, T.T., Liou, K., Oh, T.J., Kim, D.H., Nam, D.H., Yoo, J.C. and Sohng, J.K. Biosynthesis of dTDP-6-deoxy-β-D-allose, biochemical characterization of dTDP-4-keto-6-deoxyglucose reductase (GerKI) from Streptomyces sp. KCTC 0041BP. Glycobiology 17 (2007) 119-126. [PMID: 17053005]

4. Kubiak, R.L., Phillips, R.K., Zmudka, M.W., Ahn, M.R., Maka, E.M., Pyeatt, G.L., Roggensack, S.J. and Holden, H.M. Structural and functional studies on a 3′-epimerase involved in the biosynthesis of dTDP-6-deoxy-D-allose. Biochemistry 51 (2012) 9375-9383. [PMID: 23116432]

[EC 1.1.1.364 created 2013]

EC 1.1.1.365

Accepted name: D-galacturonate reductase

Reaction: L-galactonate + NADP+ = D-galacturonate + NADPH + H+

Other name(s): GalUR; gar1 (gene name)

Systematic name: L-galactonate:NADP+ oxidoreductase

Comments: The enzyme from plants is involved in ascorbic acid (vitamin C) biosynthesis [1,2]. The enzyme from the fungus Trichoderma reesei (Hypocrea jecorina) is involved in a eukaryotic degradation pathway of D-galacturonate. It is also active with D-glucuronate and glyceraldehyde [3]. Neither enzyme shows any activity with NADH.

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

References:

1. Isherwood, F.A. and Mapson, L.W. Biological synthesis of ascorbic acid: the conversion of derivatives of D-galacturonic acid into L-ascorbic acid by plant extracts. Biochem. J. 64 (1956) 13-22. [PMID: 13363799]

2. Agius, F., Gonzalez-Lamothe, R., Caballero, J.L., Munoz-Blanco, J., Botella, M.A. and Valpuesta, V. Engineering increased vitamin C levels in plants by overexpression of a D-galacturonic acid reductase. Nat. Biotechnol. 21 (2003) 177-181. [PMID: 12524550]

3. Kuorelahti, S., Kalkkinen, N., Penttila, M., Londesborough, J. and Richard, P. Identification in the mold Hypocrea jecorina of the first fungal D-galacturonic acid reductase. Biochemistry 44 (2005) 11234-11240. [PMID: 16101307]

4. Martens-Uzunova, E.S. and Schaap, P.J. An evolutionary conserved D-galacturonic acid metabolic pathway operates across filamentous fungi capable of pectin degradation. Fungal Genet. Biol. 45 (2008) 1449-1457. [PMID: 18768163]

[EC 1.1.1.365 created 2013]

EC 1.1.1.366

Accepted name: L-idonate 5-dehydrogenase (NAD+)

Reaction: L-idonate + NAD+ = 5-dehydro-D-gluconate + NADH + H+

Systematic name: L-idonate:NAD+ oxidoreductase

Comments: Involved in the catabolism of ascorbate (vitamin C) to tartrate. No activity is observed with NADP+ (cf. EC 1.1.1.264, L-idonate 5-dehydrogenase).

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

References:

1. DeBolt, S., Cook, D.R. and Ford, C.M. L-tartaric acid synthesis from vitamin C in higher plants. Proc. Natl. Acad. Sci. USA 103 (2006) 5608-5613. [PMID: 16567629]

[EC 1.1.1.366 created 2013]

EC 1.1.1.367

Accepted name: UDP-2-acetamido-2,6-β-L-arabino-hexul-4-ose reductase

Reaction: UDP-2-acetamido-2,6-dideoxy-β-L-talose + NAD(P)+ = UDP-2-acetamido-2,6-β-L-arabino-hexul-4-ose + NAD(P)H + H+

For diagram of reaction click here.

Glossary: UDP-2-acetamido-2,6-dideoxy-β-L-talose = UDP-N-acetyl-β-L-pneumosamine

Other name(s): WbjC; Cap5F

Systematic name: UDP-2-acetamido-2,6-dideoxy-L-talose:NADP+ oxidoreductase

Comments: Part of the biosynthesis of UDP-N-acetyl-L-fucosamine. Isolated from the bacteria Pseudomonas aeruginosa and Staphylococcus aureus.

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

References:

1. Kneidinger, B., O'Riordan, K., Li, J., Brisson, J.R., Lee, J.C. and Lam, J.S. Three highly conserved proteins catalyze the conversion of UDP-N-acetyl-D-glucosamine to precursors for the biosynthesis of O antigen in Pseudomonas aeruginosa O11 and capsule in Staphylococcus aureus type 5. Implications for the UDP-N-acetyl-L-fucosamine biosynthetic pathway. J. Biol. Chem. 278 (2003) 3615-3627. [PMID: 12464616]

2. Mulrooney, E.F., Poon, K.K., McNally, D.J., Brisson, J.R. and Lam, J.S. Biosynthesis of UDP-N-acetyl-L-fucosamine, a precursor to the biosynthesis of lipopolysaccharide in Pseudomonas aeruginosa serotype O11. J. Biol. Chem. 280 (2005) 19535-19542. [PMID: 15778500]

3. Miyafusa, T., Tanaka, Y., Kuroda, M., Ohta, T. and Tsumoto, K. Expression, purification, crystallization and preliminary diffraction analysis of CapF, a capsular polysaccharide-synthesis enzyme from Staphylococcus aureus. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 64 (2008) 512-515. [PMID: 18540063]

[EC 1.1.1.367 created 2014]

EC 1.1.1.368

Accepted name: 6-hydroxycyclohex-1-ene-1-carbonyl-CoA dehydrogenase

Reaction: 6-hydroxycyclohex-1-ene-1-carbonyl-CoA + NAD+ = 6-oxocyclohex-1-ene-1-carbonyl-CoA + NADH + H+

For diagram of reaction click here.

Systematic name: 6-hydroxycyclohex-1-ene-1-carbonyl-CoA:NAD+ 6-oxidoreductase

Comments: The enzyme participates in the central benzoyl-CoA degradation pathway of some anaerobic bacteria such as Thauera aromatica.

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

References:

1. Laempe, D., Jahn, M. and Fuchs, G. 6-Hydroxycyclohex-1-ene-1-carbonyl-CoA dehydrogenase and 6-oxocyclohex-1-ene-1-carbonyl-CoA hydrolase, enzymes of the benzoyl-CoA pathway of anaerobic aromatic metabolism in the denitrifying bacterium Thauera aromatica. Eur. J. Biochem. 263 (1999) 420-429. [PMID: 10406950]

[EC 1.1.1.368 created 2014]

EC 1.1.1.369

Accepted name: D-chiro-inositol 1-dehydrogenase

Reaction: 1D-chiro-inositol + NAD+ = 2D-2,3,5/4,6-pentahydroxycyclohexanone + NADH + H+

For diagram of reaction click here.

Glossary: 1D-chiro-inositol = 1,2,4/3,5,6-cyclohexane-1,2,3,4,5,6-hexol

Other name(s): DCI 1-dehydrogenase; IolG

Systematic name: 1D-chiro-inositol:NAD+ 1-oxidoreductase

Comments: The enzyme, found in the bacterium Bacillus subtilis, also catalyses the reaction of EC 1.1.1.18, inositol 2-dehydrogenase, and can also use D-glucose and D-xylose. It shows trace activity with D-ribose and D-fructose [1]. It is part of a myo-inositol/D-chiro-inositol degradation pathway leading to acetyl-CoA.

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

References:

1. Ramaley, R., Fujita, Y. and Freese, E. Purification and properties of Bacillus subtilis inositol dehydrogenase. J. Biol. Chem. 254 (1979) 7684-7690. [PMID: 112095]

2. Yoshida, K., Yamaguchi, M., Morinaga, T., Ikeuchi, M., Kinehara, M. and Ashida, H. Genetic modification of Bacillus subtilis for production of D-chiro-inositol, an investigational drug candidate for treatment of type 2 diabetes and polycystic ovary syndrome. Appl. Environ. Microbiol. 72 (2006) 1310-1315. [PMID: 16461681]

[EC 1.1.1.369 created 2014]

EC 1.1.1.370

Accepted name: scyllo-inositol 2-dehydrogenase (NAD+)

Reaction: scyllo-inositol + NAD+ = 2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+

For diagram of reaction click here.

