Continued from EC 1.4
EC 1.5.1 With NAD+ or NADP+ as acceptor
EC 1.5.3 With oxygen as acceptor
EC 1.5.4 With a disulfide as acceptor
EC 1.5.5 With a quinone or similar compound as acceptor
EC 1.5.7 With an iron-sulfur protein as acceptor
EC 1.5.8 With a flavin as acceptor
EC 1.5.98 With other, known, physiological acceptor
EC 1.5.99 With unknown physiological acceptor
Accepted name: 1-piperideine-2-carboxylate/1-pyrroline-2-carboxylate reductase [NAD(P)H]
Reaction: (1) L-pipecolate + NAD(P)+ = 1-piperideine-2-carboxylate + NAD(P)H + H+
(2) L-proline + NAD(P)+ = 1-pyrroline-2-carboxylate + NAD(P)H + H+
Other name(s): Δ1-pyrroline-2-carboxylate reductase; DELTA1-pyrroline-2-carboxylate reductase; DELTA1-piperideine-2-carboxylate/1-pyrroline-2-carboxylate reductase (ambiguous); AbLhpI; pyrroline-2-carboxylate reductase; L-proline:NAD(P)+ 2-oxidoreductase
Systematic name: L-pipecolate/L-proline:NAD(P)+ 2-oxidoreductase
Comments: The enzymes, characterized from the bacterium Azospirillum brasilense, is involved in trans-3-hydroxy-L-proline metabolism. In contrast to EC 1.5.1.21, 1-piperideine-2-carboxylate/1-pyrroline-2-carboxylate reductase (NADPH), which is specific for NADPH, this enzyme shows similar activity with NADPH and NADH.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 9029-16-7
References:
1. Meister, A., Radhakrishnan, A.N. and Buckley, S.D. Enzymatic synthesis of L-pipecolic acid and L-proline. J. Biol. Chem. 229 (1957) 789-800. [PMID: 13502341]
2. Watanabe, S., Tanimoto, Y., Yamauchi, S., Tozawa, Y., Sawayama, S. and Watanabe, Y. Identification and characterization of trans-3-hydroxy-L-proline dehydratase and Δ1-pyrroline-2-carboxylate reductase involved in trans-3-hydroxy-L-proline metabolism of bacteria. FEBS Open Bio 4 (2014) 240-250. [PMID: 24649405]
Accepted name: pyrroline-5-carboxylate reductase
Reaction: L-proline + NAD(P)+ = 1-pyrroline-5-carboxylate + NAD(P)H + H+
For diagram click here.
Other name(s): proline oxidase; L-proline oxidase; 1-pyrroline-5-carboxylate reductase; NADPH-L-δ1-pyrroline carboxylic acid reductase; L-proline-NAD(P)+ 5-oxidoreductase
Systematic name: L-proline:NAD(P)+ 5-oxidoreductase
Comments: Also reduces 1-pyrroline-3-hydroxy-5-carboxylate to L-hydroxyproline.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9029-17-8
References:
1. Adams, E. and Goldstone, A. Hydroxyproline metabolism. III. Enzymatic synthesis of hydroxyproline from δ1-pyrroline-3-hydroxy-5-carboxylate. J. Biol. Chem. 235 (1960) 3499-3503.
2. Meister, A., Radhakrishnan, A.N. and Buckley, S.D. Enzymatic synthesis of L-pipecolic acid and L-proline. J. Biol. Chem. 229 (1957) 789-800.
3. Smith, M.E. and Greenberg, D.M. Characterization of an enzyme reducing pyrroline-5-carboxylate to proline. Nature (Lond.) 177 (1956) 1130.
4. Yura, T. and Vogel, H.J. Pyrroline-5-carboxylate reductase of Neurospora crassa: partial purification and some properties. J. Biol. Chem. 234 (1959) 335-338.
Accepted name: dihydrofolate reductase
Reaction: 5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH + H+
For diagram of reaction click here.
Other name(s): tetrahydrofolate dehydrogenase; DHFR; pteridine reductase:dihydrofolate reductase; dihydrofolate reductase:thymidylate synthase; thymidylate synthetase-dihydrofolate reductase; folic acid reductase; folic reductase; dihydrofolic acid reductase; dihydrofolic reductase; 7,8-dihydrofolate reductase; NADPH-dihydrofolate reductase
Systematic name: 5,6,7,8-tetrahydrofolate:NADP+ oxidoreductase
Comments: The enzyme from animals and some micro-organisms also slowly reduces folate to 5,6,7,8-tetrahydrofolate.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9002-03-3
References:
1. Blakley, R.L. and MacDougall, B.M. Dihydrofolic reductase from Streptococcus faecalis R. J. Biol. Chem. 236 (1961) 1163.
2. Bolin, J.T., Filman, D.J., Matthews, D.A. and Kraut, J. Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 Å resolution. I. General features and binding of methotrexate. J. Biol. Chem. 257 (1982) 13650-13662. [PMID: 6815178]
3. Kaufman, B.T. and Gardiner, R.C. Studies on dihydrofolic reductase. I. Purification and properties of dihydrofolic reductase from chicken liver. J. Biol. Chem. 241 (1966) 1319-1328. [PMID: 4379915]
4. Young, I.G. and Gibson, F. Regulation of the enzymes involved in the biosynthesis of 2,3-dihydroxybenzoic acid in Aerobacter aerogenes and Escherichia coli. Biochim. Biophys. Acta 177 (1969) 401-411. [PMID: 4306838]
[EC 1.5.1.4 Deleted entry: dihydrofolate dehydrogenase. Now included with EC 1.5.1.3 dihydrofolate reductase (EC 1.5.1.4 created 1961, deleted 1976)]
Accepted name: methylenetetrahydrofolate dehydrogenase (NADP+)
Reaction: 5,10-methylenetetrahydrofolate + NADP+ = 5,10-methenyltetrahydrofolate + NADPH + H+
For diagram of reaction click here (another example).
Other name(s): N5,N10-methylenetetrahydrofolate dehydrogenase; 5,10-methylenetetrahydrofolate:NADP oxidoreductase; 5,10-methylenetetrahydrofolate dehydrogenase; methylenetetrahydrofolate dehydrogenase
Systematic name: 5,10-methylenetetrahydrofolate:NADP+ oxidoreductase
Comments: In eukaryotes, occurs as a trifunctional enzyme also having methenyltetrahydrofolate cyclohydrolase (EC 3.5.4.9) and formate—tetrahydrofolate ligase (EC 6.3.4.3) activity. In some prokaryotes occurs as a bifunctional enzyme also having methenyltetrahydrofolate cyclohydrolase activity (EC 3.5.4.9).
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9029-14-5
References:
1. Hatefi, Y., Osborn, M.J., Kay, L.D. and Huennekens, F.M. Hydroxymethyl tetrahydrofolic dehydrogenase. J. Biol. Chem. 227 (1957) 637-647.
2. Osborn, M.J. and Huennekens, F.M. Participation of anhydroleucovorin in the hydroxymethyl tetrahydrofolic dehydrogenase system. Biochim. Biophys. Acta 26 (1957) 646-647.
3. Ramasastri, B.V. and Blakley, R.L. 5,10-Methylenetetrahydrofolic acid dehydrogenase from Bakers' yeast. I. Partial purification and some properties. J. Biol. Chem. 237 (1962) 1982-1988.
4. Yeh, Y.-C. and Greenberg, D.M. Purification and properties of N5,N10-methylenetetrahydrofolate dehydrogenase of calf thymus. Biochim. Biophys. Acta 105 (1965) 279-291. [PMID: 4379024]
Accepted name: formyltetrahydrofolate dehydrogenase
Reaction: 10-formyltetrahydrofolate + NADP+ + H2O = tetrahydrofolate + CO2 + NADPH + H+
For diagram of reaction click here (another example).
Other name(s): 10-formyl tetrahydrofolate:NADP oxidoreductase; 10-formyl-H2PtGlu:NADP oxidoreductase ; 10-formyl-H4folate dehydrogenase; N10-formyltetrahydrofolate dehydrogenase ; 10-formyltetrahydrofolate dehydrogenase
Systematic name: 10-formyltetrahydrofolate:NADP+ oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37256-25-0
References:
1. Kutzbach, C. and Stokstad, E.L.R. Partial purification of a 10-formyl-tetrahydrofolate: NADP oxidoreductase from mammalian liver. Biochem. Biophys. Res. Commun. 30 (1968) 111-117. [PMID: 4384443]
Accepted name: saccharopine dehydrogenase (NAD+, L-lysine-forming)
Reaction: N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O = L-lysine + 2-oxoglutarate + NADH + H+
For diagram click here, another example.
Glossary: L-saccharopine = N6-(L-1,3-dicarboxypropyl)-L-lysine
Other name(s): lysine—2-oxoglutarate reductase; dehydrogenase, saccharopine (nicotinamide adenine dinucleotide, lysine forming); ε-N-(L-glutaryl-2)-L-lysine:NAD oxidoreductase (L-lysine forming); N6-(glutar-2-yl)-L-lysine:NAD oxidoreductase (L-lysine-forming)
Systematic name: N6-(L-1,3-dicarboxypropyl)-L-lysine:NAD+ oxidoreductase (L-lysine-forming)
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9073-96-5
References:
1. Fujioka, M. and Nakatani, Y. Saccharopine dehydrogenase. Interaction with substrate analogues. Eur. J. Biochem. 25 (1972) 301-307. [PMID: 4339117]
2. Saunders, P.P. and Broquist, H.P. Saccharopine, an intermediate of the aminoadipic acid pathway of lysine biosynthesis. IV. Saccharopine dehydrogenase. J. Biol. Chem. 241 (1966) 3435-3440. [PMID: 4287986]
Accepted name: saccharopine dehydrogenase (NADP+, L-lysine-forming)
Reaction: N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O = L-lysine + 2-oxoglutarate + NADPH + H+
For diagram click here.
Glossary: L-saccharopine = N6-(L-1,3-dicarboxypropyl)-L-lysine
Other name(s): lysine-2-oxoglutarate reductase; lysine-ketoglutarate reductase; L-lysine-α-ketoglutarate reductase; lysine:α-ketoglutarate:TPNH oxidoreductase (ε-N-[glutaryl-2]-L-lysine forming); saccharopine (nicotinamide adenine dinucleotide phosphate, lysine-forming) dehydrogenase
Systematic name: N6-(L-1,3-dicarboxypropyl)-L-lysine:NADP+ oxidoreductase (L-lysine-forming)
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9031-19-0
References:
1. Hutzler, J. and Dancis, J. Conversion of lysine to saccharopine by human tissues. Biochim. Biophys. Acta 158 (1968) 62-69. [PMID: 4385118]
2. Markovitz, P.J., Chuang, D.T. and Cox, R.P. Familial hyperlysinemias. Purification and characterization of the bifunctional aminoadipic semialdehyde synthase with lysine-ketoglutarate reductase and saccharopine dehydrogenase activities. J. Biol. Chem. 259 (1984) 11643-11646. [PMID: 6434529]
Accepted name: saccharopine dehydrogenase (NAD+, L-glutamate-forming)
Reaction: N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O = L-glutamate + (S)-2-amino-6-oxohexanoate + NADH + H+
For diagram click here.
Glossary: L-saccharopine = N6-(L-1,3-dicarboxypropyl)-L-lysine
(S)-2-amino-6-oxohexanoate = L-2-aminoadipate 6-semialdehyde = L-allysine
Other name(s): dehydrogenase, saccharopine (nicotinamide adenine dinucleotide, glutamate-forming); saccharopin dehydrogenase; NAD+ oxidoreductase (L-2-aminoadipic-δ-semialdehyde and glutamate forming); aminoadipic semialdehyde synthase; saccharopine dehydrogenase (NAD, L-glutamate-forming)
Systematic name: N6-(L-1,3-dicarboxypropyl)-L-lysine:NAD+ oxidoreductase (L-glutamate-forming)
(b>Comments: The activities of this enzyme along with EC 1.5.1.8, saccharopine dehydrogenase (NADP+, L-lysine-forming), occur on a single protein.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37256-26-1
References:
1. Hutzler, J. and Dancis, J. Conversion of lysine to saccharopine by human tissues. Biochim. Biophys. Acta 158 (1968) 62-69. [PMID: 4385118]
2. Markovitz, P.J., Chuang, D.T. and Cox, R.P. Familial hyperlysinemias. Purification and characterization of the bifunctional aminoadipic semialdehyde synthase with lysine-ketoglutarate reductase and saccharopine dehydrogenase activities. J. Biol. Chem. 259 (1984) 11643-11646. [PMID: 6434529]
Accepted name: saccharopine dehydrogenase (NADP+, L-glutamate-forming)
Reaction: N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O = L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+
For diagram click here, another example.
