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
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, GTD, 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]
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]
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]
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]
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]
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]
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]
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, PDB, 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]
Accepted name: aldose 1-dehydrogenase [NAD(P)+]
Reaction: an aldopyranose + NAD(P)+ = an aldono-1,5-lactone + NAD(P)H + H+
For diagram of reaction click here
Systematic name: an aldopyranose:NAD(P)+ 1-oxidoreductase
Comments: The enzyme from the archaeon Sulfolobus solfataricus shows broad specificity towards aldoses (D-glucose, D-galactose, D-xylose, L-arabinose, 6-deoxy-D-glucose, D-fucose) and can utilize NAD+ and NADP+ with similar catalytic efficiency. It is involved in aldose catabolism via the branched variant of the Entner-Doudoroff pathway.
Links to other databases: BRENDA, EXPASY, KEGG Metacyc, PDB, 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]
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]
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]
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]
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, PDB, 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]
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]
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]
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]
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]
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, PDB, 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]
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, PDB, 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]
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]
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, PDB, 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]
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, PDB, 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]
Accepted name: sulfolactaldehyde 3-reductase
Reaction: (2S)-2,3-dihydroxypropane-1-sulfonate + NAD+ = (2S)-2-hydroxy-3-oxopropane-1-sulfonate + NADH + H+
For diagram of reaction click here.
Glossary: sulfolactaldehyde = (2S)-2-hydroxy-3-oxopropane-1-sulfonate
(2S)-2,3-dihydroxypropane-1-sulfonic acid = (2S)-3-sulfopropanediol = (S)-DHPS
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, PDB, 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]
2. Sharma, M., Abayakoon, P., Lingford, J.P., Epa, R., John, A., Jin, Y., Goddard-Borger, E.D., Davies, G.J. and Williams, S.J. Dynamic structural changes accompany the production of dihydroxypropanesulfonate by sulfolactaldehyde reductase. ACS Catalysis 10 (2020) 2826Ð2836.
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]
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, PDB, 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]
Accepted name: L-arabinose 1-dehydrogenase [NAD(P)+]
Reaction: α-L-arabinopyranose + NAD(P)+ = L-arabinono-1,4-lactone + NAD(P)H + H+
For diagram of reaction click here
Other name(s): L-arabino-aldose dehydrogenase
Systematic name: α-L-arabinopyranose:NAD(P)+ 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. The enzyme is specific for α-L-arabinopyranose [3,4].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, 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]
4. Aro-Karkkainen, N., Toivari, M., Maaheimo, H., Ylilauri, M., Pentikainen, O.T., Andberg, M., Oja, M., Penttila, M., Wiebe, M.G., Ruohonen, L. and Koivula, A. L-arabinose/D-galactose 1-dehydrogenase of Rhizobium leguminosarum bv. trifolii characterised and applied for bioconversion of L-arabinose to L-arabonate with Saccharomyces cerevisiae. Appl. Microbiol. Biotechnol. 98 (2014) 9653-9665. [PMID: 25236800]
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]
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]
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]
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]
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]
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]
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, PDB, 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]
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, PDB, 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]
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, PDB, 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]
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]
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, PDB, 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]
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]
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.
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]
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]
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]
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]
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]
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, PDB, 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]
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]
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]
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]
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, PDB, 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]
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]
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]
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]
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]
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]
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, PDB, 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]
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, PDB, 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]
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]
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, PDB, 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]
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]
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]
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]
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]
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]
Accepted name: L-galactonate 5-dehydrogenase
Reaction: L-galactonate + NAD+ = D-tagaturonate + NADH + H+
Other name(s): lgoD (gene name); lgaC (gene name)
Systematic name: L-galactonate:NAD+ 5-oxidoreductase
Comments: The enzyme, reported from the human gut bacteria Escherichia coli and Bacteroides vulgatus, participates in an L-galactonate degradation pathway.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Cooper, R.A. The pathway for L-galactonate catabolism in Escherichia coli K-12. FEBS Lett. 103 (1979) 216-220. [PMID: 381020]
2. Kuivanen, J. and Richard, P. The yjjN of E. coli codes for an L-galactonate dehydrogenase and can be used for quantification of L-galactonate and L-gulonate. Appl. Biochem. Biotechnol. 173 (2014) 1829-1835. [PMID: 24861318]
3. Hobbs, M.E., Williams, H.J., Hillerich, B., Almo, S.C. and Raushel, F.M. L-Galactose metabolism in Bacteroides vulgatus from the human gut microbiota. Biochemistry 53 (2014) 4661-4670. [PMID: 24963813]
Accepted name: noscapine synthase
Reaction: narcotine hemiacetal + NAD+ = noscapine + NADH + H+
For diagram of reaction click here.