Glossary: 2,4,6/3,5-pentahydroxycyclohexanone = (2R,3S,4s,5R,6S)-2,3,4,5,6-pentahydroxycyclohexanone = scyllo-inosose

Other name(s): iolX (gene name)

Systematic name: scyllo-inositol:NAD+ 2-oxidoreductase

Comments: The enzyme, found in the bacterium Bacillus subtilis, has no activity with NADP+ [cf. EC 1.1.1.371, scyllo-inositol 2-dehydrogenase (NADP+)]. It is part of a scyllo-inositol degradation pathway leading to acetyl-CoA.

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

References:

1. Morinaga, T., Ashida, H. and Yoshida, K. Identification of two scyllo-inositol dehydrogenases in Bacillus subtilis. Microbiology 156 (2010) 1538-1546. [PMID: 20133360]

[EC 1.1.1.370 created 2014]

EC 1.1.1.371

Accepted name: scyllo-inositol 2-dehydrogenase (NADP+)

Reaction: scyllo-inositol + NADP+ = 2,4,6/3,5-pentahydroxycyclohexanone + NADPH + H+

For diagram of reaction click here.

Glossary: 2,4,6/3,5-pentahydroxycyclohexanone = (2R,3S,4s,5R,6S)-2,3,4,5,6-pentahydroxycyclohexanone = scyllo-inosose

Other name(s): iolW (gene name)

Systematic name: scyllo-inositol:NADP+ 2-oxidoreductase

Comments: The enzyme, found in the bacterium Bacillus subtilis, has no activity with NAD+ [cf. EC 1.1.1.370, scyllo-inositol 2-dehydrogenase (NAD+)].

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

References:

1. Morinaga, T., Ashida, H. and Yoshida, K. Identification of two scyllo-inositol dehydrogenases in Bacillus subtilis. Microbiology 156 (2010) 1538-1546. [PMID: 20133360]

[EC 1.1.1.371 created 2014]

EC 1.1.1.372

Accepted name: D/L-glyceraldehyde reductase

Reaction: (1) glycerol + NADP+ = L-glyceraldehyde + NADPH + H+
(2) glycerol + NADP+ = D-glyceraldehyde + NADPH + H+

Other name(s): gld1-(gene name); gaaD-(gene name)

Systematic name: glycerol:NADP+ oxidoreductase (D/L-glyceraldehyde-forming)

Comments: The enzyme takes part in a D-galacturonate degradation pathway in the fungi Aspergillus niger-and Trichoderma reesei-(Hypocrea jecorina). It has equal activity with D- and L-glyceraldehyde, and can also reduce glyoxal and methylglyoxal. The reaction is only observed in the direction of glyceraldehyde reduction.

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

References:

1. Liepins, J., Kuorelahti, S., Penttila, M. and Richard, P. Enzymes for the NADPH-dependent reduction of dihydroxyacetone and D-glyceraldehyde and L-glyceraldehyde in the mould Hypocrea jecorina. FEBS J. 273 (2006) 4229-4235. [PMID: 16930134]

2. Martens-Uzunova, E.S. and Schaap, P.J. An evolutionary conserved D-galacturonic acid metabolic pathway operates across filamentous fungi capable of pectin degradation. Fungal Genet. Biol. 45 (2008) 1449-1457. [PMID: 18768163]

[EC 1.1.1.372 created 2014]

EC 1.1.1.373

Accepted name: sulfolactaldehyde 3-reductase

Reaction: 2,3-dihydroxypropane-1-sulfonate + NAD+ = 2-hydroxy-3-oxopropane-1-sulfonate + NADH + H+

For diagram of reaction click here.

Glossary: 2-hydroxy-3-oxopropane-1-sulfonate = sulfolactaldehyde

Other name(s): yihU-(gene name)

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

Comments: The enzyme, characterized from the bacterium Escherichia coli, is involved in the degradation pathway of sulfoquinovose, the polar headgroup of sulfolipids found in the photosynthetic membranes of all higher plants, mosses, ferns, algae, and most photosynthetic bacteria, as well as the surface layer of some archaea.

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

References:

1. Denger, K., Weiss, M., Felux, A.K., Schneider, A., Mayer, C., Spiteller, D., Huhn, T., Cook, A.M. and Schleheck, D. Sulphoglycolysis in Escherichia coli-K-12 closes a gap in the biogeochemical sulphur cycle. Nature 507 (2014) 114-117. [PMID: 24463506]

[EC 1.1.1.373 created 2014]

EC 1.1.1.374

Reaction: UDP-N-acetyl-α-D-glucosamine + NAD+ = UDP-2-acetamido-3-dehydro-2-deoxy-α-D-glucopyranose + NADH + H+

Systematic name: UDP-N-acetyl-α-D-glucosamine:NAD+ 3-oxidoreductase

Comments: The enzyme from the archaeon Methanococcus maripaludis is is activated by KCl (200 mM).

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

References:

1. Namboori, S.C. and Graham, D.E. Enzymatic analysis of uridine diphosphate N-acetyl-D-glucosamine. Anal. Biochem. 381 (2008) 94-100. [PMID: 18634748]

[EC 1.1.1.374 created 2014]

EC 1.1.1.375

Accepted name: L-2-hydroxycarboxylate dehydrogenase [NAD(P)+]

Reaction: a (2S)-2-hydroxycarboxylate + NAD(P)+ = a 2-oxocarboxylate + NAD(P)H + H+

Other name(s): MdhII; lactate/malate dehydrogenase

Systematic name: (2S)-2-hydroxycarboxylate:NAD(P)+ oxidoreductase

Comments: The enzyme from the archaeon Methanocaldococcus jannaschii catalyses the reversible oxidation of (2R)-3-sulfolactate and (S)-malate to 3-sulfopyruvate and oxaloacetate, respectively (note that (2R)-3-sulfolactate has the same stereochemical configuration as (2S)-2-hydroxycarboxylates) [1]. The enzyme can use both NADH and NADPH, although activity is higher with NADPH [1-3]. The oxidation of (2R)-3-sulfolactate was observed only in the presence of NADP+ [1]. The same organism also possesses an NAD+-specific enzyme with similar activity, cf. >EC 1.1.1.337, L-2-hydroxycarboxylate dehydrogenase (NAD+).

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. Lee, B.I., Chang, C., Cho, S.J., Eom, S.H., Kim, K.K., Yu, Y.G. and Suh, S.W. Crystal structure of the MJ0490 gene product of the hyperthermophilic archaebacterium Methanococcus jannaschii, a novel member of the lactate/malate family of dehydrogenases. J. Mol. Biol. 307 (2001) 1351-1362. [PMID: 11292347]

3. Madern, D. The putative L-lactate dehydrogenase from Methanococcus jannaschii is an NADPH-dependent L-malate dehydrogenase. Mol. Microbiol. 37 (2000) 1515-1520. [PMID: 10998181]

[EC 1.1.1.375 created 2014]

EC 1.1.1.376

Accepted name: L-arabinose 1-dehydrogenase [NAD(P)+]

Reaction: L-arabinose + NAD(P)+ = L-arabinono-1,4-lactone + NAD(P)H + H+

Other name(s): L-arabino-aldose dehydrogenase

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

Comments: The enzymes from the bacterium Azospirillum brasilense and the archaeon Haloferax volcanii are part of the L-arabinose degradation pathway and prefer NADP+ over NAD+. In vitro the enzyme from Azospirillum brasilense shows also high catalytic efficiency with D-galactose.

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

References:

1. Novick, N.J. and Tyler, M.E. Partial purification and properties of an L-arabinose dehydrogenase from Azospirillum brasilense. Can. J. Microbiol. 29 (1983) 242-246.

2. Watanabe, S., Kodaki, T. and Makino, K. Cloning, expression, and characterization of bacterial L-arabinose 1-dehydrogenase involved in an alternative pathway of L-arabinose metabolism. J. Biol. Chem. 281 (2006) 2612-2623. [PMID: 16326697]

3. Johnsen, U., Sutter, J.M., Zaiss, H. and Schonheit, P. L-Arabinose degradation pathway in the haloarchaeon Haloferax volcanii involves a novel type of L-arabinose dehydrogenase. Extremophiles 17 (2013) 897-909. [PMID: 23949136]

[EC 1.1.1.376 created 2014]

EC 1.1.1.377

Accepted name: L-rhamnose 1-dehydrogenase (NADP+)

Reaction: L-rhamnose + NADP+ = L-rhamnono-1,4-lactone + NADPH + H+

Systematic name: L-rhamnose:NADP+ 1-oxidoreductase

Comments: The enzyme from the archaeon Thermoplasma acidophilum is part of the non-phosphorylative degradation pathway for L-rhamnose. The enzyme differs in cofactor specificity from EC 1.1.1.173, L-rhamnose 1-dehydrogenase, which is specific for NAD+.