Glossary: L-saccharopine = N6-(L-1,3-dicarboxypropyl)-L-lysine
(S)-2-amino-6-oxohexanoate = L-2-aminoadipate 6-semialdehyde = L-allysine
Other name(s): saccharopine (nicotinamide adenine dinucleotide phosphate, glutamate-forming) dehydrogenase; aminoadipic semialdehyde-glutamic reductase; aminoadipate semialdehyde-glutamate reductase; aminoadipic semialdehyde-glutamate reductase; ε-N-(L-glutaryl-2)-L-lysine:NAD+(P) oxidoreductase (L-2-aminoadipate-semialdehyde forming); saccharopine reductase
Systematic name: N6-(L-1,3-dicarboxypropyl)-L-lysine:NADP+ oxidoreductase (L-glutamate-forming)
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9033-55-0
References:
1. Jones, E.E. and Broquist, H.P. Saccharopine, an intermediate of the aminoadipic acid pathway of lysine biosynthesis. 3. Aminoadipic semialdehyde-glutamate reductase. J. Biol. Chem. 241 (1966) 3430-3434. [PMID: 4380448]
Accepted name: D-octopine dehydrogenase
Reaction: N2-(D-1-carboxyethyl)-L-arginine + NAD+ + H2O = L-arginine + pyruvate + NADH + H+
Other name(s): D-octopine synthase; octopine dehydrogenase; octopine:NAD oxidoreductase; ODH
Systematic name: N2-(D-1-carboxyethyl)-L-arginine:NAD+ oxidoreductase (L-arginine-forming)
Comments: In the reverse direction, acts also on L-ornithine, L-lysine and L-histidine.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 37256-27-2
References:
1. Kemp, J.D., Hack, E., Sutton, D.W. and El-Wakil, M. Unusual amino acids and their relationship to tumorigenesis. Proc. Int. Conf. Plant Pathol. Bact. 4th, (1979) 183-188.
2. van Thoai, N., Huc, C., Pho, D.B. and Olomucki, A. Octopine déhydrogénase. Purification et propriétés catalytiques. Biochim. Biophys. Acta 191 (1969) 46-57. [PMID: 4310628]
[EC 1.5.1.12 Transferred entry: 1-pyrroline-5-carboxylate dehydrogenase. Now EC 1.2.1.88, L-glutamate γ-semialdehyde dehydrogenase. (EC 1.5.1.12 created 1972, modified 2008, deleted 2013)]
[EC 1.5.1.13 Transferred entry: now EC 1.17.1.5, nicotinate dehydrogenase. The enzyme was incorrectly classified as acting on a CH-NH group. (EC 1.5.1.13 created 1972, deleted 2004)].
[EC 1.5.1.14 Deleted entry: 1,2-didehydropipecolate reductase. Now included with EC 1.5.1.21 δ1-piperideine-2-carboxylate reductase (EC 1.5.1.14 created 1976, deleted 1989)]
Accepted name: methylenetetrahydrofolate dehydrogenase (NAD+)
Reaction: 5,10-methylenetetrahydrofolate + NAD+ = 5,10-methenyltetrahydrofolate + NADH + H+
For diagram of reaction click here.
Other name(s): methylenetetrahydrofolate dehydrogenase (NAD)
Systematic name: 5,10-methylenetetrahydrofolate:NAD+ oxidoreductase
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 82062-90-6
References:
1. Moore, M.R., O'Brien, W.E. and Ljungdahl, L.G. Purification and characterization of nicotinamide adenine dinucleotide-dependent methylenetetrahydrofolate dehydrogenase from Clostridium formicoaceticum. J. Biol. Chem. 249 (1974) 5250-5253. [PMID: 4153026]
Accepted name: D-lysopine dehydrogenase
Reaction: N2-(D-1-carboxyethyl)-L-lysine + NADP+ + H2O = L-lysine + pyruvate + NADPH + H+
Other name(s): D-lysopine synthase; lysopine dehydrogenase; D(+)-lysopine dehydrogenase
Systematic name: N2-(D-1-carboxyethyl)-L-lysine:NADP+ oxidoreductase (L-lysine-forming)
Comments: In the reverse reaction, a number of L-amino acids can act instead of L-lysine, and 2-oxobutanoate and, to a lesser extent, glyoxylate can act instead of pyruvate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 65187-41-9
References:
1. Otten, L.A.B.M., Vreugdenhil, D. and Schilperoort, R.A. Properties of D(+)-lysopine dehydrogenase from crown gall tumour tissue. Biochim. Biophys. Acta 485 (1977) 268-277. [PMID: 21695]
Accepted name: alanopine dehydrogenase
Reaction: 2,2'-iminodipropanoate + NAD+ + H2O = L-alanine + pyruvate + NADH + H+
Other name(s): ALPDH ; alanopine[meso-N-(1-carboxyethyl)-alanine]dehydrogenase; meso-N-(1-carboxyethyl)-alanine:NAD+ oxidoreductase; alanopine: NAD oxidoreductase; ADH (ambiguous); alanopine:NAD oxidoreductase
Systematic name: 2,2'-iminodipropanoate:NAD+ oxidoreductase (L-alanine-forming)
Comments: In the reverse reaction, L-alanine can be replaced by L-cysteine, L-serine or L-threonine; glycine acts very slowly (cf. EC 1.5.1.22 strombine dehydrogenase).
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, CAS registry number: 71343-07-2
References:
1. Dando, P.R. Strombine [N-(carboxymethyl)-D-alanine] dehydrogenase and alanopine [meso-N-(1-carboxyethyl)-alanine dehydrogenase from the mussel Mytilus edulis L. Biochem. Soc. Trans. 9 (1981) 297-298.
2. Fields, J.H.A., Eng, A.K., Ramsden, W.D., Hochachka, P.W. and Weinstein, B. Alanopine and strombine are novel imino acids produced by a dehydrogenase found in the adductor muscle of the oyster, Crassostrea gigas. Arch. Biochem. Biophys. 201 (1980) 110-114. [PMID: 6156653]
3. Fields, J.H.A. and Hochachka, P.W. Purification and properties of alanopine dehydrogenase from the adductor muscle of the oyster, Crassostrea gigas (Mollusca, Bivalvia). Eur. J. Biochem. 114 (1981) 615-621. [PMID: 7238503]
Accepted name: ephedrine dehydrogenase
Reaction: (–)-ephedrine + NAD+ = (R)-2-methylimino-1-phenylpropan-1-ol + NADH + H+
Systematic name: (–)-ephedrine:NAD+ 2-oxidoreductase
Comments: The product immediately hydrolyses to methylamine and 1-hydroxy-1-phenylpropan-2-one. Acts on a number of related compounds including (–)-sympatol, (+)-pseudoephedrine and (+)-norephedrine.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 73508-06-2
References:
1. Klamann, E. and Lingens, F. Degradation of (–)-ephedrine by Pseudomonas putida. Detection of (–)-ephedrine: NAD+-oxidoreductase from Arthrobacter globiformis. Z. Naturforsch. C: Biosci. 35 (1980) 80-87. [PMID: 7405363]
Accepted name: D-nopaline dehydrogenase
Reaction: N2-(D-1,3-dicarboxypropyl)-L-arginine + NADP+ + H2O = L-arginine + 2-oxoglutarate + NADPH + H+
Other name(s): D-nopaline synthase; nopaline dehydrogenase; nopaline synthase; NOS
Systematic name: N2-(D-1,3-dicarboxypropyl)-L-arginine:NADP+ oxidoreductase (L-arginine-forming)
Comments: In the reverse direction, forms D-nopaline from L-arginine and D-ornaline from L-ornithine.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 64763-57-1
References:
1. Kemp, J.D., Sutton, D.W. and Hack, E. Purification and characterization of the crown gall specific enzyme nopaline synthase. Biochemistry 18 (1979) 3755-3760. [PMID: 476084]
Accepted name: methylenetetrahydrofolate reductase [NAD(P)H]
Reaction: 5-methyltetrahydrofolate + NAD(P)+ = 5,10-methylenetetrahydrofolate + NAD(P)H + H+
For diagram of reaction, click here or click here
Other name(s): MTHFR (gene name)
Systematic name: 5-methyltetrahydrofolate:NAD(P)+ oxidoreductase
Comments: A flavoprotein (FAD). The enzyme catalyses the reversible conversion of 5,10-methylenetetrahydrofolate to 5-methyltetrahydrofolate, playing an important role in folate metabolism by regulating the distribution of one-carbon moieties between cellular methylation reactions and nucleic acid synthesis. This enzyme, characterized from Protozoan parasites of the genus Leishmania, is unique among similar characterized eukaryotic enzymes in that it lacks the C-terminal allosteric regulatory domain (allowing it to catalyse a reversible reaction) and uses NADH and NADPH with equal efficiency under physiological conditions. cf. EC 1.5.1.53, methylenetetrahydrofolate reductase (NADPH); EC 1.5.1.54, methylenetetrahydrofolate reductase (NADH); and EC 1.5.7.1, methylenetetrahydrofolate reductase (ferredoxin).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 71822-25-8
References:
1. Vickers, T.J., Orsomando, G., de la Garza, R.D., Scott, D.A., Kang, S.O., Hanson, A.D. and Beverley, S.M. Biochemical and genetic analysis of methylenetetrahydrofolate reductase in Leishmania metabolism and virulence. J. Biol. Chem. 281 (2006) 38150-38158. [PMID: 17032644]
Accepted name: 1-piperideine-2-carboxylate/1-pyrroline-2-carboxylate reductase (NADPH)
Reaction: (1) L-pipecolate + NADP+ = 1-piperideine-2-carboxylate + NADPH + H+
(2) L-proline + NADP+ = 1-pyrroline-2-carboxylate + NADPH + H+
Glossary: 1-piperideine-2-carboxylate = 3,4,5,6-tetrahydropyridine-2-carboxylate
Other name(s): Pyr2C reductase; 1,2-didehydropipecolate reductase; P2C reductase; 1,2-didehydropipecolic reductase; DELTA1-piperideine-2-carboxylate/1-pyrroline-2-carboxylate reductase (ambiguous); L-pipecolate:NADP+ 2-oxidoreductase; DELTA1-piperideine-2-carboxylate reductase; Δ1-piperideine-2-carboxylate reductase
Systematic name: L-pipecolate/L-proline:NADP+ 2-oxidoreductase
Comments: The enzyme is involved in the catabolism of D-lysine and D-proline in bacteria that belong to the Pseudomonas genus. In contrast to EC 1.5.1.1, 1-piperideine-2-carboxylate/1-pyrroline-2-carboxylate reductase [NAD(P)H], which shows similar activity with NADPH and NADH, this enzyme is specific for NADPH.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 52037-88-4
References:
1. Payton, C.W. and Chang, Y.-F. Δ1-Piperideine-2-carboxylate reductase of Pseudomonas putida. J. Bacteriol. 149 (1982) 864-871. [PMID: 6801013]
2. Muramatsu, H., Mihara, H., Kakutani, R., Yasuda, M., Ueda, M., Kurihara, T. and Esaki, N. The putative malate/lactate dehydrogenase from Pseudomonas putida is an NADPH-dependent Δ1-piperideine-2-carboxylate/Δ1-pyrroline-2-carboxylate reductase involved in the catabolism of D-lysine and D-proline. J. Biol. Chem. 280 (2005) 5329-5335. [PMID: 15561717]
3. Watanabe, S., Tanimoto, Y., Yamauchi, S., Tozawa, Y., Sawayama, S. and Watanabe, Y. Identification and characterization of trans-3-hydroxy-L-proline dehydratase and Δ1-pyrroline-2-carboxylate reductase involved in trans-3-hydroxy-L-proline metabolism of bacteria. FEBS Open Bio 4 (2014) 240-250. [PMID: 24649405]
Accepted name: strombine dehydrogenase
Reaction: N-(carboxymethyl)-D-alanine + NAD+ + H2O = glycine + pyruvate + NADH + H+
Other name(s): strombine[N-(carboxymethyl)-D-alanine]dehydrogenase; N-(carboxymethyl)-D-alanine: NAD+ oxidoreductase
Systematic name: N-(carboxymethyl)-D-alanine:NAD+ oxidoreductase (glycine-forming)
Comments: Also catalyses the reaction of EC 1.5.1.17 alanopine dehydrogenase, but more slowly. Does not act on L-strombine.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 79393-84-3
References:
1. Dando, P.R. Strombine [N-(carboxymethyl)-D-alanine] dehydrogenase and alanopine [meso-N-(1-carboxyethyl)-alanine dehydrogenase from the mussel Mytilus edulis L. Biochem. Soc. Trans. 9 (1981) 297-298.