Glossary: noscapine = (3S)-6,7-dimethoxy-3-[(5R)-4-methoxy-6-methyl-5,6,7,8-tetrahydro[1,3]dioxolo[4,5-g]isoquinolin-5-yl]isobenzofuran-1(3H)-one
narcotine hemiacetal = (3S)-6,7-dimethoxy-3-[(5R)-4-methoxy-6-methyl-5,6,7,8-tetrahydro[1,3]dioxolo[4,5-g]isoquinolin-5-yl]-1,3-dihydroisobenzofuran-1-ol
Other name(s): NOS (gene name)
Systematic name: narcotine hemiacetal:NAD+ 1-oxidoreductase
Comments: The enzyme, characterized from the plant Papaver somniferum (opium poppy), catalyses the last step in the biosynthesis of the isoquinoline alkaloid noscapine.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Chen, X. and Facchini, P.J. Short-chain dehydrogenase/reductase catalyzing the final step of noscapine biosynthesis is localized to laticifers in opium poppy. Plant J. 77 (2014) 173-184. [PMID: 24708518]
2. Li, Y., Li, S., Thodey, K., Trenchard, I., Cravens, A. and Smolke, C.D. Complete biosynthesis of noscapine and halogenated alkaloids in yeast. Proc. Natl Acad. Sci. USA 115 (2018) E3922-E3931. [PMID: 29610307]
Accepted name: isopyridoxal dehydrogenase (5-pyridoxolactone-forming)
Reaction: isopyridoxal + NAD+ = 5-pyridoxolactone + NADH + H+
Glossary: isopyridoxal = 5-hydroxy-4-(hydroxymethyl)-6-methylpyridine-3-carbaldehyde
5-pyridoxolactone = 7-hydroxy-6-methylfuro[3,4-c]pyridin-3(1H)-one
Systematic name: isopyridoxal:NAD+ oxidoreductase (5-pyridoxolactone-forming)
Comments: The enzyme, characterized from the bacterium Arthrobacter sp. Cr-7, participates in the degradation of pyridoxine. The enzyme also catalyses the activity of EC 1.2.1.102, isopyridoxal dehydrogenase (5-pyridoxate-forming).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Lee, Y.C., Nelson, M.J. and Snell, E.E. Enzymes of vitamin B6 degradation. Purification and properties of isopyridoxal dehydrogenase and 5-formyl-3-hydroxy-2-methylpyridine-4-carboxylic-acid dehydrogenase. J. Biol. Chem 261 (1986) 15106-15111. [PMID: 3533936]
Accepted name: 3β-hydroxysteroid-4β-carboxylate 3-dehydrogenase (decarboxylating)
Reaction: a 3β-hydroxy-4α-methylsteroid-4β-carboxylate + NAD(P)+ = a 4α-methyl-3-oxosteroid + NAD(P)H + CO2 + H+
Other name(s): sdmB (gene name)
Systematic name: 3β-hydroxysteroid-4β-carboxylate:NAD(P)+ 3-oxidoreductase (decarboxylating)
Comments: This bacterial enzyme participates in the biosynthesis of bacterial sterols. Together with EC 1.14.13.246, 4β-methylsterol monooxygenase (SdmA) it forms an enzyme system that removes one methyl group from the C-4 position of 4,4-dimethylated steroid molecules. SdmA catalyses three successive oxidations of the C-4β methyl group, turning it into a carboxylate group; SdmB is a bifunctional enzyme that catalyses two different activities. As EC 1.1.1.417 it catalyses an oxidative decarboxylation that results in reduction of the 3β-hydroxy group at the C-3 carbon to an oxo group. As EC 1.1.1.270, 3β-hydroxysteroid 3-dehydrogenase, it reduces the 3-oxo group back to a 3β-hydroxyl. Since the remaining methyl group at C-4 is in an α orientation, it cannot serve as a substrate for a second round of demethylation by this system.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Lee, A.K., Banta, A.B., Wei, J.H., Kiemle, D.J., Feng, J., Giner, J.L. and Welander, P.V. C-4 sterol demethylation enzymes distinguish bacterial and eukaryotic sterol synthesis. Proc. Natl Acad. Sci. USA 115 (2018) 5884-5889. [PMID: 29784781]
Accepted name: plant 3β-hydroxysteroid-4α-carboxylate 3-dehydrogenase (decarboxylating)
Reaction: a 3β-hydroxysteroid-4α-carboxylate + NAD+ = a 3-oxosteroid + CO2 + NADH
Other name(s): 3β-HSD/D1 (gene name); 3β-HSD/D2 (gene name); 3β-hydroxysteroid dehydrogenases/C-4 decarboxylase (ambiguous)
Systematic name: 3β-hydroxysteroid-4α-carboxylate:NAD+ 3-oxidoreductase (decarboxylating)
Comments: The enzyme, found in plants, catalyses multiple reactions during plant sterol biosynthesis. Unlike the fungal/animal enzyme EC 1.1.1.170, 3β-hydroxysteroid-4α-carboxylate 3-dehydrogenase (decarboxylating), the plant enzyme is specific for NAD+.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Rondet, S., Taton, M. and Rahier, A. Identification, characterization, and partial purification of 4 α-carboxysterol-C3-dehydrogenase/ C4-decarboxylase from Zea mays. Arch. Biochem. Biophys. 366 (1999) 249-260. [PMID: 10356290]
2. Rahier, A., Darnet, S., Bouvier, F., Camara, B. and Bard, M. Molecular and enzymatic characterizations of novel bifunctional 3β-hydroxysteroid dehydrogenases/C-4 decarboxylases from Arabidopsis thaliana. J. Biol. Chem 281 (2006) 27264-27277. [PMID: 16835224]
3. Rahier, A., Bergdoll, M., Genot, G., Bouvier, F. and Camara, B. Homology modeling and site-directed mutagenesis reveal catalytic key amino acids of 3β-hydroxysteroid-dehydrogenase/C4-decarboxylase from Arabidopsis. Plant Physiol. 149 (2009) 1872-1886. [PMID: 19218365]
Accepted name: nepetalactol dehydrogenase
Reaction: (1) (+)-cis,cis-nepetalactol + NAD+ = (+)-cis,cis-nepetalactone + NADH + H+
(2) (+)-cis,trans-nepetalactol + NAD+ = (+)-cis,trans-nepetalactone + NADH + H+
For diagram of reactionclick here
Glossary: (+)-cis,cis-nepetalactol = (4aR,7S,7aS)-4,7-dimethyl-1,4a,5,6,7,7a-hexahydrocyclopenta[c]pyran-1-ol