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

References:

1. Kim, S.M., Paek, K.H. and Lee, S.B. Characterization of NADP+-specific L-rhamnose dehydrogenase from the thermoacidophilic Archaeon Thermoplasma acidophilum. Extremophiles 16 (2012) 447-454. [PMID: 22481639]

[EC 1.1.1.377 created 2014]

EC 1.1.1.378

Accepted name: L-rhamnose 1-dehydrogenase [NAD(P)+]

Reaction: L-rhamnose + NAD(P)+ = L-rhamnono-1,4-lactone + NAD(P)H + H+

Systematic name: L-rhamnose:NAD(P)+ 1-oxidoreductase

Comments: The enzyme, which occurs in the bacteria Azotobacter vinelandii and Sphingomonas sp. SKA58, is part of the non-phosphorylative degradation pathway for L-rhamnose. The enzyme differs in cofactor specificity from EC 1.1.1.173, L-rhamnose 1-dehydrogenase, which is specific for NAD+ and EC 1.1.1.377, L-rhamnose 1-dehydrogenase (NADP+).

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

References:

1. Watanabe, S., Saimura, M. and Makino, K. Eukaryotic and bacterial gene clusters related to an alternative pathway of nonphosphorylated L-rhamnose metabolism. J. Biol. Chem. 283 (2008) 20372-20382. [PMID: 18505728]

2. Watanabe, S. and Makino, K. Novel modified version of nonphosphorylated sugar metabolism - an alternative L-rhamnose pathway of Sphingomonas sp. FEBS J. 276 (2009) 1554-1567. [PMID: 19187228]

[EC 1.1.1.378 created 2014]

EC 1.1.1.379

Accepted name: (R)-mandelate dehydrogenase

Reaction: (R)-mandelate + NAD+ = phenylglyoxylate + NADH + H+

Glossary: (R)-mandelate = D-mandelate

Other name(s): ManDH2; D-ManDH2; D-mandelate dehydrogenase (ambiguous)

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

Comments: The enzyme, found in bacteria and fungi, can also accept a number of substituted mandelate derivatives, such as 3-hydroxymandelate, 4-hydroxymandelate, 2-methoxymandelate, 4-hydroxy-3-methoxymandelate and 3-hydroxy-4-methoxymandelate. The enzyme has no activity with (S)-mandelate (cf. EC 1.1.99.31, (S)-mandelate dehydrogenase) [1,2]. The enzyme transfers the pro-R-hydrogen from NADH [2].

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

References:

1. Baker, D.P. and Fewson, C.A. Purification and characterization of D(–)-mandelate dehydrogenase from Rhodotorula graminis. Microbiology 135 (1989) 2035-2044.

2. Baker, D.P., Kleanthous, C., Keen, J.N., Weinhold, E. and Fewson, C.A. Mechanistic and active-site studies on D(–)-mandelate dehydrogenase from Rhodotorula graminis. Biochem. J. 281 (1992) 211-218. [PMID: 1731758]

3. 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]

4. 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 1.1.1.379 created 2014]

EC 1.1.1.380

Accepted name: L-gulonate 5-dehydrogenase

Reaction: L-gulonate + NAD+ = D-fructuronate + NADH + H+

Glossary: D-fructuronate = D-arabino-hexuronate

Systematic name: L-gulonate:NAD+ 5-oxidoreductase

Comments: The enzyme, characterized from the bacterium Halomonas elongata, participates in a pathway for L-gulonate degradation.

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

References:

1. Cooper, R.A. The pathway for L-gulonate catabolism in Escherichia coli K-12 and Salmonella typhimurium LT-2. FEBS Lett 115 (1980) 63-67. [PMID: 6993236]

2. Wichelecki, D.J., Vendiola, J.A., Jones, A.M., Al-Obaidi, N., Almo, S.C. and Gerlt, J.A. Investigating the physiological roles of low-efficiency D-mannonate and D-gluconate dehydratases in the enolase superfamily: pathways for the catabolism of L-gulonate and L-idonate. Biochemistry 53 (2014) 5692-5699. [PMID: 25145794]

[EC 1.1.1.380 created 2014]

EC 1.1.1.381

Accepted name: 3-hydroxy acid dehydrogenase

Reaction: L-allo-threonine + NADP+ = aminoacetone + CO2 + NADPH + H+ (overall reaction)
(1a) L-allo-threonine + NADP+ = L-2-amino-3-oxobutanoate + NADPH + H+
(1b) L-2-amino-3-oxobutanoate = aminoacetone + CO2 (spontaneous)

Glossary: L-allo-threonine = (2S,3S)-2-amino-3-hydroxybutanoic acid
aminoacetone = 1-aminopropan-2-one
L-2-amino-3-oxobutanoate = (2S)-2-amino-3-oxobutanoate

Other name(s): ydfG (gene name); YMR226c (gene name)

Systematic name: L-allo-threonine:NADP+ 3-oxidoreductase

Comments: The enzyme, purified from the bacterium Escherichia coli and the yeast Saccharomyces cerevisiae, shows activity with a range of 3- and 4-carbon 3-hydroxy acids. The highest activity is seen with L-allo-threonine and D-threonine. The enzyme from Escherichia coli also shows high activity with L-serine, D-serine, (S)-3-hydroxy-2-methylpropanoate and (R)-3-hydroxy-2-methylpropanoate. The enzyme has no activity with NAD+ or L-threonine (cf. EC 1.1.1.103, L-threonine 3-dehydrogenase).

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

References:

1. Fujisawa, H., Nagata, S. and Misono, H. Characterization of short-chain dehydrogenase/reductase homologues of Escherichia coli (YdfG) and Saccharomyces cerevisiae (YMR226C). Biochim. Biophys. Acta 1645 (2003) 89-94. [PMID: 12535615]

[EC 1.1.1.381 created 2014, modified 2015]

EC 1.1.1.382

Accepted name: ketol-acid reductoisomerase (NAD+)

Reaction: (2R)-2,3-dihydroxy-3-methylbutanoate + NAD+ = (2S)-2-hydroxy-2-methyl-3-oxobutanoate + NADH + H+

Glossary: (2S)-2-hydroxy-2-methyl-3-oxobutanoate = (2S)-2-acetolactate

Systematic name: (2R)-2,3-dihydroxy-3-methylbutanoate:NAD+ oxidoreductase (isomerizing)

Comments: The enzyme, characterized from the bacteria Thermacetogenium phaeum and Desulfococcus oleovorans and from the archaeon Archaeoglobus fulgidus, is specific for NADH [cf. EC 1.1.1.86, ketol-acid reductoisomerase (NADP+) and EC 1.1.1.383, ketol-acid reductoisomerase [NAD(P)+]].

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

References:

1. Brinkmann-Chen, S., Cahn, J.K. and Arnold, F.H. Uncovering rare NADH-preferring ketol-acid reductoisomerases. Metab. Eng. 26C (2014) 17-22. [PMID: 25172159]

[EC 1.1.1.382 created 2015]

EC 1.1.1.383

Accepted name: ketol-acid reductoisomerase [NAD(P)+]

Reaction: (2R)-2,3-dihydroxy-3-methylbutanoate + NAD(P)+ = (2S)-2-hydroxy-2-methyl-3-oxobutanoate + NAD(P)H + H+

Glossary: (2S)-2-hydroxy-2-methyl-3-oxobutanoate = (2S)-2-acetolactate

Systematic name: (2R)-2,3-dihydroxy-3-methylbutanoate:NAD(P)+ oxidoreductase (isomerizing)

Comments: The enzyme, characterized from the bacteria Hydrogenobaculum sp. and Syntrophomonas wolfei subsp. wolfei and from the archaea Metallosphaera sedula and Ignisphaera aggregans, can use both NADH and NADPH with similar efficiency [cf. EC 1.1.1.86, ketol-acid reductoisomerase (NADP+) and EC 1.1.1.382, ketol-acid reductoisomerase (NAD+)].