Accepted name: tauropine dehydrogenase
Reaction: tauropine + NAD+ + H2O = taurine + pyruvate + NADH + H+
Systematic name: N2-(D-1-carboxyethyl)taurine:NAD+ oxidoreductase (taurine-forming)
Comments: In the reverse reaction, alanine can act instead of taurine, but more slowly, and 2-oxobutanoate and 2-oxopentanoate can act instead of pyruvate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 104645-74-1
References:
1. Gäde, G. Purification and properties of tauropine dehydrogenase from the shell adductor muscle of the ormer, Haliotis lamellosa. Eur. J. Biochem. 160 (1986) 311-318. [PMID: 3769931]
Accepted name: N5-(carboxyethyl)ornithine synthase
Reaction: N5-(L-1-carboxyethyl)-L-ornithine + NADP+ + H2O = L-ornithine + pyruvate + NADPH + H+
Systematic name: N5-(L-1-carboxyethyl)-L-ornithine:NADP+ oxidoreductase (L-ornithine-forming)
Comments: In the reverse direction, L-lysine can act instead of L-ornithine, but more slowly. Acts on the amino group. cf. EC 1.5.1.16 D-lysopine dehydrogenase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 129070-70-8
References:
1. Thompson, J. N5-(L-1-Carboxyethyl)-L-ornithine:NADP+ oxidoreductase from Streptococcus lactis. Purification and partial characterization. J. Biol. Chem. 264 (1989) 9592-9601. [PMID: 2498334]
Accepted name: thiomorpholine-carboxylate dehydrogenase
Reaction: thiomorpholine 3-carboxylate + NAD(P)+ = 3,4-dehydro-thiomorpholine-3-carboxylate + NAD(P)H + H+
For diagram of reaction click here.
Other name(s): ketimine reductase; ketimine-reducing enzyme
Systematic name: thiomorpholine-3-carboxylate:NAD(P)+ 5,6-oxidoreductase
Comments: The product is the cyclic imine of the 2-oxoacid corresponding to S-(2-aminoethyl)cysteine. In the reverse direction, a number of other cyclic unsaturated compounds can act as substrates, but more slowly.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 115232-54-7
References:
1. Nardini, M., Ricci, G., Caccuri, A.M., Solinas, S.P., Vesci, L. and Cavallini, D. Purification and characterization of a ketimine-reducing enzyme. Eur. J. Biochem. 173 (1988) 689-694. [PMID: 3371353]
Accepted name: β-alanopine dehydrogenase
Reaction: β-alanopine + NAD+ + H2O = β-alanine + pyruvate + NADH + H+
Systematic name: N-(D-1-carboxyethyl)-β-alanine:NAD+ oxidoreductase (β-alanine-forming)
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 113573-64-1
References:
1. Sato, M., Takahara, M., Kanno, N., Sato, Y. and Ellington, W.R. Isolation of a new opine, β-alanopine, from the extracts of the muscle of the marine bivalve mollusc Scapharca broughtonii. Comp. Biochem. Physiol. 88B (1987) 803-806.
Accepted name: 1,2-dehydroreticulinium reductase (NADPH)
Reaction: (R)-reticuline + NADP+ = 1,2-dehydroreticulinium + NADPH + H+
For diagram click here.
Other name(s): 1,2-dehydroreticulinium ion reductase
Systematic name: (R)-reticuline:NADP+ oxidoreductase
Comments: Reduces the 1,2-dehydroreticulinium ion to (R)-reticuline, which is a direct precursor of morphinan alkaloids in the poppy plant. The enzyme does not catalyse the reverse reaction to any significant extent under physiological conditions.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 130590-58-8
References:
1. De-Eknamkul, W. and Zenk, M.H. Purification and properties of 1,2-dehydroreticulinium reductase from Papaver somniferum seedlings. Phytochemistry 31 (1992) 813-821.
Accepted name: opine dehydrogenase
Reaction: (2S)-2-{[1-(R)-carboxyethyl]amino}pentanoate + NAD+ + H2O = L-2-aminopentanoic acid + pyruvate + NADH + H+
Other name(s): (2S)-2-{[1-(R)-carboxyethyl]amino}pentanoate dehydrogenase (NAD+, L-aminopentanoate-forming)
Systematic name: (2S)-2-{[1-(R)-carboxyethyl]amino}pentanoate:NAD+ oxidoreductase (L-aminopentanoate-forming)
Comments: in the forward direction, the enzyme from Arthrobacter sp. acts also on secondary amine dicarboxylates such as N-(1-carboxyethyl)methionine and N-(1-carboxyethyl)phenylalanine. Dehydrogenation forms an imine, which dissociates to the amino acid and pyruvate. In the reverse direction, the enzyme acts also on neutral amino acids as an amino donor. They include L-amino acids such as 2-aminopentanoic acid, 2-aminobutyric acid, 2-aminohexanoic acid, 3-chloroalanine, O-acetylserine, methionine, isoleucine, valine, phenylalanine, leucine and alanine. The amino acceptors include 2-oxoacids such as pyruvate, oxaloacetate, glyoxylate and 2-oxobutyrate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 108281-02-3
References:
1. Asano, Y., Yamaguchi, K. and Kondo, K. A new NAD+-dependent opine dehydrogenase from Arthrobacter sp. strain 1C. J. Bacteriol. 171 (1989) 4466-4471. [PMID: 2753861]
2. Dairi, T. and Asano, Y. Cloning, nucleotide sequencing, and expression of an opine dehydrogenase gene from Arthrobacter sp. strain 1C. Appl. Environ. Microbiol. 61 (1995) 3169-3171. [PMID: 7487048]
3. Kato, Y., Yamada, H. and Asano, Y. Stereoselective synthesis of opine-type secondary amine carboxylic acids by a new enzyme opine dehydrogenase. Use of recombinant enzymes. J. Mol. Catal., B Enzym. 1 (1996) 151-160.
[EC 1.5.1.29 Deleted entry: FMN reductase [NAD(P)H]. Now covered by EC 1.5.1.38 [FMN reductase (NADPH)], EC 1.5.1.39 [FMN reductase [NAD(P)H])] and EC 1.5.1.41 (riboflavin reductase [NAD(P)H]) (EC 1.5.1.29 created 1981 as EC 1.6.8.1, transferred 2002 to EC 1.5.1.29, modified 2002, deleted 2011)]
Accepted name: flavin reductase (NADPH)
Reaction: reduced riboflavin + NADP+ = riboflavin + NADPH + H+
Other name(s): NADPH:flavin oxidoreductase; riboflavin mononucleotide (reduced nicotinamide adenine dinucleotide phosphate) reductase; flavin mononucleotide reductase; flavine mononucleotide reductase; FMN reductase (NADPH); NADPH-dependent FMN reductase; NADPH-flavin reductase; NADPH-FMN reductase; NADPH-specific FMN reductase; riboflavin mononucleotide reductase; riboflavine mononucleotide reductase; NADPH2 dehydrogenase (flavin); NADPH2:riboflavin oxidoreductase
Systematic name: reduced-riboflavin:NADP+ oxidoreductase
Comments: The enzyme from Entamoeba histolytica reduces riboflavin and galactoflavin, and, more slowly, FMN and FAD. NADH is oxidized more slowly than NADPH.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 56626-29-0
References:
1. Lo, H.-S. and Reeves, R.E. Purification and properties of NADPH:flavin oxidoreductase from Entamoeba histolytica. Mol. Biochem. Parasitol. 2 (1980) 23-30. [PMID: 6258069]
2. Yubisui, T., Tamura, M. and Takeshita, M. Characterization of a second form of NADPH-flavin reductase purified from human erythrocytes. Biochem. Int. 15 (1987) 1-8. [PMID: 3453680]
Accepted name: berberine reductase
Reaction: (R)-canadine + 2 NADP+ = berberine + 2 NADPH + H+
For diagram click here.
Other name(s): (R)-canadine synthase
Systematic name: (R)-tetrahydroberberine:NADP+ oxidoreductase
Comments: Involved in alkaloid biosynthesis in Corydalis cava to give (R)-canadine with the opposite configuration to the precursor of berberine (see EC 1.3.3.8 tetrahydroberberine oxidase). Also acts on 7,8-dihydroberberine.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Bauer, W. and Zenk, M.H. Formation of (R)-configurated tetrahydroprotoberberine alkaloids in vivo and in vitro. Tetrahedron Lett. 32 (1991) 487-490.
Accepted name: vomilenine reductase
Reaction: (2R)-1,2-dihydrovomilenine + NADP+ = vomilenine + NADPH + H+
For diagram of reaction, click here
Other name(s): VR (gene name); 1,2-dihydrovomilenine:NADP+ oxidoreductase
Systematic name: (2R)-1,2-dihydrovomilenine:NADP+ oxidoreductase
Comments: The enzyme, characterized from the plant Rauvolfia serpentina, participates in the ajmaline biosynthesis pathway.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 462127-03-3
References:
1. von Schumann, G., Gao, S. and Stöckigt, J. Vomilenine reductase - a novel enzyme catalyzing a crucial step in the biosynthesis of the therapeutically applied antiarrhythmic alkaloid ajmaline. J. Bioorg. Med. Chem. 10 (2002) 1913-1918. [PMID: 11937349]
2. Guo, J., Gao, D., Lian, J. and Qu, Y. De novo biosynthesis of antiarrhythmic alkaloid ajmaline. Nat. Commun. 15 (2024) 457. [PMID: 38212296]
Accepted name: pteridine reductase
Reaction: 5,6,7,8-tetrahydrobiopterin + 2 NADP+ = biopterin + 2 NADPH + 2 H+
Other name(s): PTR1; pteridine reductase 1
Systematic name: 5,6,7,8-tetrahydrobiopterin:NADP+ oxidoreductase
Comments: The enzyme from Leishmania (both amastigote and promastigote forms) catalyses the reduction by NADPH of folate and a wide variety of unconjugated pterins, including biopterin, to their tetrahydro forms. It also catalyses the reduction of 7,8-dihydropterins and 7,8-dihydrofolate to their tetrahydro forms. In contrast to EC 1.5.1.3 (dihydrofolate reductase) and EC 1.5.1.34 (6,7-dihydropteridine reductase), pteridine reductase will not catalyse the reduction of the quinonoid form of dihydrobiopterin. The enzyme is specific for NADPH; no activity has been detected with NADH. It also differs from EC 1.5.1.3 (dihydrofolate reductase) in being specific for the B side of NADPH.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 131384-61-7
References:
1. Nare, B., Hardy, L. and Beverley, S.M. The roles of pteridine reductase 1 and dihydrofolate reductase-thymidylate synthase in pteridine metabolism in the protozoan parasite Leishmania major. J. Biol. Chem. 272 (1997) 13883-13891. [PMID: 9153248]
2. Gourley, D.G., Schüttelkopf, A.W., Leonard, G.A., Luba, J., Hardy, L.W., Beverley, S.M. and Hunter, W.N. Pteridine reductase mechanism correlates pterin metabolism with drug resistance in trypanosomatid parasites. Nat. Struct. Biol. 8 (2001) 521-525. [PMID: 11373620]
3. Fitzpatrick, P.F. The aromatic amino acid hydroxylases. Adv. Enzymol. Relat. Areas Mol. Biol. 74 (2000) 235-294. [PMID: 10800597]
Accepted name: 6,7-dihydropteridine reductase
Reaction: a 5,6,7,8-tetrahydropteridine + NAD(P)+ = a 6,7-dihydropteridine + NAD(P)H + H+
For diagram click here.
Other name(s): 6,7-dihydropteridine:NAD(P)H oxidoreductase; DHPR; NAD(P)H2:6,7-dihydropteridine oxidoreductase; NADH-dihydropteridine reductase; NADPH-dihydropteridine reductase; NADPH-specific dihydropteridine reductase; dihydropteridine (reduced nicotinamide adenine dinucleotide) reductase; dihydropteridine reductase; dihydropteridine reductase (NADH); 5,6,7,8-tetrahydropteridine:NAD(P)H+ oxidoreductase
Systematic name: 5,6,7,8-tetrahydropteridine:NAD(P)+ oxidoreductase
Comments: The substrate is the quinonoid form of dihydropteridine. Not identical with EC 1.5.1.3 dihydrofolate reductase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9074-11-7
References:
1. Harano, T. New diaphorases from Bombyx silkworm eggs. NADH/NADPH cytochrome c reductase activity mediated with 6,7-dimethyltetrahydropterin. Insect Biochem. 2 (1972) 385-399.