(+)-cis,trans-nepetalactol = (+)-iridodial lactol = (4aS,7S,7aR)-4,7-dimethyl-1,4a,5,6,7,7a-hexahydrocyclopenta[c]pyran-1-ol
Other name(s): NEPS1 (gene name)
Systematic name: nepetalactol:NAD+ 1-oxidoreductase
Comments: The enzyme, characterized from the plant Nepeta mussinii, binds an NAD+ cofactor. It also catalyses the activity of EC 5.5.1.34, (+)-cis,trans-nepetalactol synthase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Lichman, B.R., Kamileen, M.O., Titchiner, G.R., Saalbach, G., Stevenson, C.EM., Lawson, D.M. and O'Connor, S.E. Uncoupled activation and cyclization in catmint reductive terpenoid biosynthesis. Nat. Chem. Biol. 15 (2019) 71-79. [PMID: 30531909]
2. Lichman, B.R., O'Connor, S.E. and Kries, H. Biocatalytic strategies towards [4+2] cycloadditions. Chemistry 25 (2019) 6864-6877. [PMID: 30664302]
Accepted name: D-apiose dehydrogenase
Reaction: D-apiofuranose + NAD+ = D-apionolactone + NADH + H+
Other name(s): apsD (gene name)
Systematic name: D-apiofuranose:NAD+ 1-oxidoreductase
Comments: The enzyme, characterized from several bacterial species, is involved in a catabolic pathway for D-apiose.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Carter, M.S., Zhang, X., Huang, H., Bouvier, J.T., Francisco, B.S., Vetting, M.W., Al-Obaidi, N., Bonanno, J.B., Ghosh, A., Zallot, R.G., Andersen, H.M., Almo, S.C. and Gerlt, J.A. Functional assignment of multiple catabolic pathways for D-apiose. Nat. Chem. Biol. 14 (2018) 696-705. [PMID: 29867142]
Accepted name: D-apionate oxidoisomerase
Reaction: D-apionate + NAD+ = 3-oxo-D-isoapionate + NADH + H+
Glossary: 3-oxo-D-isoapionate = 2,4-dihydroxy-2-(hydroxymethyl)-3-oxobutanoate
Other name(s): apnO (gene name)
Systematic name: D-apionate:NAD+ oxidoreductase (isomerizing)
Comments: The enzyme, characterized from several bacterial species, participates in the degradation of D-apionate. The reaction involves migration of a hydroxymethyl group from position 3 to position 2 and oxidation of the 3-hydroxyl group.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Carter, M.S., Zhang, X., Huang, H., Bouvier, J.T., Francisco, B.S., Vetting, M.W., Al-Obaidi, N., Bonanno, J.B., Ghosh, A., Zallot, R.G., Andersen, H.M., Almo, S.C. and Gerlt, J.A. Functional assignment of multiple catabolic pathways for D-apiose. Nat. Chem. Biol. 14 (2018) 696-705. [PMID: 29867142]
Accepted name: pseudoephedrine dehydrogenase
Reaction: (+)-(1S,2S)-pseudoephedrine + NAD+ = (S)-2-(methylamino)-1-phenylpropan-1-one + NADH + H+
Other name(s): PseDH
Systematic name: (+)-(1S,2S)-pseudoephedrine:NAD+ 1-oxidoreductase
Comments: The enzyme, characterized from the bacterium Arthrobacter sp. TS-15, acts on a broad range of different aryl-alkyl ketones, such as haloketones, ketoamines, diketones, and ketoesters. It accepts various types of aryl groups including phenyl-, pyridyl-, thienyl-, and furyl-rings, but the presence of an aromatic ring is essential for the activity. In addition, the presence of a functional group on the alkyl chain, such as an amine, a halogen, or a ketone, is also crucial. The enzyme exhibits a strict anti-Prelog enantioselectivity. When acting on diketones, it catalyses the reduction of only the keto group closest to the ring, with no further reduction to the diol. cf. EC 1.1.1.423, ephedrine dehydrogenase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Shanati, T., Lockie, C., Beloti, L., Grogan, G. and Ansorge-Schumacher, M.B. Two enantiocomplementary ephedrine dehydrogenases from Arthrobacter sp. TS-15 with broad substrate specificity. ACS Catal. 9 (2019) 6202-6211.
2. Shanati, T., Ansorge-Schumacher, M. Enzymes and methods for the stereoselective reduction of carbonyl compounds, oxidation and stereoselective reductive amination - for the enantioselective preparation of alcohol amine compounds. Patent WO2019002459, (2019).
Accepted name: (1R,2S)-ephedrine 1-dehydrogenase
Reaction: (–)-(1R,2S)-ephedrine + NAD+ = (S)-2-(methylamino)-1-phenylpropan-1-one + NADH + H+
Glossary: (–)-(1R,2S)-ephedrine = (1R,2S)-2-(methylamino)-1-phenylpropan-1-ol
(S)-2-(methylamino)-1-phenylpropan-1-one = (S)-methcathinone
Other name(s): EDH; ephedrine dehydrogenase
Systematic name: (–)-(1R,2S)-ephedrine:NAD+ 1-oxidoreductase
Comments: The enzyme, characterized from the bacterium Arthrobacter sp. TS-15, acts on a broad range of different aryl-alkyl ketones, such as haloketones, ketoamines, diketones, and ketoesters. It exhibits a strict enantioselectivity and accepts various types of aryl groups including phenyl-, pyridyl-, thienyl-, and furyl-rings, but the presence of an aromatic ring is essential for the activity. In addition, the presence of a functional group on the alkyl chain, such as an amine, a halogen, or a ketone, is also crucial. When acting on diketones, it catalyses the reduction of only the keto group closest to the ring, with no further reduction to the diol. cf. EC 1.1.1.422, pseudoephedrine dehydrogenase and EC 1.5.1.18, ephedrine dehydrogenase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Shanati, T., Lockie, C., Beloti, L., Grogan, G. and Ansorge-Schumacher, M.B. Two enantiocomplementary ephedrine dehydrogenases from Arthrobacter sp. TS-15 with broad substrate specificity. ACS Catal. 9 (2019) 6202-6211.