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

References:

1. Brinkmann-Chen, S., Cahn, J.K. and Arnold, F.H. Uncovering rare NADH-preferring ketol-acid reductoisomerases. Metab. Eng. 26C (2014) 17-22. [PMID: 25172159]

[EC 1.1.1.383 created 2015]

EC 1.1.1.384

Accepted name: dTDP-3,4-didehydro-2,6-dideoxy-α-D-glucose 3-reductase

Reaction: dTDP-4-dehydro-2,6-dideoxy-α-D-glucose + NADP+ = dTDP-3,4-didehydro-2,6-dideoxy-α-D-glucose + NADPH + H+

For diagram of reaction click here.

Glossary: dTDP-4-dehydro-2,6-dideoxy-α-D-glucose = dTDP-2,6-dideoxy-α-D-threo-hexopyranos-4-ulose
dTDP-3,4-didehydro-2,6-dideoxy-α-D-glucose = thymidine 5'-[(2R,6R)-6-methyl-4,5-dioxotetrahydro-2H-pyran-2-yl] diphosphate

Other name(s): KijD10; dTDP-4-keto-2,6-dideoxy-D-glucose 3-oxidoreductase; dTDP-4-dehydro-2,6-dideoxy-α-D-glucose 3-oxidoreductase

Systematic name: dTDP-4-dehydro-2,6-dideoxy-α-D-glucose:NADP+ 3-oxidoreductase

Comments: The enzyme is involved in the biosynthesis of several deoxysugars, including L-digitoxose, L- and D-olivose, L-oliose, D-mycarose and forosamine.

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

References:

1. Aguirrezabalaga, I., Olano, C., Allende, N., Rodriguez, L., Brana, A.F., Mendez, C. and Salas, J.A. Identification and expression of genes involved in biosynthesis of L-oleandrose and its intermediate L-olivose in the oleandomycin producer Streptomyces antibioticus. Antimicrob. Agents Chemother. 44 (2000) 1266-1275. [PMID: 10770761]

2. Wang, L., White, R.L. and Vining, L.C. Biosynthesis of the dideoxysugar component of jadomycin B: genes in the jad cluster of Streptomyces venezuelae ISP5230 for L-digitoxose assembly and transfer to the angucycline aglycone. Microbiology 148 (2002) 1091-1103. [PMID: 11932454]

3. Hong, L., Zhao, Z., Melancon, C.E., 3rd, Zhang, H. and Liu, H.W. In vitro characterization of the enzymes involved in TDP-D-forosamine biosynthesis in the spinosyn pathway of Saccharopolyspora spinosa. J. Am. Chem. Soc. 130 (2008) 4954-4967. [PMID: 18345667]

4. Kubiak, R.L. and Holden, H.M. Combined structural and functional investigation of a C-3''-ketoreductase involved in the biosynthesis of dTDP-L-digitoxose. Biochemistry 50 (2011) 5905-5917. [PMID: 21598943]

[EC 1.1.1.384 created 2015]

EC 1.1.1.385

Accepted name: dihydroanticapsin dehydrogenase

Reaction: L-dihydroanticapsin + NAD+ = L-anticapsin + NADH + H+

For diagram of reaction click here.

Glossary: L-dihydroanticapsin = 3-[(1R,2S,5R,6S)-5-hydroxy-7-oxabicyclo[4.1.0]hept-2-yl]-L-alanine
L-anticapsin = 3-[(1R,2S,6R)-5-oxo-7-oxabicyclo[4.1.0]hept-2-yl]-L-alanine

Other name(s): BacC; ywfD (gene name)

Systematic name: L-dihydroanticapsin:NAD+ oxidoreductase

Comments: The enzyme, characterized from the bacterium Bacillus subtilis, is involved in the biosynthesis of the nonribosomally synthesized dipeptide antibiotic bacilysin, composed of L-alanine and L-anticapsin.

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

References:

1. Parker, J.B. and Walsh, C.T. Action and timing of BacC and BacD in the late stages of biosynthesis of the dipeptide antibiotic bacilysin. Biochemistry 52 (2013) 889-901. [PMID: 23317005]

[EC 1.1.1.385 created 2015]

EC 1.1.1.386

Accepted name: ipsdienol dehydrogenase

Reaction: (R)-ipsdienol + NAD(P)+ = ipsdienone + NAD(P)H + H+

For diagram of reaction click here.

Glossary: ipsdienone = 2-methyl-6-methyleneocta-2,7-dien-4-one
(R)-ipsdienol = (4R)-2-methyl-6-methyleneocta-2,7-dien-4-ol

Other name(s): IDOLDH

Systematic name: (R)-ipsdienol:NAD(P)+ oxidoreductase

Comments: The enzyme is involved in pheromone production by the pine engraver beetle, Ips pini.

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

References:

1. Figueroa-Teran, R., Welch, W.H., Blomquist, G.J. and Tittiger, C. Ipsdienol dehydrogenase (IDOLDH): a novel oxidoreductase important for Ips pini pheromone production. Insect Biochem. Mol. Biol. 42 (2012) 81-90. [PMID: 22101251]

[EC 1.1.1.386 created 2015]

EC 1.1.1.387

Accepted name: L-serine 3-dehydrogenase (NAD+)

Reaction: L-serine + NAD+ = 2-aminoacetaldehyde + CO2 + NADH + H+ (overall reaction)
(1a) L-serine + NAD+ = 2-aminomalonate semialdehyde + NADH + H+
(1b) 2-aminomalonate semialdehyde = 2-aminoacetaldehyde + CO2 (spontaneous)

Other name(s): NAD+-dependent L-serine dehydrogenase

Systematic name: L-serine:NAD+ 3-oxidoreductase

Comments: The enzyme, purified from the bacterium Pseudomonas aeruginosa, also shows activity with L-threonine (cf. EC 1.1.1.103, L-threonine 3-dehydrogenase). The enzyme has only very low activity with NADP+ [cf. EC 1.1.1.276, serine 3-dehydrogenase (NADP+)].

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

References:

1. Tchigvintsev, A., Singer, A., Brown, G., Flick, R., Evdokimova, E., Tan, K., Gonzalez, C.F., Savchenko, A. and Yakunin, A.F. Biochemical and structural studies of uncharacterized protein PA0743 from Pseudomonas aeruginosa revealed NAD+-dependent L-serine dehydrogenase. J. Biol. Chem. 287 (2012) 1874-1883. [PMID: 22128181]

[EC 1.1.1.387 created 2015]

EC 1.1.1.388

Accepted name: glucose-6-phosphate dehydrogenase (NAD+)

Reaction: D-glucose 6-phosphate + NAD+ = 6-phospho-D-glucono-1,5-lactone + NADH + H+

Other name(s): Glc6PDH; azf (gene name); archaeal zwischenferment

Systematic name: D-glucose-6-phosphate:NAD+ 1-oxidoreductase

Comments: The enzyme catalyses a step of the pentose phosphate pathway. The enzyme from the archaeon Haloferax volcanii is specific for NAD+. cf. EC 1.1.1.363, glucose-6-phosphate dehydrogenase [NAD(P)+] and EC 1.1.1.49, glucose-6-phosphate dehydrogenase (NADP+).

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

References:

1. Pickl, A. and Schonheit, P. The oxidative pentose phosphate pathway in the haloarchaeon Haloferax volcanii involves a novel type of glucose-6-phosphate dehydrogenase--The archaeal Zwischenferment. FEBS Lett. 589 (2015) 1105-1111. [PMID: 25836736]

[EC 1.1.1.388 created 2015]

EC 1.1.1.389

Accepted name: 2-dehydro-3-deoxy-L-galactonate 5-dehydrogenase

Reaction: 2-dehydro-3-deoxy-L-galactonate + NAD+ = 3-deoxy-D-glycero-2,5-hexodiulosonate + NADH + H+

Systematic name: 2-dehydro-3-deoxy-L-galactonate:NAD+ 5-oxidoreductase

Comments: The enzyme, characterized from agarose-degrading bacteria, is involved in a degradation pathway for 3,6-anhydro-α-L-galactopyranose, a major component of the polysaccharides of red macroalgae.

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

References:

1. Lee, S.B., Cho, S.J., Kim, J.A., Lee, S.Y., Kim, S.M. and Lim, H.S. Metabolic pathway of 3,6-anhydro-L-galactose in agar-degrading microorganisms. Biotechnol. Bioprocess Eng. 19 (2014) 866-878.