2. Hasegawa, H. Dihydropteridine reductase from bovine liver. Purification, crystallization, and isolation of a binary complex with NADH. J. Biochem. (Tokyo) 81 (1977) 169-177. [PMID: 191436]
3. Kaufman, S. Phenylalanine hydroxylase. Methods Enzymol. 5 (1962) 809-816.
4. Lind, K.E. Dihydropteridine reductase. Investigation of the specificity for quinoid dihydropteridine and the inhibition by 2,4-diaminopteridines. Eur. J. Biochem. 25 (1972) 560-562. [PMID: 4402916]
5. Nakanishi, N., Hasegawa, H. and Watabe, S. A new enzyme, NADPH-dihydropteridine reductase in bovine liver. J. Biochem. (Tokyo) 81 (1977) 681-685. [PMID: 16875]
[EC 1.5.1.35 Deleted entry: 1-pyrroline dehydrogenase. The enzyme is identical to EC 1.2.1.19, aminobutyraldehyde dehydrogenase, as the substrates 1-pyrroline and 4-aminobutanal are interconvertible. (EC 1.5.1.35 created 2006, deleted 2007)]
Accepted name: flavin reductase (NADH)
Reaction: reduced flavin + NAD+ = flavin + NADH + H+
Other name(s): NADH-dependent flavin reductase; flavin:NADH oxidoreductase
Systematic name: flavin:NAD+ oxidoreductase
Comments: The enzyme from Escherichia coli W catalyses the reduction of free flavins by NADH. The enzyme has similar affinity to FAD, FMN and riboflavin. Activity with NADPH is more than 2 orders of magnitude lower than activity with NADH.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Galan, B., Diaz, E., Prieto, M.A. and Garcia, J.L. Functional analysis of the small component of the 4-hydroxyphenylacetate 3-monooxygenase of Escherichia coli W: a prototype of a new Flavin:NAD(P)H reductase subfamily. J. Bacteriol. 182 (2000) 627-636. [PMID: 10633095]
Accepted name: FAD reductase (NADH)
Reaction: FADH2 + NAD+ = FAD + NADH + H+
For diagram of reaction click here.
Other name(s): NADH-FAD reductase; NADH-dependent FAD reductase; NADH:FAD oxidoreductase; NADH:flavin adenine dinucleotide oxidoreductase
Systematic name: FADH2:NAD+ oxidoreductase
Comments: The enzyme from Burkholderia phenoliruptrix can reduce either FAD or flavin mononucleotide (FMN) but prefers FAD. Unlike EC 1.5.1.36, flavin reductase (NADH), the enzyme can not reduce riboflavin. The enzyme does not use NADPH as acceptor.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Gisi, M.R. and Xun, L. Characterization of chlorophenol 4-monooxygenase (TftD) and NADH:flavin adenine dinucleotide oxidoreductase (TftC) of Burkholderia cepacia AC1100. J. Bacteriol. 185 (2003) 2786-2792. [PMID: 12700257]
Accepted name: FMN reductase (NADPH)
Reaction: FMNH2 + NADP+ = FMN + NADPH + H+
For diagram of reaction click here.
Other name(s): FRP; flavin reductase P; SsuE
Systematic name: FMNH2:NADP+ oxidoreductase
Comments: The enzymes from bioluminescent bacteria contain FMN [4], while the enzyme from Escherichia coli does not [8]. The enzyme often forms a two-component system with monooxygenases such as luciferase. Unlike EC 1.5.1.39, this enzyme does not use NADH as acceptor [1,2]. While FMN is the preferred substrate, the enzyme can also use FAD and riboflavin with lower activity [3,6,8].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Gerlo, E. and Charlier, J. Identification of NADH-specific and NADPH-specific FMN reductases in Beneckea harveyi. Eur. J. Biochem. 57 (1975) 461-467. [PMID: 1175652]
2. Jablonski, E. and DeLuca, M. Purification and properties of the NADH and NADPH specific FMN oxidoreductases from Beneckea harveyi. Biochemistry 16 (1977) 2932-2936. [PMID: 880288]
3. Jablonski, E. and DeLuca, M. Studies of the control of luminescence in Beneckea harveyi: properties of the NADH and NADPH:FMN oxidoreductases. Biochemistry 17 (1978) 672-678. [PMID: 23827]
4. Lei, B., Liu, M., Huang, S. and Tu, S.C. Vibrio harveyi NADPH-flavin oxidoreductase: cloning, sequencing and overexpression of the gene and purification and characterization of the cloned enzyme. J. Bacteriol. 176 (1994) 3552-3558. [PMID: 8206832]
5. Tanner, J.J., Lei, B., Tu, S.C. and Krause, K.L. Flavin reductase P: structure of a dimeric enzyme that reduces flavin. Biochemistry 35 (1996) 13531-13539. [PMID: 8885832]
6. Liu, M., Lei, B., Ding, Q., Lee, J.C. and Tu, S.C. Vibrio harveyi NADPH:FMN oxidoreductase: preparation and characterization of the apoenzyme and monomer-dimer equilibrium. Arch. Biochem. Biophys. 337 (1997) 89-95. [PMID: 8990272]
7. Lei, B. and Tu, S.C. Mechanism of reduced flavin transfer from Vibrio harveyi NADPH-FMN oxidoreductase to luciferase. Biochemistry 37 (1998) 14623-14629. [PMID: 9772191]
8. Eichhorn, E., van der Ploeg, J.R. and Leisinger, T. Characterization of a two-component alkanesulfonate monooxygenase from Escherichia coli. J. Biol. Chem. 274 (1999) 26639-26646. [PMID: 10480865]
Accepted name: FMN reductase [NAD(P)H]
Reaction: FMNH2 + NAD(P)+ = FMN + NAD(P)H + H+
For diagram of reaction click here.
Other name(s): FRG
Systematic name: FMNH2:NAD(P)+ oxidoreductase
Comments: Contains FMN. The enzyme can utilize NADH and NADPH with similar reaction rates. Different from , FMN reductase (NADH) and EC 1.5.1.38, FMN reductase (NADPH). The luminescent bacterium Vibrio harveyi possesses all three enzymes [1]. Also reduces riboflavin and FAD, but more slowly.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Watanabe, H. and Hastings, J.W. Specificities and properties of three reduced pyridine nucleotide-flavin mononucleotide reductases coupling to bacterial luciferase. Mol. Cell. Biochem. 44 (1982) 181-187. [PMID: 6981058]
Accepted name: 8-hydroxy-5-deazaflavin:NADPH oxidoreductase
Reaction: reduced coenzyme F420 + NADP+ = oxidized coenzyme F420 + NADPH + H+
For diagram of reaction click here.
Other name(s): 8-OH-5dFl:NADPH oxidoreductase
Systematic name: reduced coenzyme F420:NADP+ oxidoreductase
Comments: The enzyme has an absolute requirement for both the 5-deazaflavin structure and the presence of an 8-hydroxy group in the substrate [1].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Eker, A.P., Hessels, J.K. and Meerwaldt, R. Characterization of an 8-hydroxy-5-deazaflavin:NADPH oxidoreductase from Streptomyces griseus. Biochim. Biophys. Acta 990 (1989) 80-86. [PMID: 2492438]
Accepted name: riboflavin reductase [NAD(P)H]
Reaction: reduced riboflavin + NAD(P)+ = riboflavin + NAD(P)H + H+
For diagram of reaction click here.
Other name(s): NAD(P)H-FMN reductase (ambiguous); NAD(P)H-dependent FMN reductase (ambiguous); NAD(P)H:FMN oxidoreductase (ambiguous); NAD(P)H:flavin oxidoreductase (ambiguous); NAD(P)H2 dehydrogenase (FMN) (ambiguous); NAD(P)H2:FMN oxidoreductase (ambiguous); riboflavin mononucleotide reductase (ambiguous); flavine mononucleotide reductase (ambiguous); riboflavin mononucleotide (reduced nicotinamide adenine dinucleotide (phosphate)) reductase; flavin mononucleotide reductase (ambiguous); riboflavine mononucleotide reductase (ambiguous); Fre
Systematic name: riboflavin:NAD(P)+ oxidoreductase
Comments: Catalyses the reduction of soluble flavins by reduced pyridine nucleotides. Highest activity with riboflavin. When NADH is used as acceptor, the enzyme can also utilize FMN and FAD as substrates, with lower activity than riboflavin. When NADPH is used as acceptor, the enzyme has a very low activity with FMN and no activity with FAD [1].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Fontecave, M., Eliasson, R. and Reichard, P. NAD(P)H:flavin oxidoreductase of Escherichia coli. A ferric iron reductase participating in the generation of the free radical of ribonucleotide reductase. J. Biol. Chem. 262 (1987) 12325-12331. [PMID: 3305505]
2. Spyrou, G., Haggård-Ljungquist, E., Krook, M., Jörnvall, H., Nilsson, E. and Reichard, P. Characterization of the flavin reductase gene (fre) of Escherichia coli and construction of a plasmid for overproduction of the enzyme. J. Bacteriol. 173 (1991) 3673-3679. [PMID: 2050627]
3. Ingelman, M., Ramaswamy, S., Nivière, V., Fontecave, M. and Eklund, H. Crystal structure of NAD(P)H:flavin oxidoreductase from Escherichia coli. Biochemistry 38 (1999) 7040-7049. [PMID: 10353815]
Accepted name: FMN reductase (NADH)
Reaction: FMNH2 + NAD+ = FMN + NADH + H+
For diagram of reaction click here.
Other name(s): NADH-FMN reductase; NADH-dependent FMN reductase; NADH:FMN oxidoreductase; NADH:flavin oxidoreductase
Systematic name: FMNH2:NAD+ oxidoreductase
Comments: The enzyme often forms a two-component system with monooxygenases. Unlike EC 1.5.1.38, FMN reductase (NADPH), and EC 1.5.1.39, FMN reductase [NAD(P)H], this enzyme has a strong preference for NADH over NADPH, although some activity with the latter is observed [1,2]. While FMN is the preferred substrate, FAD can also be used with much lower activity [1,3].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Fontecave, M., Eliasson, R. and Reichard, P. NAD(P)H:flavin oxidoreductase of Escherichia coli. A ferric iron reductase participating in the generation of the free radical of ribonucleotide reductase. J. Biol. Chem. 262 (1987) 12325-12331. [PMID: 3305505]
2. Spyrou, G., Haggård-Ljungquist, E., Krook, M., Jörnvall, H., Nilsson, E. and Reichard, P. Characterization of the flavin reductase gene (fre) of Escherichia coli and construction of a plasmid for overproduction of the enzyme. J. Bacteriol. 173 (1991) 3673-3679. [PMID: 2050627]
3. Ingelman, M., Ramaswamy, S., Nivière, V., Fontecave, M. and Eklund, H. Crystal structure of NAD(P)H:flavin oxidoreductase from Escherichia coli. Biochemistry 38 (1999) 7040-7049. [PMID: 10353815]
Accepted name: carboxynorspermidine synthase
Reaction: (1) carboxynorspermidine + H2O + NADP+ = L-aspartate 4-semialdehyde + propane-1,3-diamine + NADPH + H+
(2) carboxyspermidine + H2O + NADP+ = L-aspartate 4-semialdehyde + putrescine + NADPH + H+
Other name(s): carboxynorspermidine dehydrogenase; carboxyspermidine dehydrogenase; CASDH; CANSDH; VC1624 (gene name)
Systematic name: carboxynorspermidine:NADP+ oxidoreductase
Comments: The reaction takes place in the opposite direction. Part of a bacterial polyamine biosynthesis pathway. L-aspartate 4-semialdehyde and propane-1,3-diamine/putrescine form a Schiff base that is reduced to form carboxynorspermidine/carboxyspermidine, respectively [1]. The enzyme from the bacterium Vibrio cholerae is essential for biofilm formation [2]. The enzyme from Campylobacter jejuni only produces carboxyspermidine in vivo even though it also can produce carboxynorspermidine in vitro [3].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Nakao, H., Shinoda, S. and Yamamoto, S. Purification and some properties of carboxynorspermidine synthase participating in a novel biosynthetic pathway for norspermidine in Vibrio alginolyticus. J. Gen. Microbiol. 137 (1991) 1737-1742. [PMID: 1955861]
2. Lee, J., Sperandio, V., Frantz, D.E., Longgood, J., Camilli, A., Phillips, M.A. and Michael, A.J. An alternative polyamine biosynthetic pathway is widespread in bacteria and essential for biofilm formation in Vibrio cholerae. J. Biol. Chem. 284 (2009) 9899-9907. [PMID: 19196710]
3. Hanfrey, C.C., Pearson, B.M., Hazeldine, S., Lee, J., Gaskin, D.J., Woster, P.M., Phillips, M.A. and Michael, A.J. Alternative spermidine biosynthetic route is critical for growth of Campylobacter jejuni and is the dominant polyamine pathway in human gut microbiota. J. Biol. Chem. 286 (2011) 43301-43312. [PMID: 22025614]
Accepted name: festuclavine dehydrogenase
Reaction: festuclavine + NAD+ = 6,8-dimethyl-6,7-didehydroergoline + NADH + H+
For diagram of reaction click here.