2. Shanati, T., Ansorge-Schumacher, M. Enzymes and methods for the stereoselective reduction of carbonyl compounds, oxidation and stereoselective reductive amination - for the enantioselective preparation of alcohol amine compounds. (2019) Patent WO2019002459.
Accepted name: D-xylose 1-dehydrogenase (NADP+, D-xylono-1,4-lactone-forming)
Reaction: D-xylose + NADP+ = D-xylono-1,4-lactone + NADPH + H+
Other name(s): xacA (gene name); xdh (gene name)
Systematic name: D-xylose:NADP+ 1-oxidoreductase (D-xylono-1,4-lactone-forming)
Comments: The enzyme, which participates in the degradation of D-xylose, has been characterized from several halophilic archaeal species. cf. EC 1.1.1.179, D-xylose 1-dehydrogenase (NADP+, D-xylono-1,5-lactone-forming).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Johnsen, U. and Schonheit, P. Novel xylose dehydrogenase in the halophilic archaeon Haloarcula marismortui. J. Bacteriol. 186 (2004) 6198-6207. [PMID: 15342590]
2. Johnsen, U., Dambeck, M., Zaiss, H., Fuhrer, T., Soppa, J., Sauer, U. and Schonheit, P. D-Xylose degradation pathway in the halophilic archaeon Haloferax volcanii. J. Biol. Chem. 284 (2009) 27290-27303. [PMID: 19584053]
3. Sutter, J.M., Johnsen, U. and Schonheit, P. Characterization of a pentonolactonase involved in D-xylose and L-arabinose catabolism in the haloarchaeon Haloferax volcanii. FEMS Microbiol. Lett. 364 (2017) . [PMID: 28854683]
Accepted name: levoglucosan dehydrogenase
Reaction: levoglucosan + NAD+ = 3-dehydrolevoglucosan + NADH + H+
Glossary: levoglucosan = 1,6-anhydro-β-D-glucopyranose
Other name(s): 1,6-anhydro-β-D-glucose dehydrogenase
Systematic name: 1,6-anhydro-β-D-glucopyranose:NAD+ 3-oxidoreductase
Comments: Levoglucosan is formed from the pyrolysis of carbohydrates such as starch and cellulose and is an important molecular marker for pollution from biomass burning. This enzyme is present only in bacteria, and has been characterized from Arthrobacter sp. I-552 and Pseudarthrobacter phenanthrenivorans. cf. EC 2.7.1.232, levoglucosan kinase.
References:
1. Nakahara, K., Kitamura, Y., Yamagishi, Y., Shoun, H. and Yasui, T. Levoglucosan dehydrogenase involved in the assimilation of levoglucosan in Arthrobacter sp. I-552. Biosci. Biotechnol. Biochem. 58 (1994) 2193-2196. [PMID: 7765713]
2. Sugiura, M., Nakahara, M., Yamada, C., Arakawa, T., Kitaoka, M. and Fushinobu, S. Identification, functional characterization, and crystal structure determination of bacterial levoglucosan dehydrogenase. J. Biol. Chem. 293 (2018) 17375-17386. [PMID: 30224354]
Accepted name: UDP-N-acetyl-α-D-quinovosamine dehydrogenase
Reaction: UDP-N-acetyl-α-D-quinovosamine + NAD(P)+ = UDP-2-acetamido-2,6-dideoxy-α-D-xylohex-4-ulose + NAD(P)H + H+
Glossary: UDP-N-acetyl-α-D-quinovosamine = UDP-N-acetyl-6-deoxy-α-D-glucosamine
Other name(s): wbpV (gene name); wreQ (gene name)
Systematic name: UDP-N-acetyl-α-D-quinovosamine:NAD(P)+ 4-dehydrogenase
Comments: The enzyme participates in the biosynthesis of N-acetyl-α-D-quinovosamine, a 6-deoxy sugar that is present in the O antigens of many Gram-negative bacteria, including Pseudomonas aeruginosa serotypes O6 and O10, Rhizobium etli, and Brucella abortus.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Belanger, M., Burrows, L.L. and Lam, J.S. Functional analysis of genes responsible for the synthesis of the B-band O antigen of Pseudomonas aeruginosa serotype O6 lipopolysaccharide. Microbiology (Reading) 145 (1999) 3505-3521. [PMID: 10627048]
2. Forsberg, L.S., Noel, K.D., Box, J. and Carlson, R.W. Genetic locus and structural characterization of the biochemical defect in the O-antigenic polysaccharide of the symbiotically deficient Rhizobium etli mutant, CE166. Replacement of N-acetylquinovosamine with its hexosyl-4-ulose precursor. J. Biol. Chem. 278 (2003) 51347-51359. [PMID: 14551189]
3. Li, T., Simonds, L., Kovrigin, E.L. and Noel, K.D. In vitro biosynthesis and chemical identification of UDP-N-acetyl-D-quinovosamine (UDP-D-QuiNAc). J. Biol. Chem. 289 (2014) 18110-18120. [PMID: 24817117]
Accepted name: D-arabinose 1-dehydrogenase (NADP+)
Reaction: D-arabinofuranose + NADP+ = D-arabinono-1,4-lactone + NADPH + H+
Other name(s): AraDH; adh-4 (gene name)
Systematic name: D-arabinose:NADP+ 1-oxidoreductase