[EC 1.1.1.389 created 2015]

EC 1.1.1.390

Accepted name: sulfoquinovose 1-dehydrogenase

Reaction: sulfoquinovose + NAD+ = 6-deoxy-6-sulfo-D-glucono-1,5-lactone + NADH + H+

For diagram of reaction click here.

Glossary: sulfoquinovose = 6-deoxy-6-sulfo-D-glucopyranose

Systematic name: 6-deoxy-6-sulfo-D-glucopyranose:NAD+ 1-oxidoreductase

Comments: The enzyme, characterized from the bacterium Pseudomonas putida SQ1, participates in a sulfoquinovose degradation pathway. Activity with NADP+ is only 4% of that with NAD+.

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

References:

1. Felux, A.K., Spiteller, D., Klebensberger, J. and Schleheck, D. Entner-Doudoroff pathway for sulfoquinovose degradation in Pseudomonas putida SQ1. Proc. Natl. Acad. Sci. USA 112 (2015) E4298-E4305. [PMID: 26195800]

[EC 1.1.1.390 created 2015]

EC 1.1.1.391

Accepted name: 3β-hydroxycholanate 3-dehydrogenase (NAD+)

Reaction: isolithocholate + NAD+ = 3-oxo-5β-cholan-24-oate + NADH + H+

Glossary: isolithocholate = 3β-hydroxy-5β-cholan-24-oate

Other name(s): 3β-hydroxysteroid dehydrogenase

Systematic name: isolithocholate:NAD+ 3-oxidoreductase

Comments: This bacterial enzyme is involved, along with EC 1.1.1.52, 3α-hydroxycholanate dehydrogenase (NAD+), or EC 1.1.1.392, 3α-hydroxycholanate dehydrogenase (NADP+), in the modification of secondary bile acids to form 3β-bile acids (also known as iso-bile acids). The enzyme catalyses the reaction in the reduction direction in vivo. Also acts on related 3-oxo bile acids. cf. EC 1.1.1.393, 3β-hydroxycholanate 3-dehydrogenase (NADP+).

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

References:

1. Edenharder, R., Pfutzner, A. and Hammann, R. Characterization of NAD-dependent 3 α- and 3 β-hydroxysteroid dehydrogenase and of NADP-dependent 7 β-hydroxysteroid dehydrogenase from Peptostreptococcus productus, Biochim. Biophys. Acta 1004 (1989) 230-238. [PMID: 2752021]

2. Edenharder, R. and Pfutzner, M. Partial purification and characterization of an NAD-dependent 3 β-hydroxysteroid dehydrogenase from Clostridium innocuum, Appl. Environ. Microbiol. 55 (1989) 1656-1659. [PMID: 2764572]

3. Devlin, A.S. and Fischbach, M.A. A biosynthetic pathway for a prominent class of microbiota-derived bile acids. Nat. Chem. Biol. 11 (2015) 685-690. [PMID: 26192599]

[EC 1.1.1.391 created 2016]

EC 1.1.1.392

Accepted name: 3α-hydroxycholanate dehydrogenase (NADP+)

Reaction: lithocholate + NADP+ = 3-oxo-5β-cholan-24-oate + NADPH + H+

Glossary: lithocholate = 3α-hydroxy-5β-cholan-24-oate

Other name(s): α-hydroxy-cholanate dehydrogenase (ambiguous)

Systematic name: lithocholate:NADP+ 3-oxidoreductase

Comments: This bacterial enzyme is involved in the modification of secondary bile acids to form 3β-bile acids (also known as iso-bile acids) via a 3-oxo intermediate. The enzyme catalyses a reversible reaction in vitro. Also acts on related bile acids. cf. EC 1.1.1.52, 3α-hydroxycholanate dehydrogenase (NAD+).

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

References:

1. Devlin, A.S. and Fischbach, M.A. A biosynthetic pathway for a prominent class of microbiota-derived bile acids. Nat. Chem. Biol. 11 (2015) 685-690. [PMID: 26192599]

[EC 1.1.1.392 created 2016]

EC 1.1.1.393

Accepted name: 3β-hydroxycholanate 3-dehydrogenase (NADP+)

Reaction: isolithocholate + NADP+ = 3-oxo-5β-cholan-24-oate + NADPH + H+

Glossary: isolithocholate = 3β-hydroxy-5β-cholan-24-oate

Other name(s): 3β-hydroxysteroid dehydrogenase (ambiguous)

Systematic name: isolithocholate:NADP+ 3-oxidoreductase

Comments: This bacterial enzyme is involved, along with EC 1.1.1.52, 3α-hydroxycholanate dehydrogenase (NAD+), or EC 1.1.1.392, 3α-hydroxycholanate dehydrogenase (NADP+), in the modification of secondary bile acids to form 3β-bile acids (also known as iso-bile acids). The enzyme catalyses the reaction in the reduction direction in vivo. Also acts on related 3-oxo bile acids. cf. EC 1.1.1.391, 3β-hydroxycholanate 3-dehydrogenase (NAD+).

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

References:

1. Akao, T., Akao, T., Hattori, M., Namba, T. and Kobashi, K. 3 β-Hydroxysteroid dehydrogenase of Ruminococcus sp. from human intestinal bacteria. J. Biochem. 99 (1986) 1425-1431. [PMID: 3458705]

2. Devlin, A.S. and Fischbach, M.A. A biosynthetic pathway for a prominent class of microbiota-derived bile acids. Nat. Chem. Biol. 11 (2015) 685-690. [PMID: 26192599]

[EC 1.1.1.393 created 2016]

EC 1.1.1.394

Accepted name: aurachin B dehydrogenase

Reaction: aurachin B + NAD+ + H2O = 4-[(2E,6E)-farnesyl]-4-hydroxy-2-methyl-3-oxo-3,4-dihydroquinoline 1-oxide + NADH + H+ (overall reaction)
(1a) 4-[(2E,6E)-farnesyl]-3,4-dihydroxy-2-methyl-3,4-dihydroquinoline 1-oxide + NAD+ = 4-[(2E,6E)-farnesyl]-4-hydroxy-2-methyl-3-oxo-3,4-dihydroquinoline 1-oxide + NADH + H+
(1b) aurachin B + H2O = 4-[(2E,6E)-farnesyl]-3,4-dihydroxy-2-methyl-3,4-dihydroquinoline 1-oxide (spontaneous)

Glossary: aurachin B= 4-[(2E,6E,10E)-3,7-dimethyldodeca-2,6,10-trien-1-yl]-3-hydroxy-2-methylquinoline 1-oxide

Other name(s): AuaH

Systematic name: aurachin B:NAD+ 3-oxidoreductase

Comments: The enzyme from the bacterium Stigmatella aurantiaca catalyses the final step in the conversion of aurachin C to aurachin B. In vivo the enzyme catalyses the reduction of 4-hydroxy-2-methyl-3-oxo-4-[(2E,6E)-farnesyl]-3,4-dihydroquinoline-1-oxide to form 2-methyl-1-oxo-4-[(2E,6E)-farnesyl]-3,4-dihydroquinoline-3,4-diol (note that the reactions written above proceed from right to left), which then undergoes a spontaneous dehydration to form aurachin B.

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

References:

1. Katsuyama, Y., Harmrolfs, K., Pistorius, D., Li, Y. and Muller, R. A semipinacol rearrangement directed by an enzymatic system featuring dual-function FAD-dependent monooxygenase. Angew Chem. Int. Ed. Engl. 51 (2012) 9437-9440. [PMID: 22907798]

[EC 1.1.1.394 created 2016]

EC 1.1.1.395

Accepted name: 3α-hydroxy bile acid-CoA-ester 3-dehydrogenase

Reaction: a 3α-hydroxy bile acid CoA ester + NAD+ = a 3-oxo bile acid CoA ester + NADH + H+

Other name(s): baiA1 (gene name); baiA2 (gene name); baiA3 (gene name)

Systematic name: 3α-hydroxy-bile-acid-CoA-ester:NAD+ 3-oxidoreductase

Comments: This bacterial enzyme is involved in the 7-dehydroxylation process associated with bile acid degradation. The enzyme has very little activity with unconjugated bile acid substrates. It has similar activity with choloyl-CoA, chenodeoxycholoyl-CoA, deoxycholoyl-CoA, and lithocholoyl-CoA.