Glossary: festuclavine = 6,8β-dimethylergoline
Other name(s): FgaFS; festuclavine synthase
Systematic name: festuclavine:NAD+ oxidoreductase
Comments: The enzyme participates in the biosynthesis of fumigaclavine C, an ergot alkaloid produced by some fungi of the Trichocomaceae family. The reaction proceeds in vivo in the opposite direction to the one shown here.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Wallwey, C., Matuschek, M., Xie, X.L. and Li, S.M. Ergot alkaloid biosynthesis in Aspergillus fumigatus: Conversion of chanoclavine-I aldehyde to festuclavine by the festuclavine synthase FgaFS in the presence of the old yellow enzyme FgaOx3. Org. Biomol. Chem. 8 (2010) 3500-3508. [PMID: 20526482]
Accepted name: FAD reductase [NAD(P)H]
Reaction: FADH2 + NAD(P)+ = FAD + NAD(P)H + H+
For diagram of reaction click here.
Other name(s): GTNG_3158 (gene name)
Systematic name: FADH2:NAD(P)+ oxidoreductase
Comments: This enzyme, isolated from the bacterium Geobacillus thermodenitrificans, participates in the pathway of tryptophan degradation. The enzyme is part of a system that also includes a bifunctional riboflavin kinase/FMN adenylyltransferase and EC 1.14.14.8, anthranilate 3-monooxygenase (FAD). It can reduce either FAD or flavin mononucleotide (FMN) but prefers FAD. The enzyme has a slight preference for NADPH as acceptor. cf. EC 1.5.1.37, FAD reductase (NADH).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Liu, X., Dong, Y., Li, X., Ren, Y., Li, Y., Wang, W., Wang, L. and Feng, L. Characterization of the anthranilate degradation pathway in Geobacillus thermodenitrificans NG80-2. Microbiology 156 (2010) 589-595. [PMID: 19942660]
Accepted name: agroclavine dehydrogenase
Reaction: agroclavine + NADP+ = 6,8-dimethyl-6,7,8,9-tetradehydroergoline + NADPH + H+
For diagram of reaction click here.
Glossary: agroclavine = 6,8-dimethyl-8,9-didehydroergoline
Other name(s): easG (gene name)
Systematic name: agroclavine:NADP+ oxidoreductase
Comments: The enzyme participates in the biosynthesis of ergotamine, an ergot alkaloid produced by some fungi of the Clavicipitaceae family. The reaction is catalysed in the opposite direction to that shown. The substrate for the enzyme is an iminium intermediate that is formed spontaneously from chanoclavine-I aldehyde in the presence of glutathione.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Matuschek, M., Wallwey, C., Xie, X. and Li, S.M. New insights into ergot alkaloid biosynthesis in Claviceps purpurea: an agroclavine synthase EasG catalyses, via a non-enzymatic adduct with reduced glutathione, the conversion of chanoclavine-I aldehyde to agroclavine. Org. Biomol. Chem. 9 (2011) 4328-4335. [PMID: 21494745]
Accepted name: dihydromethanopterin reductase [NAD(P)+]
Reaction: 5,6,7,8-tetrahydromethanopterin + NAD(P)+ = 7,8-dihydromethanopterin + NAD(P)H + H+
For diagram of reaction click here.
Other name(s): DmrA; H2MPT reductase; 5,6,7,8-tetrahydromethanopterin 5,6-oxidoreductase; dihydromethanopterin reductase
Systematic name: 5,6,7,8-tetrahydromethanopterin:NAD(P)+ 5,6-oxidoreductase
Comments: The enzyme, characterized from the bacterium Methylobacterium extorquens, is involved in biosynthesis of dephospho-tetrahydromethanopterin. The specific activity with NADH is 15% of that with NADPH at the same concentration [1]. It does not reduce 7,8-dihydrofolate (cf. EC 1.5.1.3, dihydrofolate reductase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Caccamo, M.A., Malone, C.S. and Rasche, M.E. Biochemical characterization of a dihydromethanopterin reductase involved in tetrahydromethanopterin biosynthesis in Methylobacterium extorquens AM1. J. Bacteriol. 186 (2004) 2068-2073. [PMID: 15028691]
Accepted name: 2-methyl-1-pyrroline reductase
Reaction: (R)-2-methylpyrrolidine + NADP+ = 2-methyl-1-pyrroline + NADPH + H+
Other name(s): (R)-imine reductase (ambiguous)
Systematic name: (R)-2-methylpyrrolidine:NADP+ 2-oxidoreductase
Comments: The enzyme from the bacterium Streptomyces sp. GF3587 is highly specific for its substrate and forms only the (R) isomer.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Mitsukura, K., Suzuki, M., Shinoda, S., Kuramoto, T., Yoshida, T. and Nagasawa, T. Purification and characterization of a novel (R)-imine reductase from Streptomyces sp. GF3587. Biosci. Biotechnol. Biochem. 75 (2011) 1778-1782. [PMID: 21897027]
Accepted name: 1-pyrroline-2-carboxylate reductase [NAD(P)H]
Reaction: L-proline + NAD(P)+ = 1-pyrroline-2-carboxylate + NAD(P)H + H+
Systematic name: L-proline:NAD(P)+ 2-oxidoreductase
Comments: The enzyme from the bacterium Colwellia psychrerythraea is involved in trans-3-hydroxy-L-proline metabolism. In contrast to EC 1.5.1.1, 1-piperideine-2-carboxylate/1-pyrroline-2-carboxylate reductase [NAD(P)H], which shows similar activity with 1-piperideine-2-carboxylate and 1-pyrroline-2-carboxylate, this enzyme is specific for the latter. While the enzyme is active with both NADH and NADPH, activity is higher with NADPH.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Watanabe, S., Tanimoto, Y., Yamauchi, S., Tozawa, Y., Sawayama, S. and Watanabe, Y. Identification and characterization of trans-3-hydroxy-L-proline dehydratase and Δ1-pyrroline-2-carboxylate reductase involved in trans-3-hydroxy-L-proline metabolism of bacteria. FEBS Open Bio 4 (2014) 240-250. [PMID: 24649405]
Accepted name: dihydromonapterin reductase
Reaction: 5,6,7,8-tetrahydromonapterin + NADP+ = 7,8-dihydromonapterin + NADPH + H+
Glossary: 7,8-dihydromonapterin = 2-amino-6-[(1S,2S)-1,2,3-trihydroxypropyl]-7,8-dihydropteridin-4(3H)-one
Other name(s): FolM; H2-MPt reductase
Systematic name: 5,6,7,8-tetrahydromonapterin:NADP+ oxidoreductase
Comments: The enzyme, found in many Gram negative bacteria, also slowly reduces 7,8-dihydrofolate to 5,6,7,8-tetrahydrofolate (cf. EC 1.5.1.3, dihydrofolate reductase). The enzyme has no activity with NADH.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Pribat, A., Blaby, I.K., Lara-Nunez, A., Gregory, J.F., 3rd, de Crecy-Lagard, V. and Hanson, A.D. FolX and FolM are essential for tetrahydromonapterin synthesis in Escherichia coli and Pseudomonas aeruginosa. J. Bacteriol. 192 (2010) 475-482. [PMID: 19897652]
Accepted name: N-[(2S)-2-amino-2-carboxyethyl]-L-glutamate dehydrogenase
Reaction: N-[(2S)-2-amino-2-carboxyethyl]-L-glutamate + NAD+ + H2O = 2-oxoglutarate + L-2,3-diaminopropanoate + NADH + H+
Other name(s): SbnB
Systematic name: N-[(2S)-2-amino-2-carboxyethyl]-L-glutamate:NAD+ dehydrogenase (L-2,3-diaminopropanoate-forming)
Comments: The enzyme, characterized from the bacterium Staphylococcus aureus, is involved in the biosynthesis of the siderophore staphyloferrin B.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Beasley, F.C., Cheung, J. and Heinrichs, D.E. Mutation of L-2,3-diaminopropionic acid synthase genes blocks staphyloferrin B synthesis in Staphylococcus aureus. BMC Microbiol. 11 (2011) 199. [PMID: 21906287]
2. Kobylarz, M.J., Grigg, J.C., Takayama, S.J., Rai, D.K., Heinrichs, D.E. and Murphy, M.E. Synthesis of L-2,3-diaminopropionic acid, a siderophore and antibiotic precursor. Chem. Biol. 21 (2014) 379-388. [PMID: 24485762]
Accepted name: staphylopine dehydrogenase
Reaction: staphylopine + NADP+ + H2O = (2S)-2-amino-4-{[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino}butanoate + pyruvate + NADPH + H+
For diagram of reaction click here.
Glossary: staphylopine = (2S)-4-{[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino}-2-[(1-carboxyethyl)amino]butanoate
Other name(s): cntM (gene name); staphylopine synthase
Systematic name: staphylopine:NADP+ oxidoreductase [(2S)-2-amino-4-{[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino}butanoate]-forming
Comments: The enzyme, characterized from the bacterium Staphylococcus aureus, catalyses the last reaction in the biosynthesis of the metallophore staphylopine, which is involved in the acquisition of nickel, copper, and cobalt.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Ghssein, G., Brutesco, C., Ouerdane, L., Fojcik, C., Izaute, A., Wang, S., Hajjar, C., Lobinski, R., Lemaire, D., Richaud, P., Voulhoux, R., Espaillat, A., Cava, F., Pignol, D., Borezee-Durant, E. and Arnoux, P. Biosynthesis of a broad-spectrum nicotianamine-like metallophore in Staphylococcus aureus. Science 352 (2016) 1105-1109. [PMID: 27230378]
2. McFarlane, J.S., Davis, C.L. and Lamb, A.L. Staphylopine, pseudopaline, and yersinopine dehydrogenases: A structural and kinetic analysis of a new functional class of opine dehydrogenase. J. Biol. Chem 293 (2018) 8009-8019. [PMID: 29618515]
Accepted name: methylenetetrahydrofolate reductase (NADPH)
Reaction: 5-methyltetrahydrofolate + NADP+ = 5,10-methylenetetrahydrofolate + NADPH + H+
For diagram of reaction, click here and for its place in C1 metabolism, click here
Other name(s): MTHFR (gene name); methylenetetrahydrofolate (reduced nicotinamide adenine dinucleotide phosphate) reductase; 5,10-methylenetetrahydrofolate reductase (NADPH); 5,10-methylenetetrahydrofolic acid reductase (ambiguous); 5,10-CH2-H4folate reductase (ambiguous); methylenetetrahydrofolate reductase (NADPH2); 5,10-methylenetetrahydrofolate reductase (ambiguous); methylenetetrahydrofolate reductase (ambiguous); N5,10-methylenetetrahydrofolate reductase (ambiguous); 5,10-methylenetetrahydropteroylglutamate reductase (ambiguous); N5,N10-methylenetetrahydrofolate reductase (ambiguous); methylenetetrahydrofolic acid reductase (ambiguous); 5-methyltetrahydrofolate:(acceptor) oxidoreductase (incorrect); 5,10-methylenetetrahydrofolate reductase (FADH2) (ambiguous)
Systematic name: 5-methyltetrahydrofolate:NADP+ oxidoreductase
Comments: A flavoprotein (FAD). The enzyme from yeast and mammals catalyses a physiologically irreversible reduction of 5,10-methylenetetrahydrofolate to 5-methyltetrahydrofolate using NADPH as the electron donor. It plays an important role in folate metabolism by regulating the distribution of one-carbon moieties between cellular methylation reactions and nucleic acid synthesis. The enzyme contains an N-terminal catalytic domain and a C-terminal allosteric regulatory domain that binds S-adenosyl-L-methionine, which acts as an inhibitor. cf. EC 1.5.1.54, methylenetetrahydrofolate reductase (NADH); EC 1.5.1.20, methylenetetrahydrofolate reductase [NAD(P)H]; and EC 1.5.7.1, methylenetetrahydrofolate reductase (ferredoxin).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Donaldson, K.O. and Keresztesy, J.C. Naturally occurring forms of folic acid. I. J. Biol. Chem. 234 (1959) 3235-3240. [PMID: 13817476]
2. Kutzbach, C. and Stokstad, E.L.R. Mammalian methylenetetrahydrofolate reductase. Partial purification, properties, and inhibition by S-adenosylmethionine. Biochim. Biophys. Acta 250 (1971) 459-477. [PMID: 4399897]