Comments: The enzyme from the archaeon Saccharolobus solfataricus is tetrameric and contains zinc. L-fucose also is a substrate. In contrast to EC 1.1.1.116 (D-arabinose 1-dehydrogenase (NAD+)) and EC 1.1.1.117 (D-arabinose 1-dehydrogenase [NAD(P)+]), this enzyme is specific for NADP+.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Brouns, S.J., Walther, J., Snijders, A.P., van de Werken, H.J., Willemen, H.L., Worm, P., de Vos, M.G., Andersson, A., Lundgren, M., Mazon, H.F., van den Heuvel, R.H., Nilsson, P., Salmon, L., de Vos, W.M., Wright, P.C., Bernander, R. and van der Oost, J. Identification of the missing links in prokaryotic pentose oxidation pathways: evidence for enzyme recruitment. J. Biol. Chem. 281 (2006) 27378-27388. [PMID: 16849334]
2. Brouns, S.J., Turnbull, A.P., Willemen, H.L., Akerboom, J. and van der Oost, J. Crystal structure and biochemical properties of the D-arabinose dehydrogenase from Sulfolobus solfataricus. J. Mol. Biol. 371 (2007) 1249-1260. [PMID: 17610898]
Accepted name: 4-methylthio 2-oxobutanoate reductase (NADH)
Reaction: (2R)-2-hydroxy-4-(methylsulfanyl)butanoate + NAD+ = 4-(methylsulfanyl)-2-oxobutanoate + NADH + H+
Other name(s): CTBP1 (gene name); C-terminal-binding protein 1; MTOB reductase; 4-methylthio 2-oxobutyrate reductase; 4-methylthio 2-oxobutyric acid reductase
Systematic name: (2R)-2-hydroxy-4-(methylsulfanyl)butanoate:NAD+ 2-oxidoreductase
Comments: The substrate of this enzyme is formed as an intermediate during L-methionine salvage from S-methyl-5'-thioadenosine, which is formed during the biosynthesis of polyamines. The human enzyme also functions as a transcriptional co-regulator that downregulates the expression of many tumor-suppressor genes, thus providing a link between gene repression and the methionine salvage pathway. A similar, but NADP-specific, enzyme is involved in dimethylsulfoniopropanoate biosynthesis in algae and phytoplankton.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Kumar, V., Carlson, J.E., Ohgi, K.A., Edwards, T.A., Rose, D.W., Escalante, C.R., Rosenfeld, M.G. and Aggarwal, A.K. Transcription corepressor CtBP is an NAD(+)-regulated dehydrogenase. Mol. Cell 10 (2002) 857-869. [PMID: 12419229]
2. Achouri, Y., Noel, G. and Van Schaftingen, E. 2-Keto-4-methylthiobutyrate, an intermediate in the methionine salvage pathway, is a good substrate for CtBP1. Biochem. Biophys. Res. Commun. 352 (2007) 903-906. [PMID: 17157814]
3. Hilbert, B.J., Grossman, S.R., Schiffer, C.A. and Royer, W.E., Jr. Crystal structures of human CtBP in complex with substrate MTOB reveal active site features useful for inhibitor design. FEBS Lett. 588 (2014) 1743-1748. [PMID: 24657618]
4. Korwar, S., Morris, B.L., Parikh, H.I., Coover, R.A., Doughty, T.W., Love, I.M., Hilbert, B.J., Royer, W.E., Jr., Kellogg, G.E., Grossman, S.R. and Ellis, K.C. Design, synthesis, and biological evaluation of substrate-competitive inhibitors of C-terminal Binding Protein (CtBP). Bioorg. Med. Chem. 24 (2016) 2707-2715. [PMID: 27156192]
Accepted name: (2S)-[(R)-hydroxy(phenyl)methyl]succinyl-CoA dehydrogenase
Reaction: (2S)-[(R)-hydroxy(phenyl)methyl]succinyl-CoA + NAD+ = (S)-2-benzoylsuccinyl-CoA + NADH + H+
Other name(s): bbsCD (gene name)
Systematic name: (2S)-[(R)-hydroxy(phenyl)methyl]succinyl-CoA:NAD+ oxidoreductase
Comments: The enzyme, purified from the bacterium Thauera aromatica, is involved in an anaerobic toluene degradation pathway. It is specific for NAD+.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. von Horsten, S., Lippert, M.L., Geisselbrecht, Y., Schuhle, K., Schall, I., Essen, L.O. and Heider, J. Inactive pseudoenzyme subunits in heterotetrameric BbsCD, a novel short-chain alcohol dehydrogenase involved in anaerobic toluene degradation. FEBS J. (2021) . [PMID: 34601806]
Accepted name: D-xylose reductase (NADH)
Reaction: xylitol + NAD+ = D-xylose + NADH + H+
Other name(s): XYL1 (gene name) (ambiguous)
Systematic name: xylitol:NAD+ oxidoreductase
Comments: Xylose reductases catalyse the reduction of xylose to xylitol, the initial reaction in the fungal D-xylose degradation pathway. Most of the enzymes exhibit a strict requirement for NADPH (cf. EC 1.1.1.431, D-xylose reductase (NADPH)). Some D-xylose reductases have dual coenzyme specificity, though they still prefer NADPH to NADH (cf. EC 1.1.1.307, D-xylose reductase [NAD(P)H]). The enzyme from Candida parapsilosis is a rare example of a xylose reductase that significantly prefers NADH, with Km and Vmax values for NADH being 10-fold lower and 10-fold higher, respectively, than for NADPH.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Lee, J.K., Koo, B.S. and Kim, S.Y. Cloning and characterization of the xyl1 gene, encoding an NADH-preferring xylose reductase from Candida parapsilosis, and its functional expression in Candida tropicalis. Appl. Environ. Microbiol. 69 (2003) 6179-6188. [PMID: 14532079]