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

References:

1. Mallonee, D.H., Lijewski, M.A. and Hylemon, P.B. Expression in Escherichia coli and characterization of a bile acid-inducible 3α-hydroxysteroid dehydrogenase from Eubacterium sp. strain VPI 12708. Curr. Microbiol. 30 (1995) 259-263. [PMID: 7766153]

2. Bhowmik, S., Jones, D.H., Chiu, H.P., Park, I.H., Chiu, H.J., Axelrod, H.L., Farr, C.L., Tien, H.J., Agarwalla, S. and Lesley, S.A. Structural and functional characterization of BaiA, an enzyme involved in secondary bile acid synthesis in human gut microbe. Proteins 82 (2014) 216-229. [PMID: 23836456]

[EC 1.1.1.395 created 2016]

EC 1.1.1.396

Accepted name: bacteriochlorophyllide a dehydrogenase

Reaction: (1) 3-deacetyl-3-(1-hydroxyethyl)bacteriochlorophyllide a + NAD+ = bacteriochlorophyllide a + NADH + H+
(2) 3-devinyl-3-(1-hydroxyethyl)chlorophyllide a + NAD+ = 3-acetyl-3-devinylchlorophyllide a + NADH + H+

For diagram of reaction click here.

Other name(s): bchC (gene name)

Systematic name: 3-deacetyl-3-hydroxyethylbacteriochlorophyllide-a:NAD+ oxidoreductase (bacteriochlorophyllide a-forming)

Comments: The enzyme, together with EC 1.3.7.15, chlorophyllide-a reductase, and EC 4.2.1.165, chlorophyllide-a 31-hydratase, is involved in the conversion of chlorophyllide a to bacteriochlorophyllide a. The enzymes can act in multiple orders, resulting in the formation of different intermediates, but the final product of the cumulative action of the three enzymes is always bacteriochlorophyllide a. The enzyme oxidizes a hydroxyl group on ring A, converting it to an oxo group.

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

References:

1. Wellington, C.L. and Beatty, J.T. Promoter mapping and nucleotide sequence of the bchC bacteriochlorophyll biosynthesis gene from Rhodobacter capsulatus. Gene 83 (1989) 251-261. [PMID: 2555268]

2. McGlynn, P. and Hunter, C.N. Genetic analysis of the bchC and bchA genes of Rhodobacter sphaeroides. Mol. Gen. Genet. 236 (1993) 227-234. [PMID: 8437569]

3. Lange, C., Kiesel, S., Peters, S., Virus, S., Scheer, H., Jahn, D. and Moser, J. Broadened substrate specificity of 3-hydroxyethyl bacteriochlorophyllide a dehydrogenase (BchC) indicates a new route for the biosynthesis of bacteriochlorophyll a. J. Biol. Chem. 290 (2015) 19697-19709. [PMID: 26088139]

[EC 1.1.1.396 created 2016]

EC 1.1.1.397

Accepted name: β-methylindole-3-pyruvate reductase

Reaction: (2S,3R)-2-hydroxy-3-(indol-3-yl)butanoate + NAD+ = (R)-3-(indol-3-yl)-2-oxobutanoate + NADH + H+

Glossary: (R)-3-(indol-3-yl)-2-oxobutanoate = (R)-β-methylindole-3-pyruvate
(2S,3R)-2-hydroxy-3-(indol-3-yl)butanoate = indolmycenate

Other name(s): ind2 (gene name)

Systematic name: (2S,3R)-2-hydroxy-3-(indol-3-yl)butanoate:NAD+ oxidoreductase

Comments: The enzyme, characterized from the bacterium Streptomyces griseus, participates in the biosynthesis of indolmycin, an antibacterial drug that inhibits the bacterial tryptophan—tRNA ligase (EC 6.1.1.2).

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

References:

1. Du, Y.L., Alkhalaf, L.M. and Ryan, K.S. In vitro reconstitution of indolmycin biosynthesis reveals the molecular basis of oxazolinone assembly. Proc. Natl. Acad. Sci. USA 112 (2015) 2717-2722. [PMID: 25730866]

[EC 1.1.1.397 created 2016]

EC 1.1.1.398

Accepted name: 2-glutathionyl-2-methylbut-3-en-1-ol dehydrogenase

Reaction: 2-(glutathione-S-yl)-2-methylbut-3-en-1-ol + 2 NAD+ + H2O = 2-(glutathione-S-yl)-2-methylbut-3-enoate + 2 NADH + 2 H+ (overall reaction)
(1a) 2-(glutathione-S-yl)-2-methylbut-3-en-1-ol + NAD+ = 2-(glutathione-S-yl)-2-methylbut-3-enal + NADH + H+
(1b) 2-(glutathione-S-yl)-2-methylbut-3-enal + NAD+ + H2O = 2-(glutathione-S-yl)-2-methylbut-3-enoate + NADH + H+

Other name(s): isoH (gene name); 4-hydroxy-3-glutathionyl-3-methylbut-1-ene dehydrogenase

Systematic name: 2-(glutathione-S-yl)-2-methylbut-3-en-1-ol:NAD+ oxidoreductase

Comments: The enzyme, characterized from the bacterium Rhodococcus sp. AD45, is involved in isoprene degradation.

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

References:

1. van Hylckama Vlieg, J.E., Kingma, J., Kruizinga, W. and Janssen, D.B. Purification of a glutathione S-transferase and a glutathione conjugate-specific dehydrogenase involved in isoprene metabolism in Rhodococcus sp. strain AD45. J. Bacteriol. 181 (1999) 2094-2101. [PMID: 10094686]

[EC 1.1.1.398 created 2016]

EC 1.1.1.399

Accepted name: 2-oxoglutarate reductase

Reaction: (R)-2-hydroxyglutarate + NAD+ = 2-oxoglutarate + NADH + H+

Other name(s): serA (gene name)

Systematic name: (R)-2-hydroxyglutarate,NAD+ 2-oxidireductase

Comments: The enzyme catalyses a reversible reaction. The enzyme from the bacterium Peptoniphilus asaccharolyticus is specific for (R)-2-hydroxyglutarate [1,2]. The SerA enzyme from the bacterium Escherichia coli can also accept (S)-2-hydroxyglutarate with a much higher Km, and also catalyses the activity of EC 1.1.1.95, phosphoglycerate dehydrogenase [3].

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

References:

1. Lerud, R.F. and Whiteley, H.R. Purification and properties of α-ketoglutarate reductase from Micrococcus aerogenes. J. Bacteriol. 106 (1971) 571-577. [PMID: 4396793]

2. Johnson, W.M. and Westlake, D.W. Purification and characterization of glutamic acid dehydrogenase and α-ketoglutaric acid reductase from Peptococcus aerogenes. Can. J. Microbiol. 18 (1972) 881-892. [PMID: 4338318]

3. Zhao, G. and Winkler, M.E. A novel α-ketoglutarate reductase activity of the serA-encoded 3-phosphoglycerate dehydrogenase of Escherichia coli K-12 and its possible implications for human 2-hydroxyglutaric aciduria. J. Bacteriol. 178 (1996) 232-239. [PMID: 8550422]

[EC 1.1.1.399 created 2016]

EC 1.1.1.400

Accepted name: 2-methyl-1,2-propanediol dehydrogenase

Reaction: 2-methylpropane-1,2-diol + NAD+ = 2-hydroxy-2-methylpropanal + NADH + H+

Other name(s): mpdB (gene name)

Systematic name: 2-methylpropane-1,2-diol:NAD+ 1-oxidoreductase

Comments: This bacterial enzyme is involved in the degradation pathways of the alkene 2-methylpropene and the fuel oxygenate methyl tert-butyl ether (MTBE), a widely occurring groundwater contaminant.

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

References:

1. Lopes Ferreira, N., Labbe, D., Monot, F., Fayolle-Guichard, F. and Greer, C.W. Genes involved in the methyl tert-butyl ether (MTBE) metabolic pathway of Mycobacterium austroafricanum IFP 2012. Microbiology 152 (2006) 1361-1374. [PMID: 16622053]

2. Kottegoda, S., Waligora, E. and Hyman, M. Metabolism of 2-methylpropene (isobutylene) by the aerobic bacterium Mycobacterium sp. strain ELW1. Appl. Environ. Microbiol. 81 (2015) 1966-1976. [PMID: 25576605]

[EC 1.1.1.400 created 2016]

EC 1.1.1.401

Accepted name: 2-dehydro-3-deoxy-L-rhamnonate dehydrogenase (NAD+)

Reaction: 2-dehydro-3-deoxy-L-rhamnonate + NAD+ = 2,4-didehydro-3-deoxy-L-rhamnonate + NADH + H+

Other name(s): 2-keto-3-deoxy-L-rhamnonate dehydrogenase

Systematic name: 2-dehydro-3-deoxy-L-rhamnonate:NAD+ 4-oxidoreductase

Comments: The enzyme, characterized from the bacteria Sphingomonas sp. SKA58 and Sulfobacillus thermosulfidooxidans, is involved in the non-phosphorylative degradation pathway for L-rhamnose. It does not show any detectable activity with NADP+ or with other aldoses.