3. Daubner, S.C. and Matthews, R.T. Purification and properties of methylenetetrahydrofolate reductase from pig liver. J. Biol. Chem. 257 (1982) 140-145. [PMID: 6975779]
4. Zhou, J., Kang, S.S., Wong, P.W., Fournier, B. and Rozen, R. Purification and characterization of methylenetetrahydrofolate reductase from human cadaver liver. Biochem Med Metab Biol 43 (1990) 234-242. [PMID: 2383427]
5. Roje, S., Chan, S.Y., Kaplan, F., Raymond, R.K., Horne, D.W., Appling, D.R. and Hanson, A.D. Metabolic engineering in yeast demonstrates that S-adenosylmethionine controls flux through the methylenetetrahydrofolate reductase reaction in vivo. J. Biol. Chem. 277 (2002) 4056-4061. [PMID: 11729203]
6. Froese, D.S., Kopec, J., Rembeza, E., Bezerra, G.A., Oberholzer, A.E., Suormala, T., Lutz, S., Chalk, R., Borkowska, O., Baumgartner, M.R. and Yue, W.W. Structural basis for the regulation of human 5,10-methylenetetrahydrofolate reductase by phosphorylation and S-adenosylmethionine inhibition. Nat. Commun. 9 (2018) 2261. [PMID: 29891918]
Accepted name: methylenetetrahydrofolate reductase (NADH)
Reaction: 5-methyltetrahydrofolate + NAD+ = 5,10-methylenetetrahydrofolate + NADH + H+
For diagram of reaction, click here and for its place in C1 metabolism, click here
Other name(s): metF (gene name); 5,10-methylenetetrahydrofolic acid reductase (ambiguous); 5,10-CH2-H4folate reductase (ambiguous); methylenetetrahydrofolate (reduced riboflavin adenine dinucleotide) reductase; 5,10-methylenetetrahydrofolate reductase (ambiguous); methylenetetrahydrofolate reductase (ambiguous); N5,10-methylenetetrahydrofolate reductase (ambiguous); 5,10-methylenetetrahydropteroylglutamate reductase (ambiguous); N5,N10-methylenetetrahydrofolate reductase (ambiguous); methylenetetrahydrofolic acid reductase (ambiguous); 5-methyltetrahydrofolate:(acceptor) oxidoreductase (incorrect); 5,10-methylenetetrahydrofolate reductase (FADH2) (ambiguous)
Systematic name: 5-methyltetrahydrofolate:NAD+ oxidoreductase
Comments: A flavoprotein (FAD). The enzyme, found in plants and some bacteria, catalyses the reversible conversion of 5,10-methylenetetrahydrofolate to 5-methyltetrahydrofolate using NADH as the electron donor. It play an important role in folate metabolism by regulating the distribution of one-carbon moieties between cellular methylation reactions and nucleic acid synthesis. These proteins either contain a C-terminal domain that does not mediate allosteric regulation (as in plants) or lack this domain entirely (as in Escherichia coli). As a result, the plant enzymes are not inhibited by S-adenosyl-L-methionine, unlike other eukaryotic enzymes, and catalyse a reversible reaction. cf. EC 1.5.1.53, methylenetetrahydrofolate reductase (NADPH); EC 1.5.1.20, methylenetetrahydrofolate reductase [NAD(P)H]; and EC 1.5.7.1, methylenetetrahydrofolate reductase (ferredoxin).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Wohlfarth, G., Geerligs, G. and Diekert, G. Purification and properties of a NADH-dependent 5,10-methylenetetrahydrofolate reductase from Peptostreptococcus productus. Eur. J. Biochem. 192 (1990) 411-417. [PMID: 2209595]
2. Sheppard, C.A., Trimmer, E.E. and Matthews, R.G. Purification and properties of NADH-dependent 5,10-methylenetetrahydrofolate reductase (MetF) from Escherichia coli. J. Bacteriol. 181 (1999) 718-725. [PMID: 9922232]
3. Guenther, B.D., Sheppard, C.A., Tran, P., Rozen, R., Matthews, R.G. and Ludwig, M.L. The structure and properties of methylenetetrahydrofolate reductase from Escherichia coli suggest how folate ameliorates human hyperhomocysteinemia. Nat. Struct. Biol. 6 (1999) 359-365. [PMID: 10201405]
4. Roje, S., Wang, H., McNeil, S.D., Raymond, R.K., Appling, D.R., Shachar-Hill, Y., Bohnert, H.J. and Hanson, A.D. Isolation, characterization, and functional expression of cDNAs encoding NADH-dependent methylenetetrahydrofolate reductase from higher plants. J. Biol. Chem. 274 (1999) 36089-36096. [PMID: 10593891]
5. Bertsch, J., Oppinger, C., Hess, V., Langer, J.D. and Muller, V. Heterotrimeric NADH-oxidizing methylenetetrahydrofolate reductase from the acetogenic bacterium Acetobacterium woodii. J. Bacteriol. 197 (2015) 1681-1689. [PMID: 25733614]
Accepted name: carboxyaminopropylagmatine dehydrogenase
Reaction: N1-[(S)-3-amino-3-carboxypropyl]agamatine + NADP+ + H2O = agmatine + L-aspartate 4-semialdehyde + NADPH + H+
Glossary: N1-[(S)-3-amino-3-carboxypropyl]agamatine = carboxyaminopropylagmatine
L-aspartate 4-semialdehyde = L-aspartate β-semialdehyde
Other name(s): slr0049 (locus name)
Systematic name: N1-[(S)-2-aminobutanoate]agmatine:NADP+ oxidoreductase (agmatine-forming)
Comments: The enzyme, characterized from the cyanobacterium Synechocystis sp. PCC 6803, catalyses the reductive condensation of agmatine and L-aspartate 4-semialdehyde. It participates in a biosynthetic pathway for spermidine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Xi, H., Nie, X., Gao, F., Liang, X., Li, H., Zhou, H., Cai, Y. and Yang, C. A bacterial spermidine biosynthetic pathway via carboxyaminopropylagmatine. Sci Adv 9 (2023) eadj9075. [PMID: 37878710]
Accepted name: 3,17-didehydrostemmadenine reductase
Reaction: 17-dehydrostemmadenine + NADP+ = 3,17-didehydrostemmadenine + NADPH + H+
For diagram of reaction, click here
Glossary: 3,17-didehydrostemmadenine = 3,4-didehydro-17-dehydrostemmadenine
Other name(s): Redox1
Systematic name: 17-dehydrostemmadenine:NADP+ 3(4)-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. Both the substrate and the product of the enzyme are unstable.
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: 18-hydroxynorfluorocurarine reductase
Reaction: 17,18-epoxy-17-hydroxycur-19-ene + NADP+ = 18-hydroxynorfluorocurarine + NADPH + H+
For diagram of reaction click here
Glossary: 17,18-epoxy-17-hydroxycur-19-ene = (19E)-18-hydroxycur-19-en-17-al = Wieland-Gumlich aldehyde
norfluorocurarine = (19E)-cura-2(16),19-dien-17-al
Other name(s): Wieland-Gumlich aldehyde synthase
Systematic name: 17,18-epoxy-17-hydroxycur-19-ene:NADP+ oxidoreductase
Comments: The enzyme, isolated from the tree Strychnos nux-vomica, participates in the biosynthesis of strychnine. It belongs to the family of medium-chain dehydrogenase/reductases (MDRs). The enzyme forms an aldehyde group at C16, which results in spontaneous cyclization. In vitro the enzyme can also act on norfluorocurarine, but more slowly.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Hong, B., Grzech, D., Caputi, L., Sonawane, P., Lopez, C.ER., Kamileen, M.O., Hernandez Lozada, N.J., Grabe, V. and O'Connor, S.E. Biosynthesis of strychnine. Nature 607 (2022) 617-622. [PMID: 35794473]
EC 1.5.3.13 N1-acetylpolyamine oxidase
EC 1.5.3.14 polyamine oxidase (propane-1,3-diamine-forming)
EC 1.5.3.15 N8-acetylspermidine oxidase (propane-1,3-diamine-forming)
EC 1.5.3.16 spermine oxidase
EC 1.5.3.17 non-specific polyamine oxidase
EC 1.5.3.18 L-saccharopine oxidase
EC 1.5.3.19 4-methylaminobutanoate oxidase (formaldehyde-forming)
EC 1.5.3.20 N-alkylglycine oxidase
EC 1.5.3.21 4-methylaminobutanoate oxidase (methylamine-forming)
EC 1.5.3.22 coenzyme F420H2 oxidase
EC 1.5.3.23 glyphosate oxidoreductase
EC 1.5.3.24 sarcosine oxidase (5,10-methylenetetrahydrofolate-forming)
EC 1.5.3.25 fructosyl amine oxidase (glucosone-forming)
EC 1.5.3.26 fructosyl amine oxidase (fructosamine-forming)
EC 1.5.3.27 2-(methylaminoethyl)phosphonate oxidase
Accepted name: sarcosine oxidase (formaldehyde-forming)
Reaction: sarcosine + H2O + O2 = glycine + formaldehyde + H2O2
Other name(s): MSOX; monomeric sarcosine oxidase; sarcosine oxidase (ambiguous)
Systematic name: sarcosine:oxygen oxidoreductase (demethylating)
Comments: The enzyme, reported from bacteria and fungi, catalyses the oxidative demethylation of sarcosine. It contains a FAD cofactor bound to an L-cysteine residue. cf. EC 1.5.3.24, sarcosine oxidase (5,10-methylenetetrahydrofolate-forming).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9029-22-5
References:
1. Mori, N., Sano, M., Tani, Y. and Yamada, H. Purification and propertie of sarcosine oxidase from Cylindrocarpon didymum M-1. Agric. Biol. Chem. 44 (1980) 1391-1397.
2. Nishiya, Y. and Imanaka, T. Cloning and sequencing of the sarcosine oxidase gene from Arthrobacter sp. TE1826. J. Ferment. Bioeng. 75 (1993) 239-244.
3. Nishiya, Y. and Imanaka, T. Alteration of substrate specificity and optimum pH of sarcosine oxidase by random and site-directed mutagenesis. Appl. Environ. Microbiol. 60 (1994) 4213-4215. [PMID: 16349451]
4. Trickey, P., Wagner, M.A., Jorns, M.S. and Mathews, F.S. Monomeric sarcosine oxidase: structure of a covalently flavinylated amine oxidizing enzyme. Structure 7 (1999) 331-345. [PMID: 10368302]
5. Wagner, M.A., Trickey, P., Chen, Z.W., Mathews, F.S. and Jorns, M.S. Monomeric sarcosine oxidase: 1. Flavin reactivity and active site binding determinants. Biochemistry 39 (2000) 8813-8824. [PMID: 10913292]
6. Zhao, G., Bruckner, R.C. and Jorns, M.S. Identification of the oxygen activation site in monomeric sarcosine oxidase: role of Lys265 in catalysis. Biochemistry 47 (2008) 9124-9135. [PMID: 18693755]
7. Jorns, M.S., Chen, Z.W. and Mathews, F.S. Structural characterization of mutations at the oxygen activation site in monomeric sarcosine oxidase. Biochemistry 49 (2010) 3631-3639. [PMID: 20353187]
8. Bucci, A., Yu, T.Q., Vanden-Eijnden, E. and Abrams, C.F. Kinetics of O2 entry and exit in monomeric sarcosine oxidase via Markovian milestoning molecular dynamics. J Chem Theory Comput 12 (2016) 2964-2972. [PMID: 27168219]
Accepted name: N-methyl-L-amino-acid oxidase
Reaction: an N-methyl-L-amino acid + H2O + O2 = an L-amino acid + formaldehyde + H2O2
Other name(s): N-methylamino acid oxidase; demethylase
Systematic name: N-methyl-L-amino-acid:oxygen oxidoreductase (demethylating)
Comments: A flavoprotein.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9029-23-6
References:
1. Moritani, M. Demethylase. IV. Kinetics and reaction mechanism. Hukuoka Acta Med. 43 (1952) 651-658.
2. Moritani, M. Demethylase. V. Specificity and its relation to amino acid oxidase. Hukuoka Acta Med. 43 (1952) 731-735.
3. Moritani, M., Tung, T.-C., Fujii, S., Mito, H., Izumika, N., Kenmochi, K. and Hirohata, R. Specificity of rabbit kidney demethylase. J. Biol. Chem. 209 (1954) 485-492.
[EC 1.5.3.3 Deleted entry: spermine oxidase (EC 1.5.3.3 created 1961, deleted 1972)]
Accepted name: N6-methyl-lysine oxidase
Reaction: N6-methyl-L-lysine + H2O + O2 = L-lysine + formaldehyde + H2O2
Other name(s): ε-alkyl-L-lysine:oxygen oxidoreductase ; N6-methyllysine oxidase; ε-N-methyllysine demethylase; ε-alkyllysinase
Systematic name: N6-methyl-L-lysine:oxygen oxidoreductase (demethylating)
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37256-28-3
References:
1. Kim, S., Benoiton, L. and Paik, W.K. α-Alkyllysinase. Purification and properties of the enzyme. J. Biol. Chem. 239 (1964) 3790-3796.