Accepted name: D-xylose reductase (NADPH)
Reaction: xylitol + NADP+ = D-xylose + NADPH + H+
Other name(s): XYL1 (gene name, ambiguous); xyl1 (gene name, ambiguous); xyrA (gene name); xyrB (gene name)
Systematic name: xylitol:NADP+ oxidoreductase
Comments: Xylose reductases catalyse the reduction of xylose to xylitol, the initial reaction in the fungal D-xylose degradation pathway. Most of the enzymes exhibit a strict requirement for NADPH (e.g. the enzymes from Saccharomyces cerevisiae, Aspergillus niger, Trichoderma reesei, Candida tropicalis, Saitozyma flava, and Candida intermedia). Some D-xylose reductases have dual coenzyme specificity, though they still prefer NADPH to NADH (cf. EC 1.1.1.307, D-xylose reductase [NAD(P)H]). Very rarely the enzyme prefers NADH (cf. EC 1.1.1.430, D-xylose reductase (NADH)).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Bolen, P.L. and Detroy, R.W. Induction of NADPH-linked D-xylose reductase and NAD-linked xylitol dehydrogenase activities in Pachysolen tannophilus by D-xylose, L-arabinose, or D-galactose. Biotechnol. Bioeng. 27 (1985) 302-307. [PMID: 18553673]
2. Suzuki, T., Yokoyama, S., Kinoshita, Y., Yamada, H., Hatsu, M., Takamizawa, K. and Kawai, K. Expression of xyrA gene encoding for D-xylose reductase of Candida tropicalis and production of xylitol in Escherichia coli. J. Biosci. Bioeng. 87 (1999) 280-284. [PMID: 16232468]
3. Nidetzky, B., Mayr, P., Hadwiger, P. and Stutz, A.E. Binding energy and specificity in the catalytic mechanism of yeast aldose reductases. Biochem. J. 344 Pt 1 (1999) 101-107. [PMID: 10548539]
4. Mayr, P., Bruggler, K., Kulbe, K.D. and Nidetzky, B. D-Xylose metabolism by Candida intermedia: isolation and characterisation of two forms of aldose reductase with different coenzyme specificities. J. Chromatogr. B Biomed. Sci. Appl. 737 (2000) 195-202. [PMID: 10681056]
5. Sene, L., Felipe, M.G., Silva, S.S. and Vitolo, M. Preliminary kinetic characterization of xylose reductase and xylitol dehydrogenase extracted from Candida guilliermondii FTI 20037 cultivated in sugarcane bagasse hydrolysate for xylitol production. Appl. Biochem. Biotechnol. 91-93 (2001) 671-680. [PMID: 11963895]
6. Jeong, E.Y., Sopher, C., Kim, I.S. and Lee, H. Mutational study of the role of tyrosine-49 in the Saccharomyces cerevisiae xylose reductase. Yeast 18 (2001) 1081-1089. [PMID: 11481678]
7. Chroumpi, T., Peng, M., Aguilar-Pontes, M.V., Muller, A., Wang, M., Yan, J., Lipzen, A., Ng, V., Grigoriev, I.V., Makela, M.R. and de Vries, R.P. Revisiting a ‘simple’ fungal metabolic pathway reveals redundancy, complexity and diversity. Microb. Biotechnol. 14 (2021) 2525-2537. [PMID: 33666344]
8. Terebieniec, A., Chroumpi, T., Dilokpimol, A., Aguilar-Pontes, M.V., Makela, M.R. and de Vries, R.P. Characterization of D-xylose reductase, XyrB, from Aspergillus niger. Biotechnol Rep (Amst) 30 (2021) e00610. [PMID: 33842213]
Accepted name: 6-dehydroglucose reductase
Reaction: D-glucose + NADP+ = 6-dehydro-D-glucose + NADPH + H+
Glossary: quinovose = 6-deoxy-D-glucopyranose
Other name(s): D-glucose 6-dehydrogenase; smoB (gene name); squF (gene name)
Systematic name: D-glucose:NADP+ 6-oxidoreductase
Comments: The enzyme, characterized from alphaproteobacteria, is involved in a D-sulfoquinovose degradation pathway.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Sharma, M., Lingford, J.P., Petricevic, M., Snow, A.J.D., Zhang, Y., Jarva, M.A., Mui, J.W., Scott, N.E., Saunders, E.C., Mao, R., Epa, R., da Silva, B.M., Pires, D.E.V., Ascher, D.B., McConville, M.J., Davies, G.J., Williams, S.J. and Goddard-Borger, E.D. Oxidative desulfurization pathway for complete catabolism of sulfoquinovose by bacteria. Proc. Natl. Acad. Sci. USA 119 (2022) e2116022119. [PMID: 35074914]
2. Liu, J., Wei, Y., Ma, K., An, J., Liu, X., Liu, Y., Ang, E.L., Zhao, H. and Zhang, Y. Mechanistically diverse pathways for sulfoquinovose degradation in bacteria. ACS Catal. 11 (2021) 14740-14750.