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

References:

1. Watanabe, S. and Makino, K. Novel modified version of nonphosphorylated sugar metabolism – an alternative L-rhamnose pathway of Sphingomonas sp. FEBS J. 276 (2009) 1554-1567. [PMID: 19187228]

2. Bae, J., Kim, S.M. and Lee, S.B. Identification and characterization of 2-keto-3-deoxy-L-rhamnonate dehydrogenase belonging to the MDR superfamily from the thermoacidophilic bacterium Sulfobacillus thermosulfidooxidans: implications to L-rhamnose metabolism in archaea. Extremophiles 19 (2015) 469-478. [PMID: 25617114]

[EC 1.1.1.401 created 2016]

EC 1.1.1.402

Accepted name: D-erythritol 1-phosphate dehydrogenase

Reaction: D-erythritol 1-phosphate + NADP+ = D-erythrulose 1-phosphate + NADPH + H+

Other name(s): eryB (gene name)

Systematic name: D-erythritol-1-phosphate 2-oxidoreductase

Comments: The enzyme, characterized from the pathogenic bacterium Brucella abortus, which causes brucellosis in livestock, participates in erythritol catabolism.

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

References:

1. Sperry, J.F. and Robertson, D.C. Erythritol catabolism by Brucella abortus. J. Bacteriol. 121 (1975) 619-630. [PMID: 163226]

2. Sangari, F.J., Aguero, J. and Garcia-Lobo, J.M. The genes for erythritol catabolism are organized as an inducible operon in Brucella abortus. Microbiology 146 (2000) 487-495. [PMID: 10708387]

3. Barbier, T., Collard, F., Zuniga-Ripa, A., Moriyon, I., Godard, T., Becker, J., Wittmann, C., Van Schaftingen, E. and Letesson, J.J. Erythritol feeds the pentose phosphate pathway via three new isomerases leading to D-erythrose-4-phosphate in Brucella. Proc. Natl. Acad. Sci. USA 111 (2014) 17815-17820. [PMID: 25453104]

[EC 1.1.1.402 created 2016]

EC 1.1.1.403

Accepted name: D-threitol dehydrogenase (NAD+)

Reaction: D-threitol + NAD+ = D-erythrulose + NADH + H+

Other name(s): dthD (gene name)

Systematic name: D-threitol:NAD+ oxidoreductase

Comments: The enzyme, characterized from the bacterium Mycobacterium smegmatis, participates in the degradation of D-threitol.

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

References:

1. Huang, H., Carter, M.S., Vetting, M.W., Al-Obaidi, N., Patskovsky, Y., Almo, S.C. and Gerlt, J.A. A general strategy for the discovery of metabolic pathways: D-threitol, L-threitol, and erythritol utilization in Mycobacterium smegmatis. J. Am. Chem. Soc. 137 (2015) 14570-14573. [PMID: 26560079]

[EC 1.1.1.403 created 2016]

EC 1.1.1.404

Accepted name: tetrachlorobenzoquinone reductase

Reaction: 2,3,5,6-tetrachlorohydroquinone + NAD+ = 2,3,5,6-tetrachloro-1,4-benzoquinone + NADH + H+

Other name(s): pcpD (gene name); TCBQ reductase

Systematic name: 2,3,5,6-tetrachlorohydroquinone:NAD+ oxidoreductase

Comments: Contains FMN. The enzyme, characterized from the bacterium Sphingobium chlorophenolicum, participates in the degradation of pentachlorophenol.

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

References:

1. Chen, L. and Yang, J. Biochemical characterization of the tetrachlorobenzoquinone reductase involved in the biodegradation of pentachlorophenol. Int J Mol Sci 9 (2008) 198-212. [PMID: 19325743]

2. Yadid, I., Rudolph, J., Hlouchova, K. and Copley, S.D. Sequestration of a highly reactive intermediate in an evolving pathway for degradation of pentachlorophenol. Proc. Natl. Acad. Sci. USA 110 (2013) E2182-E2190. [PMID: 23676275]

[EC 1.1.1.404 created 2017]

EC 1.1.1.405

Accepted name: ribitol-5-phosphate 2-dehydrogenase (NADP+)

Reaction: D-ribitol 5-phosphate + NADP+ = D-ribulose 5-phosphate + NADPH + H+

Other name(s): acs1 (gene name); bcs1 (gene name); tarJ (gene name); ribulose-5-phosphate reductase; ribulose-5-P reductase; D-ribulose 5-phosphate reductase

Systematic name: D-ribitol-5-phosphate:NADP+ 2-oxidoreductase

Comments: Requires Zn2+. The enzyme, characterized in bacteria, is specific for NADP. It is part of the synthesis pathway of CDP-ribitol. In Haemophilus influenzae it is part of a multifunctional enzyme also catalysing EC 2.7.7.40, D-ribitol-5-phosphate cytidylyltransferase. cf. EC 1.1.1.137, ribitol-5-phosphate 2-dehydrogenase.

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

References:

1. Zolli, M., Kobric, D.J. and Brown, E.D. Reduction precedes cytidylyl transfer without substrate channeling in distinct active sites of the bifunctional CDP-ribitol synthase from Haemophilus influenzae. Biochemistry 40 (2001) 5041-5048. [PMID: 11305920]

2. Pereira, M.P. and Brown, E.D. Bifunctional catalysis by CDP-ribitol synthase: convergent recruitment of reductase and cytidylyltransferase activities in Haemophilus influenzae and Staphylococcus aureus. Biochemistry 43 (2004) 11802-11812. [PMID: 15362865]

3. Pereira, M.P., D'Elia, M.A., Troczynska, J. and Brown, E.D. Duplication of teichoic acid biosynthetic genes in Staphylococcus aureus leads to functionally redundant poly(ribitol phosphate) polymerases. J. Bacteriol. 190 (2008) 5642-5649. [PMID: 18556787]

4. Baur, S., Marles-Wright, J., Buckenmaier, S., Lewis, R.J. and Vollmer, W. Synthesis of CDP-activated ribitol for teichoic acid precursors in Streptococcus pneumoniae. J. Bacteriol. 191 (2009) 1200-1210. [PMID: 19074383]

[EC 1.1.1.405 created 2017]

EC 1.1.1.406

Accepted name: galactitol 2-dehydrogenase (L-tagatose-forming)

Reaction: galactitol + NAD+ = L-tagatose + NADH + H+

For diagram of reaction click here.

Other name(s): GatDH

Systematic name: galactitol:NAD+ 2-oxidoreductase (L-tagatose-forming)

Comments: The enzyme, characterized in the bacterium Rhodobacter sphaeroides, has a wide subtrate specificity. In addition to galactitol, it primarily oxidizes D-threitol and xylitol, and in addition to L-tagatose, it primarily reduces L-erythrulose, D-ribulose and L-glyceraldehyde. It is specific for NAD+. The enzyme also shows activity with D-tagatose (cf. EC 1.1.1.16, galactitol 2-dehydrogenase).

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

References:

1. Schneider, K.H., Jakel, G., Hoffmann, R. and Giffhorn, F. Enzyme evolution in Rhodobacter sphaeroides: selection of a mutant expressing a new galactitol dehydrogenase and biochemical characterization of the enzyme. Microbiology 141 (1995) 1865-1873. [PMID: 7551050]

2. Carius, Y., Christian, H., Faust, A., Zander, U., Klink, B.U., Kornberger, P., Kohring, G.W., Giffhorn, F. and Scheidig, A.J. Structural insight into substrate differentiation of the sugar-metabolizing enzyme galactitol dehydrogenase from Rhodobacter sphaeroides D. J. Biol. Chem. 285 (2010) 20006-20014. [PMID: 20410293]

[EC 1.1.1.406 created 2017]

EC 1.1.1.407

Accepted name: D-altritol 5-dehydrogenase

Reaction: D-altritol + NAD+ = D-tagatose + NADH + H+

For diagram of reaction click here.