Accepted name: (S)-6-hydroxynicotine oxidase
Reaction: (S)-6-hydroxynicotine + H2O + O2 = 1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2 (overall reaction)
(1a) (S)-6-hydroxynicotine + O2 = 5-(N-methyl-4,5-dihydro-1H-pyrrol-2-yl)pyridin-2-ol + H2O2
(1b) 5-(N-methyl-4,5-dihydro-1H-pyrrol-2-yl)pyridin-2-ol + H2O = 1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one (spontaneous)
For diagram of reaction click here.
Glossary: (S)-6-hydroxynicotine = 5-[(2S)-1-methylpyrrolidin-2-yl]pyridin-2-ol
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one = 6-hydroxypseudooxynicotine
5-(N-methyl-4,5-dihydro-1H-pyrrol-2-yl)pyridin-2-ol = 6-hydroxy-N-methylmyosmine
Other name(s): L-6-hydroxynicotine oxidase; 6-hydroxy-L-nicotine oxidase; 6-hydroxy-L-nicotine:oxygen oxidoreductase; nctB (gene name)
Systematic name: (S)-6-hydroxynicotine:oxygen oxidoreductase
Comments: A flavoprotein (FAD). The enzyme, which participates in nicotine degradation, is specific for the (S) isomer of 6-hydroxynicotine. The bacterium Arthrobacter nicotinovorans, in which this enzyme was originally discovered, has a different enzyme that catalyses a similar reaction with the less common (R)-isomer (cf. EC 1.5.3.6, (R)-6-hydroxynicotine oxidase).
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37256-29-4
References:
1. Decker, K. and Bleeg, H. Induction and purification of stereospecific nicotine oxidizing enzymes from Arthrobacter oxidans. Biochim. Biophys. Acta 105 (1965) 313-324. [PMID: 5849820]
2. Dai, V.D., Decker, K. and Sund, H. Purification and properties of L-6-hydroxynicotine oxidase. Eur. J. Biochem. 4 (1968) 95-102. [PMID: 5646150]
3. Schenk, S., Hoelz, A., Krauss, B. and Decker, K. Gene structures and properties of enzymes of the plasmid-encoded nicotine catabolism of Arthrobacter nicotinovorans. J. Mol. Biol. 284 (1998) 1323-1339. [PMID: 9878353]
4. Qiu, J., Wei, Y., Ma, Y., Wen, R., Wen, Y. and Liu, W. A novel (S)-6-hydroxynicotine oxidase gene from Shinella sp. strain HZN7. Appl. Environ. Microbiol. 80 (2014) 5552-5560. [PMID: 25002425]
Accepted name: (R)-6-hydroxynicotine oxidase
Reaction: (R)-6-hydroxynicotine + H2O + O2 = 1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2 (overall reaction)
(1a) (R)-6-hydroxynicotine + O2 = 5-(N-methyl-4,5-dihydro-1H-pyrrol-2-yl)pyridin-2-ol + H2O2
(1b) 5-(N-methyl-4,5-dihydro-1H-pyrrol-2-yl)pyridin-2-ol + H2O = 1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one (spontaneous)
For diagram of reaction click here.
Glossary: (R)-6-hydroxynicotine = 5-[(2R)-1-methylpyrrolidin-2-yl]pyridin-2-ol
5-(N-methyl-4,5-dihydro-1H-pyrrol-2-yl)pyridin-2-ol = 6-hydroxy-N-methylmyosmine
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one = 6-hydroxypseudooxynicotine
Other name(s): D-6-hydroxynicotine oxidase; 6-hydroxy-D-nicotine oxidase
Systematic name: (R)-6-hydroxynicotine:oxygen oxidoreductase
Comments: A flavoprotein (FAD). The enzyme, which participates in nicotine degradation, is specific for (R) isomer of 6-hydroxynicotine, derived from the uncommon (R)-nicotine. The bacterium Arthrobacter nicotinovorans, in which this enzyme was originally discovered, has a different enzyme that catalyses a similar reaction with the (S)-isomer (cf. EC 1.5.3.5, (S)-6-hydroxynicotine oxidase).
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37233-46-8
References:
1. Decker, K. and Bleeg, H. Induction and purification of stereospecific nicotine oxidizing enzymes from Arthrobacter oxidans. Biochim. Biophys. Acta 105 (1965) 313-324. [PMID: 5849820]
2. Brühmüller, M., Möhler, H.K. and Decker, K. Covalently bound flavin in D-6-hydroxynicotine oxidase from Arthrobacter oxidans. Purification and properties of D-6-hydroxynicotine oxidase. Eur. J. Biochem. 29 (1972) 143-151. [PMID: 4628374]
3. Brandsch, R., Hinkkanen, A.E., Mauch, L., Nagursky, H. and Decker, K. 6-Hydroxy-D-nicotine oxidase of Arthrobacter oxidans. Gene structure of the flavoenzyme and its relationship to 6-hydroxy-L-nicotine oxidase. Eur. J. Biochem. 167 (1987) 315-320. [PMID: 3622516]
4. Schenk, S., Hoelz, A., Krauss, B. and Decker, K. Gene structures and properties of enzymes of the plasmid-encoded nicotine catabolism of Arthrobacter nicotinovorans. J. Mol. Biol. 284 (1998) 1323-1339. [PMID: 9878353]
5. Koetter, J.W. and Schulz, G.E. Crystal structure of 6-hydroxy-D-nicotine oxidase from Arthrobacter nicotinovorans. J. Mol. Biol. 352 (2005) 418-428. [PMID: 16095622]
Accepted name: L-pipecolate oxidase
Reaction: L-pipecolate + O2 = (S)-2,3,4,5-tetrahydropyridine-2-carboxylate + H2O2
Glossary: L-1-piperideine 6-carboxylate = (S)-2,3,4,5-tetrahydropyridine-2-carboxylate = (S)-1,6-didehydropiperidine-2-carboxylate
(S)-2-amino-6-oxohexanoate = L-2-aminoadipate 6-semialdehyde = L-allysine
Other name(s): pipecolate oxidase; L-pipecolic acid oxidase
Systematic name: L-pipecolate:oxygen 1,6-oxidoreductase
Comments: The product reacts with water to form 2-aminoadipate 6-semialdehyde, i.e. 2-amino-6-oxohexanoate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 81669-65-0
References:
1. Baginsky, B.L. and Rodwell, V.W. Metabolism of pipecolic acid in a Pseudomonas species. V. Pipecolate oxidase and dehydrogenase. J. Bacteriol. 94 (1967) 1034-1039. [PMID: 6051341]
2. Kinzel, J.J. and Bhattacharjee, J.K. Lysine biosynthesis in Rhodotorula glutinis: properties of pipecolic acid oxidase. J. Bacteriol. 151 (1982) 1073-1077. [PMID: 6809728]
[EC 1.5.3.8 Deleted entry: now included with EC 1.3.3.8 tetrahydroberberine oxidase (EC 1.5.3.8 created 1989, deleted 1992)]
[EC 1.5.3.9 Transferred entry: now EC 1.21.3.3, reticuline oxidase (EC 1.5.3.9 created 1989, modified 1999, deleted 2002)]
Accepted name: dimethylglycine oxidase
Reaction: N,N-dimethylglycine + 5,6,7,8-tetrahydrofolate + O2 = sarcosine + 5,10-methylenetetrahydrofolate + H2O2
Other name(s): dmg (gene name); N,N-dimethylglycine:oxygen oxidoreductase (demethylating)
Systematic name: N,N-dimethylglycine,5,6,7,8-tetrahydrofolate:oxygen oxidoreductase (demethylating,5,10-methylenetetrahydrofolate-forming)
Comments: A flavoprotein (FAD). The enzyme, characterized from the bacterium Arthrobacter globiformis, contains two active sites connected by a large "reaction chamber". An imine intermediate is transferred between the sites, eliminating the production of toxic formaldehyde. In the absence of folate the enzyme does form formaldehyde. Does not oxidize sarcosine. cf. EC 1.5.8.4, dimethylglycine dehydrogenase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37256-30-7
References:
1. Mori, N., Kawakami, B., Tani, Y. and Yamada, H. Purification and properties of dimethylglycine oxidase from Cylindrocarpon didymum M-1. Agric. Biol. Chem. 44 (1980) 1383-1389.
2. Meskys, R., Harris, R.J., Casaite, V., Basran, J. and Scrutton, N.S. Organization of the genes involved in dimethylglycine and sarcosine degradation in Arthrobacter spp.: implications for glycine betaine catabolism. Eur. J. Biochem. 268 (2001) 3390-3398. [PMID: 11422368]
3. Basran, J., Bhanji, N., Basran, A., Nietlispach, D., Mistry, S., Meskys, R. and Scrutton, N.S. Mechanistic aspects of the covalent flavoprotein dimethylglycine oxidase of Arthrobacter globiformis studied by stopped-flow spectrophotometry. Biochemistry 41 (2002) 4733-4743. [PMID: 11926836]
4. Leys, D., Basran, J. and Scrutton, N.S. Channelling and formation of ‘active’ formaldehyde in dimethylglycine oxidase. EMBO J. 22 (2003) 4038-4048. [PMID: 12912903]
5. Basran, J., Fullerton, S., Leys, D. and Scrutton, N.S. Mechanism of FAD reduction and role of active site residues His-225 and Tyr-259 in Arthrobacter globiformis dimethylglycine oxidase: analysis of mutant structure and catalytic function. Biochemistry 45 (2006) 11151-11161. [PMID: 16964976]
6. Tralau, T., Lafite, P., Levy, C., Combe, J.P., Scrutton, N.S. and Leys, D. An internal reaction chamber in dimethylglycine oxidase provides efficient protection from exposure to toxic formaldehyde. J. Biol. Chem. 284 (2009) 17826-17834. [PMID: 19369258]
7. Casaite, V., Poviloniene, S., Meskiene, R., Rutkiene, R. and Meskys, R. Studies of dimethylglycine oxidase isoenzymes in Arthrobacter globiformis cells. Curr. Microbiol. 62 (2011) 1267-1273. [PMID: 21188587]
[EC 1.5.3.11 Deleted entry: Now included with EC 1.5.3.13 N1-acetylpolyamine oxidase, EC 1.5.3.14 polyamine oxidase (propane-1,3-diamine-forming), EC 1.5.3.15 N8-acetylspermidine oxidase (propane-1,3-diamine-forming), EC 1.5.3.16 spermine oxidase and EC 1.5.3.17 non-specific polyamine oxidase (EC 1.5.3.11 created 1992, deleted 2009)]
Accepted name: dihydrobenzophenanthridine oxidase
Reaction: (1) dihydrosanguinarine + O2 = sanguinarine + H2O2;
(2) dihydrochelirubine + O2 = chelirubine + H2O2;
(3) dihydromacarpine + O2 = macarpine + H2O2
For diagram click here.
Systematic name: dihydrobenzophenanthridine:oxygen oxidoreductase
Comments: a CuII enzyme found in higher plants that produces oxidized forms of the benzophenanthridine alkaloids
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 114051-83-1
References:
1. Schumacher, H.-M. and Zenk, M.H. Partial purification and characterization of dihydrobenzophenanthridine oxidase from Eschscholtzia tenuifolia cell suspension cultures. Plant Cell Reports 7 (1988) 43-46.