Accepted name: sulfoacetaldehyde reductase (NADH)
Reaction: isethionate + NAD+ = 2-sulfoacetaldehyde + NADH + H+
Glossary: isethionate = 2-hydroxyethanesulfonate
2-sulfoacetaldehyde = 2-oxoethanesulfonate
Other name(s): sarD (gene name); tauF (gene name); sqwF (gene name); BkTauF
Systematic name: isethionate:NAD+ oxidoreductase
Comments: The enzymes from the bacteria Bilophila wadsworthia and Clostridium sp. MSTE9 catalyse the reaction only in the reduction direction. In the bacterium Bifidobacterium kashiwanohense the optimal reaction pH for sulfoacetaldehyde reduction is 7.5, while that for isethionate oxidation is 10.0. cf. EC 1.1.1.313, sulfoacetaldehyde reductase (NADPH).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Peck, S.C., Denger, K., Burrichter, A., Irwin, S.M., Balskus, E.P. and Schleheck, D. A glycyl radical enzyme enables hydrogen sulfide production by the human intestinal bacterium Bilophila wadsworthia. Proc. Natl. Acad. Sci. USA 116 (2019) 3171-3176. [PMID: 30718429]
2. Xing, M., Wei, Y., Zhou, Y., Zhang, J., Lin, L., Hu, Y., Hua, G.,, N. Nanjaraj Urs, A., Liu, D., Wang, F., Guo, C., Tong, Y., Li, M., Liu, Y., Ang, E.L., Zhao, H., Yuchi, Z. and Zhang, Y. Radical-mediated C-S bond cleavage in C2 sulfonate degradation by anaerobic bacteria. Nat. Commun. 10 (2019) 1609. [PMID: 30962433]
3. Zhou, Y., Wei, Y., Nanjaraj Urs, A.N., Lin, L., Xu, T., Hu, Y., Ang, E.L., Zhao, H., Yuchi, Z. and Zhang, Y. Identification and characterization of a new sulfoacetaldehyde reductase from the human gut bacterium Bifidobacterium kashiwanohense. Biosci Rep 39 (2019) . [PMID: 31123167]
4. Liu, J., Wei, Y., Ma, K., An, J., Liu, X., Liu, Y., Ang, E.L., Zhao, H. and Zhang, Y. Mechanistically diverse pathways for sulfoquinovose degradation in bacteria. ACS Catal. 11 (2021) 14740-14750.
Accepted name: 2-dehydro-3-deoxy-L-fuconate 4-dehydrogenase
Reaction: 2-dehydro-3-deoxy-L-fuconate + NAD+ = 2,4-didehydro-3-deoxy-L-fuconate + NADH + H+
For diagram of reaction click here
Glossary: 2-dehydro-3-deoxy-L-fuconate = (4S,5S)-4,5-dihydroxy-2-oxohexanoate
2,4-didehydro-3-deoxy-L-fuconate = (5S)-5-hydroxy-2,4-dioxohexanoate
Systematic name: 2-dehydro-3-deoxy-L-fuconate:NAD+ 4-oxidoreductase
Comments: The enzyme, originally described from the bacterium Xanthomonas campestris pv. campestris, participates in an L-fucose degradation pathway. It can also act on 2-dehydro-3-deoxy-L-galactonate and 2-dehydro-3-deoxy-D-pentonate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Yew, W.S., Fedorov, A.A., Fedorov, E.V., Rakus, J.F., Pierce, R.W., Almo, S.C. and Gerlt, J.A. Evolution of enzymatic activities in the enolase superfamily: L-fuconate dehydratase from Xanthomonas campestris. Biochemistry 45 (2006) 14582-14597. [PMID: 17144652]
2. Watanabe, S., Fukumori, F., Nishiwaki, H., Sakurai, Y., Tajima, K. and Watanabe, Y. Novel non-phosphorylative pathway of pentose metabolism from bacteria. Sci. Rep. 9 (2019) 155. [PMID: 30655589]
Accepted name: L-fucose dehydrogenase
For diagram of reaction click here
Reaction: β-L-fucopyranose + NADP+ = L-fucono-1,5-lactone + NADPH + H+
Systematic name: β-L-fucopyranose:NADP+ 1-oxidoreductase
Comments: The enzyme, characterized from the bacterium Burkholderia multivorans, participates in an L-fucose degradation pathway. The enzyme catalyses the oxidation of β-L-fucopyranose to L-fucono-1,5-lactone, which is unstable and is rapidly converted to L-fucono-1,4-lactone. The α anomer is not recognized. The enzyme can also act on β-L-galactopyranose and D-arabinose with lower activity. NADP is a better cosubstrate than NAD.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Hobbs, M.E., Vetting, M., Williams, H.J., Narindoshvili, T., Kebodeaux, D.M., Hillerich, B., Seidel, R.D., Almo, S.C. and Raushel, F.M. Discovery of an L-fucono-1,5-lactonase from cog3618 of the amidohydrolase superfamily. Biochemistry 52 (2013) 239-253. [PMID: 23214453]
Accepted name: lactate dehydrogenase (NAD+,ferredoxin)
Reaction: lactate + 2 NAD+ + 2 reduced ferredoxin [iron-sulfur] cluster = pyruvate + 2 NADH + 2 oxidized ferredoxin [iron-sulfur] cluster
Other name(s): electron bifurcating LDH/Etf complex
Systematic name: lactate:NAD+,ferredoxin oxidoreductase
Comments: The enzyme, isolated from the bacterium Acetobacterium woodii, uses flavin-based electron confurcation to drive endergonic lactate oxidation with NAD+ as oxidant at the expense of simultaneous exergonic electron flow from reduced ferredoxin to NAD+.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Weghoff, M.C., Bertsch, J. and Muller, V. A novel mode of lactate metabolism in strictly anaerobic bacteria. Environ. Microbiol. 17 (2015) 670-677. [PMID: 24762045]