Systematic name: D-altritol:NAD+ 5-oxidoreductase

Comments: The enzyme, characterized in Agrobacterium fabrum C58, also has low activity with D-mannitol and D-arabinitol. It is part of a D-altritol degradation pathway.

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

References:

1. Wichelecki, D.J., Vetting, M.W., Chou, L., Al-Obaidi, N., Bouvier, J.T., Almo, S.C. and Gerlt, J.A. ATP-binding cassette (ABC) transport system solute-binding protein-guided identification of novel D-altritol and galactitol catabolic pathways in Agrobacterium tumefaciens C58. J. Biol. Chem. 290 (2015) 28963-28976. [PMID: 26472925]

[EC 1.1.1.407 created 2017]

EC 1.1.1.408

Accepted name: 4-phospho-D-threonate 3-dehydrogenase

Reaction: 4-phospho-D-threonate + NAD+ = glycerone phosphate + CO2 + NADH + H+ (overall reaction)
(1a) 4-phospho-D-threonate + NAD+ = 3-dehydro-4-phospho-D-threonate + NADH + H+
(1b) 3-dehydro-4-phospho-D-threonate = glycerone phosphate + CO2 (spontaneous)

For diagram of reaction click here.

Glossary: D-threonate = (2S,3R)-2,3,4-trihydroxybutanoate
glycerone phosphate = dihydroxyacetone phosphate = 3-hydroxy-2-oxopropyl phosphate

Other name(s): pdxA2 (gene name) (ambiguous)

Systematic name: 4-phospho-D-threonate:NAD+ 3-oxidoreductase

Comments: The enzyme, characterized from bacteria, is involved in a pathway for D-threonate catabolism.

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

References:

1. Zhang, X., Carter, M.S., Vetting, M.W., San Francisco, B., Zhao, S., Al-Obaidi, N.F., Solbiati, J.O., Thiaville, J.J., de Crecy-Lagard, V., Jacobson, M.P., Almo, S.C. and Gerlt, J.A. Assignment of function to a domain of unknown function: DUF1537 is a new kinase family in catabolic pathways for acid sugars. Proc. Natl Acad. Sci. USA 113 (2016) E4161-E4169. [PMID: 27402745]

[EC 1.1.1.408 created 2017]

EC 1.1.1.409

Accepted name: 4-phospho-D-erythronate 3-dehydrogenase

Reaction: 4-phospho-D-erythronate + NAD+ = glycerone phosphate + CO2 + NADH + H+ (overall reaction)
(1a) 4-phospho-D-erythronate + NAD+ = 3-dehydro-4-phospho-L-threonate + NADH + H+
(1b) 3-dehydro-4-phospho-L-threonate = glycerone phosphate + CO2 (spontaneous)

For diagram of reaction click here.

Glossary: D-erythronate = (2R,3R)-2,3,4-trihydroxybutanoate

Other name(s): pdxA2 (gene name) (ambiguous)

Systematic name: 4-phospho-D-erythronate:NAD+ 3-oxidoreductase

Comments: The enzyme, characterized from bacteria, is involved in a pathway for D-erythronate catabolism.

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

References:

1. Zhang, X., Carter, M.S., Vetting, M.W., San Francisco, B., Zhao, S., Al-Obaidi, N.F., Solbiati, J.O., Thiaville, J.J., de Crecy-Lagard, V., Jacobson, M.P., Almo, S.C. and Gerlt, J.A. Assignment of function to a domain of unknown function: DUF1537 is a new kinase family in catabolic pathways for acid sugars. Proc. Natl Acad. Sci. USA 113 (2016) E4161-E4169. [PMID: 27402745]

[EC 1.1.1.409 created 2017]

EC 1.1.1.410

Accepted name: D-erythronate 2-dehydrogenase

Reaction: D-erythronate + NAD+ = 2-dehydro-D-erythronate + NADH + H+

For diagram of reaction click here.

Glossary: D-erythronate = (2R,3R)-2,3,4-trihydroxybutanoate
2-dehydro-D-erythronate = (3R)-3,4-dihydroxy-2-oxobutanoate

Other name(s): denD (gene name)

Systematic name: D-erythronate:NAD+ 2-oxidoreductase

Comments: The enzyme, characterized from bacteria, is involved in D-erythronate catabolism.

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

References:

1. Zhang, X., Carter, M.S., Vetting, M.W., San Francisco, B., Zhao, S., Al-Obaidi, N.F., Solbiati, J.O., Thiaville, J.J., de Crecy-Lagard, V., Jacobson, M.P., Almo, S.C. and Gerlt, J.A. Assignment of function to a domain of unknown function: DUF1537 is a new kinase family in catabolic pathways for acid sugars. Proc. Natl Acad. Sci. USA 113 (2016) E4161-E4169. [PMID: 27402745]

[EC 1.1.1.410 created 2017]

EC 1.1.1.411

Accepted name: L-threonate 2-dehydrogenase

Reaction: L-threonate + NAD+ = 2-dehydro-L-erythronate + NADH + H+

For diagram of reaction click here.

Glossary: L-threonate = (2R,3S)-2,3,4-trihydroxybutanoate
2-dehydro-L-erythronate = (3R)-3,4-dihydroxy-2-oxobutanoate

Other name(s): ltnD (gene name)

Systematic name: L-threonate:NAD+ 2-oxidoreductase

Comments: The enzyme, characterized from bacteria, is involved in L-threonate catabolism.

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

References:

1. Zhang, X., Carter, M.S., Vetting, M.W., San Francisco, B., Zhao, S., Al-Obaidi, N.F., Solbiati, J.O., Thiaville, J.J., de Crecy-Lagard, V., Jacobson, M.P., Almo, S.C. and Gerlt, J.A. Assignment of function to a domain of unknown function: DUF1537 is a new kinase family in catabolic pathways for acid sugars. Proc. Natl Acad. Sci. USA 113 (2016) E4161-E4169. [PMID: 27402745]

[EC 1.1.1.411 created 2017]

EC 1.1.1.412

Accepted name: 2-alkyl-3-oxoalkanoate reductase

Reaction: a (2R,3S)-2-alkyl-3-hydroxyalkanoate + NADP+ = an (R)-2-alkyl-3-oxoalkanoate + NADPH + H+

Other name(s): oleD (gene name)

Systematic name: (2R,3S)-2-alkyl-3-hydroxyalkanoate:NADP+ oxidoreductase

Comments: The enzyme, found in certain bacterial species, is part of a pathway for the production of olefins.

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

References:

1. Bonnett, S.A., Papireddy, K., Higgins, S., del Cardayre, S. and Reynolds, K.A. Functional characterization of an NADPH dependent 2-alkyl-3-ketoalkanoic acid reductase involved in olefin biosynthesis in Stenotrophomonas maltophilia. Biochemistry 50 (2011) 9633-9640. [PMID: 21958090]

[EC 1.1.1.412 created 2017]

EC 1.1.1.413

Accepted name: A-factor type γ-butyrolactone 1'-reductase (1S-forming)

Reaction: a (3R,4R)-3-[(1S)-1-hydroxyalkyl]-4-(hydroxymethyl)oxolan-2-one + NADP+ = a (3R,4R)-3-alkanoyl-4-(hydroxymethyl)oxolan-2-one + NADPH + H+

Glossary: a (3R,4R)-3-[(1S)-1-hydroxyalkyl]-4-(hydroxymethyl)oxolan-2-one = a VB type γ-butyrolactone
a (3R,4R)-3-alkanoyl-4-(hydroxymethyl)oxolan-2-one = an A-factor type γ-butyrolactone

Other name(s): barS1 (gene name)

Systematic name: (3R,4R)-3-[(1S)-1-hydroxyalkyl]-4-(hydroxymethyl)oxolan-2-one:NADP+ 1'-oxidoreductase

Comments: The enzyme, which is found in bacteria that produce virginiae-butanolide (VB) type γ-butyrolactone autoregulators, reduces its substrate stereospecifically, forming a hydroxyl group in the (S) configuration.

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

References:

1. Shikura, N., Yamamura, J. and Nihira, T. barS1, a gene for biosynthesis of a γ-butyrolactone autoregulator, a microbial signaling molecule eliciting antibiotic production in Streptomyces species. J. Bacteriol. 184 (2002) 5151-5157. [PMID: 12193632]

[EC 1.1.1.413 created 2017]


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