Accepted name: 5-dehydrofumagillol 5-reductase
Reaction: fumagillol + NADP+ = 5-dehydrofumagillol + NADPH + H+
For diagram of reaction click here
Glossary: fumagillol = (3R,4S,5S,6R)-5-methoxy-4-[(2R,3R)-2-methyl-3-(3-methylbut-2-en-1-yl)oxiran-2-yl]-1-oxaspiro[2.5]octan-6-ol
Other name(s): af490 (gene name); Fma-KR
Systematic name: fumagillol:NADP+ 5-oxidoreductase
Comments: The enzyme, characterized from the mold Aspergillus fumigatus, participates in the biosynthesis of the meroterpenoid fumagillin. It is a partial polyketide synthase (PKS) consisting of only a dehydratase (DH) and a ketoreductase (KR) domain.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Lin, H.C., Tsunematsu, Y., Dhingra, S., Xu, W., Fukutomi, M., Chooi, Y.H., Cane, D.E., Calvo, A.M., Watanabe, K. and Tang, Y. Generation of complexity in fungal terpene biosynthesis: discovery of a multifunctional cytochrome P450 in the fumagillin pathway. J. Am. Chem. Soc. 136 (2014) 4426-4436. [PMID: 24568283]
Accepted name: cis-4-hydroxycyclohexanecarboxylate dehydrogenase
Reaction: cis-4-hydroxycyclohexane-1-carboxylate + NAD+ = 4-oxocyclohexane-1-carboxylate + NADH + H+
Glossary: cis-4-hydroxycyclohexane-1-carboxylate = cis-4-hydroxycyclohexanecarboxylate
4-oxocyclohexane-1-carboxylate = 4-oxocyclohexanecarboxylate
Other name(s): chcB2 (gene name)
Systematic name: cis-4-hydroxycyclohexane-1-carboxylate:NAD+ 4-oxidoreductase
Comments: The enzyme from Corynebacterium cyclohexanicum is highly specific for the cis-4-hydroxy derivative. cf. EC 1.1.1.226, trans-4-hydroxycyclohexanecarboxylate dehydrogenase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Yamamoto, T., Hasegawa, Y., Lau, P.CK. and Iwaki, H. Identification and characterization of a chc gene cluster responsible for the aromatization pathway of cyclohexanecarboxylate degradation in Sinomonas cyclohexanicum ATCC 51369. J. Biosci. Bioeng. 132 (2021) 621-629. [PMID: 34583900]
Accepted name: 17-dehydrostemmadenine reductase
Reaction: stemmadenine + NADP+ = 17-dehydrostemmadenine + NADPH + H+
For diagram of reaction, click here
Other name(s): Redox2
Systematic name: stemmadenine:NADP+ 17-oxidoreductase
Comments: The enzyme, characterized from the plant Catharanthus roseus (Madagascar periwinkle), participates in a biosynthetic pathway that leads to production of the bisindole alkaloid compounds vinblastine and vincristine, which are used as anticancer drugs.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Qu, Y., Easson, M.EA.M., Simionescu, R., Hajicek, J., Thamm, A.MK., Salim, V. and De Luca, V. Solution of the multistep pathway for assembly of corynanthean, strychnos, iboga, and aspidosperma monoterpenoid indole alkaloids from 19E-geissoschizine. Proc. Natl. Acad. Sci. USA 115 (2018) 3180-3185. [PMID: 29511102]
Accepted name: rhazimal reductase
Reaction: rhazimol + NADP+ = rhazimal + NADPH + H+
For diagram of reaction click here
Other name(s): AsRHR
Systematic name: rhazimol:NADP+ oxidoreductase (rhazimol-forming)
Comments: Isolated from the plant Alstonia scholaris (blackboard tree).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Wang, Z., Xiao, Y., Wu, S., Chen, J., Li, A. and Tatsis, E.C. Deciphering and reprogramming the cyclization regioselectivity in bifurcation of indole alkaloid biosynthesis. Chem. Sci. 13 (2022) 12389-12395. [PMID: 36349266]
Accepted name: polyprenol dehydrogenase [NAD(P)H]
Reaction: (1) a ditrans,polycis-polyprenol + NAD(P)+ = a ditrans,polycis-polyprenal + NAD(P)H + H+
(2) a dolichol + NAD(P)+ = a dolichal + NAD(P)H + H+
Other name(s): dolichal reductase; DHRSX (gene name)
Systematic name: ditrans,polycis-polyprenol:NAD(P)+ oxidoreductase
Comments: The enzyme, present in all eukaryotes, catalyses the dehydrogenation of ditrans,polycis-polyprenol and the reduction of dolichal as part of the pathway that converts ditrans,polycis-polyprenol to dolichol (cf. EC 1.3.1.94, polyprenal reductase). The enzyme works equally well with NAD+ and NADP+, but due to the cellular ratios of NAD+/NADH and NADP+/NADPH, the enzyme catalyses the oxidation of of polyprenol using NAD+ as the electron acceptor, and the reduction of dolichal using NADPH as the electron donor.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Wilson, M.P., Kentache, T., Althoff, C.R., Schulz, C., de Bettignies, G., Mateu Cabrera, G., Cimbalistiene, L., Burnyte, B., Yoon, G., Costain, G., Vuillaumier-Barrot, S., Cheillan, D., Rymen, D., Rychtarova, L., Hansikova, H., Bury, M., Dewulf, J.P., Caligiore, F., Jaeken, J., Cantagrel, V., Van Schaftingen, E., Matthijs, G., Foulquier, F. and Bommer, G.T. A pseudoautosomal glycosylation disorder prompts the revision of dolichol biosynthesis. Cell (2024) . [PMID: 38821050]