2. Arakawa, H., Clark, W.G., Psenak. M. and Coscia, C.J. Purification and characterization of dihydrobenzophenanthridine oxidase from elicited Sanguinaria canadensis cell cultures. Arch. Biochem. Biophys. 299 (1992) 1-7. [PMID: 1444440]
Accepted name: N1-acetylpolyamine oxidase
Reaction: (1) N1-acetylspermidine + O2 + H2O = putrescine + 3-acetamidopropanal + H2O2
(2) N1-acetylspermine + O2 + H2O = spermidine + 3-acetamidopropanal + H2O2
Other name(s): hPAO-1; PAO (ambiguous); mPAO; hPAO; polyamine oxidase (ambiguous)
Systematic name: N1-acetylpolyamine:oxygen oxidoreductase (3-acetamidopropanal-forming)
Comments: The enzyme also catalyses the reaction: N1,N12-diacetylspermine + O2 + H2O = N1-acetylspermidine + 3-acetamamidopropanal + H2O2 [1]. No or very weak activity with spermine, or spermidine in absence of aldehydes. In presence of aldehydes the enzyme catalyses the reactions: 1. spermine + O2 + H2O = spermidine + 3-aminopropanal + H2O2, and with weak efficiency 2. spermidine + O2 + H2O = putrescine + 3-aminopropanal + H2O2 [2]. A flavoprotein (FAD). This enzyme, encoded by the PAOX gene, is found in mammalian peroxisomes and oxidizes N1-acetylated polyamines at the exo (three-carbon) side of the secondary amine, forming 3-acetamamidopropanal. Since the products of the reactions are deacetylated polyamines, this process is known as polyamine back-conversion. Differs in specificity from EC 1.5.3.14 [polyamine oxidase (propane-1,3-diamine-forming)], EC 1.5.3.15 [N8-acetylspermidine oxidase (propane-1,3-diamine-forming)], EC 1.5.3.16 (spermine oxidase) and EC 1.5.3.17 (non-specific polyamine oxidase).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Vujcic, S., Liang, P., Diegelman, P., Kramer, D.L. and Porter, C.W. Genomic identification and biochemical characterization of the mammalian polyamine oxidase involved in polyamine back-conversion. Biochem. J. 370 (2003) 19-28. [PMID: 12477380]
2. Jarvinen, A., Grigorenko, N., Khomutov, A.R., Hyvonen, M.T., Uimari, A., Vepsalainen, J., Sinervirta, R., Keinanen, T.A., Vujcic, S., Alhonen, L., Porter, C.W. and Janne, J. Metabolic stability of α-methylated polyamine derivatives and their use as substitutes for the natural polyamines. J. Biol. Chem. 280 (2005) 6595-6601. [PMID: 15611107]
3. Wang, Y., Hacker, A., Murray-Stewart, T., Frydman, B., Valasinas, A., Fraser, A.V., Woster, P.M. and Casero, R.A., Jr. Properties of recombinant human N1-acetylpolyamine oxidase (hPAO): potential role in determining drug sensitivity. Cancer Chemother Pharmacol 56 (2005) 83-90. [PMID: 15791459]
4. Wu, T., Yankovskaya, V. and McIntire, W.S. Cloning, sequencing, and heterologous expression of the murine peroxisomal flavoprotein, N1-acetylated polyamine oxidase. J. Biol. Chem. 278 (2003) 20514-20525. [PMID: 12660232]
Accepted name: polyamine oxidase (propane-1,3-diamine-forming)
Reaction: spermidine + O2 + H2O = propane-1,3-diamine + 4-aminobutanal + H2O2
Other name(s): MPAO (ambiguous); maize PAO
Systematic name: spermidine:oxygen oxidoreductase (propane-1,3-diamine-forming)
Comments: As the products of the reaction cannot be converted directly to other polyamines, this class of polyamine oxidases is considered to be involved in the terminal catabolism of polyamines [1]. This enzyme less efficiently catalyses the oxidation of N1-acetylspermine and spermine. A flavoprotein (FAD). Differs in specificity from EC 1.5.3.13 (N1-acetylpolyamine oxidase), EC 1.5.3.15 [N8-acetylspermidine oxidase (propane-1,3-diamine-forming)], EC 1.5.3.16 (spermine oxidase) and EC 1.5.3.17 (non-specific polyamine oxidase).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Tavladoraki, P., Schinina, M.E., Cecconi, F., Di Agostino, S., Manera, F., Rea, G., Mariottini, P., Federico, R. and Angelini, R. Maize polyamine oxidase: primary structure from protein and cDNA sequencing. FEBS Lett. 426 (1998) 62-66. [PMID: 9598979]
2. Federico, R., Ercolini, L., Laurenzi, M., Angelini, R. Oxidation of acetylpolyamines by maize polyamine oxidase. Phytochemistry 43 (1996) 339-341.
Accepted name: N8-acetylspermidine oxidase (propane-1,3-diamine-forming)
Reaction: N8-acetylspermidine + O2 + H2O = propane-1,3-diamine + 4-acetamidobutanal + H2O2
Systematic name: N8-acetylspermidine:oxygen oxidoreductase (propane-1,3-diamine-forming)
Comments: Also active with N1-acetylspermine, weak activity with N1,N12-diacetylspermine. No activity with diaminopropane, putrescine, cadaverine, diaminohexane, norspermidine, spermine and spermidine. Absence of monoamine oxidase (EC 1.4.3.4) activity. Differs in specificity from EC 1.5.3.13 (N1-acetylpolyamine oxidase), EC 1.5.3.14 [polyamine oxidase (propane-1,3-diamine-forming)], EC 1.5.3.16 (spermine oxidase) and EC 1.5.3.17 (non-specific polyamine oxidase).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Shukla, O.P., Muller, S. and Walter, R.D. Polyamine oxidase from Acanthamoeba culbertsoni specific for N8-acetylspermidine. Mol. Biochem. Parasitol. 51 (1992) 91-98. [PMID: 1565141]
Accepted name: spermine oxidase
Reaction: spermine + O2 + H2O = spermidine + 3-aminopropanal + H2O2
Other name(s): PAOh1/SMO; PAOh1 (ambiguous); AtPAO1; AtPAO4; SMO; mSMO; SMO(PAOh1); SMO/PAOh1; SMO5; mSMOmu
Systematic name: spermidine:oxygen oxidoreductase (spermidine-forming)
Comments: The enzyme from Arabidopsis thaliana (AtPAO1) oxidizes norspermine to norspermidine with high efficiency [3]. The mammalian enzyme, encoded by the SMOX gene, is a cytosolic enzyme that catalyses the oxidation of spermine at the exo (three-carbon) side of the tertiary amine. No activity with spermidine. Weak activity with N1-acetylspermine. A flavoprotein (FAD). Differs in specificity from EC 1.5.3.13 (N1-acetylpolyamine oxidase), EC 1.5.3.14 [polyamine oxidase (propane-1,3-diamine-forming)], EC 1.5.3.15 [N8-acetylspermidine oxidase (propane-1,3-diamine-forming)] and EC 1.5.3.17 (non-specific polyamine oxidase).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Murray-Stewart, T., Wang, Y., Goodwin, A., Hacker, A., Meeker, A. and Casero, R.A., Jr. Nuclear localization of human spermine oxidase isoforms - possible implications in drug response and disease etiology. FEBS J. 275 (2008) 2795-2806. [PMID: 18422650]
2. Cervelli, M., Polticelli, F., Federico, R. and Mariottini, P. Heterologous expression and characterization of mouse spermine oxidase. J. Biol. Chem. 278 (2003) 5271-5276. [PMID: 12458219]
3. Tavladoraki, P., Rossi, M.N., Saccuti, G., Perez-Amador, M.A., Polticelli, F., Angelini, R. and Federico, R. Heterologous expression and biochemical characterization of a polyamine oxidase from Arabidopsis involved in polyamine back conversion. Plant Physiol. 141 (2006) 1519-1532. [PMID: 16778015]
4. Wang, Y., Murray-Stewart, T., Devereux, W., Hacker, A., Frydman, B., Woster, P.M. and Casero, R.A., Jr. Properties of purified recombinant human polyamine oxidase, PAOh1/SMO. Biochem. Biophys. Res. Commun. 304 (2003) 605-611. [PMID: 12727196]
Accepted name: non-specific polyamine oxidase
Reaction: (1) spermine + O2 + H2O = spermidine + 3-aminopropanal + H2O2
(2) spermidine + O2 + H2O = putrescine + 3-aminopropanal + H2O2
(3) N1-acetylspermine + O2 + H2O = spermidine + 3-acetamidopropanal + H2O2
(4) N1-acetylspermidine + O2 + H2O = putrescine + 3-acetamidopropanal + H2O2
Other name(s): polyamine oxidase (ambiguous); Fms1; AtPAO3
Systematic name: polyamine:oxygen oxidoreductase (3-aminopropanal or 3-acetamidopropanal-forming)
Comments: A flavoprotein (FAD). The non-specific polyamine oxidases may differ from each other considerably. The enzyme from Saccharomyces cerevisiae shows a rather broad specificity and also oxidizes N8-acetylspermidine [3]. The enzyme from Ascaris suum shows high activity with spermine and spermidine, but also oxidizes norspermine [2]. The enzyme from Arabidopsis thaliana shows high activity with spermidine, but also oxidizes other polyamines [1]. The specific polyamine oxidases are classified as EC 1.5.3.13 (N1-acetylpolyamine oxidase), EC 1.5.3.14 [polyamine oxidase (propane-1,3-diamine-forming)], EC 1.5.3.15 [N8-acetylspermidine oxidase (propane-1,3-diamine-forming)] and EC 1.5.3.16 (spermine oxidase).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Moschou, P.N., Sanmartin, M., Andriopoulou, A.H., Rojo, E., Sanchez-Serrano, J.J. and Roubelakis-Angelakis, K.A. Bridging the gap between plant and mammalian polyamine catabolism: a novel peroxisomal polyamine oxidase responsible for a full back-conversion pathway in Arabidopsis. Plant Physiol. 147 (2008) 1845-1857. [PMID: 18583528]
2. Muller, S. and Walter, R.D. Purification and characterization of polyamine oxidase from Ascaris suum. Biochem. J. 283 (1992) 75-80. [PMID: 1567380]
3. Landry, J. and Sternglanz, R. Yeast Fms1 is a FAD-utilizing polyamine oxidase. Biochem. Biophys. Res. Commun. 303 (2003) 771-776. [PMID: 12670477]
Accepted name: L-saccharopine oxidase
Reaction: N6-(L-1,3-dicarboxypropyl)-L-lysine + H2O + O2 = (S)-2-amino-6-oxohexanoate + L-glutamate + H2O2
Glossary: L-saccharopine = N6-(L-1,3-dicarboxypropyl)-L-lysine
(S)-2-amino-6-oxohexanoate = L-2-aminoadipate 6-semialdehyde = L-allysine
Other name(s): FAP2
Systematic name: L-saccharopine:oxygen oxidoreductase (L-glutamate forming)
Comments: The enzyme is involved in pipecolic acid biosynthesis. A flavoprotein (FAD).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Yoshida, N., Akazawa, S., Katsuragi, T. and Tani, Y. Characterization of two fructosyl-amino acid oxidase homologs of Schizosaccharomyces pombe. J. Biosci. Bioeng. 97 (2004) 278-280. [PMID: 16233628]
2. Wickwire, B.M., Wagner, C. and Broquist, H.P. Pipecolic acid biosynthesis in Rhizoctonia leguminicola. II. Saccharopine oxidase: a unique flavin enzyme involved in pipecolic acid biosynthesis. J. Biol. Chem. 265 (1990) 14748-14753. [PMID: 2394693]
Accepted name: 4-methylaminobutanoate oxidase (formaldehyde-forming)
Reaction: 4-methylaminobutanoate + O2 + H2O = 4-aminobutanoate + formaldehyde + H2O2
For diagram of reaction click here.
Other name(s): mabO (gene name)
Systematic name: 4-methylaminobutanoate:oxygen oxidoreductase (formaldehyde-forming)
Comments: A flavoprotein (FAD). In the enzyme from the soil bacterium Arthrobacter nicotinovorans the cofactor is covalently bound. Participates in the nicotine degradation pathway of this organism.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Chiribau, C.B., Sandu, C., Fraaije, M., Schiltz, E. and Brandsch, R. A novel γ-N-methylaminobutyrate demethylating oxidase involved in catabolism of the tobacco alkaloid nicotine by Arthrobacter nicotinovorans pAO1. Eur. J. Biochem. 271 (2004) 4677-4684. [PMID: 15606755]
Accepted name: N-alkylglycine oxidase
Reaction: N-alkylglycine + H2O + O2 = alkylamine + glyoxalate + H2O2
Other name(s): N-carboxymethylalkylamine:oxygen oxidoreductase (decarboxymethylating)
Systematic name: N-alkylglycine:oxygen oxidoreductase (alkylamine forming)
Comments: Isolated from the mold Cladosporium sp. G-10. Acts on N6-(carboxymethyl)lysine, 6-[(carboxymethy)amino]hexanoic acid, sarcosine and N-ethylglycine. It has negligible action on glycine (cf. EC 1.4.3.19 glycine oxidase).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Gomi, K. and Horiuchi, T. Purification and characterization of a new enzyme, N-alkylglycine oxidase from Cladosporium sp. G-10. Biochim. Biophys. Acta 1429 (1999) 439-445. [PMID: 9989229]
Accepted name: 4-methylaminobutanoate oxidase (methylamine-forming)
Reaction: 4-methylaminobutanoate + O2 + H2O = succinate semialdehyde + methylamine + H2O2
For diagram of reaction click here.
Other name(s): mao (gene name, ambiguous)
Systematic name: 4-methylaminobutanoate methylamidohydrolase
Comments: The enzyme participates in the nicotine degradation pathway of the soil bacterium Arthrobacter nicotinovorans. Has a very weak monoamine oxidase (EC 1.4.3.4) activity with 4-aminobutanoate [1].
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Chiribau, C.B., Sandu, C., Fraaije, M., Schiltz, E. and Brandsch, R. A novel γ-N-methylaminobutyrate demethylating oxidase involved in catabolism of the tobacco alkaloid nicotine by Arthrobacter nicotinovorans pAO1. Eur. J. Biochem. 271 (2004) 4677-4684. [PMID: 15606755]
2. Chiribau, C.B., Mihasan, M., Ganas, P., Igloi, G.L., Artenie, V. and Brandsch, R. Final steps in the catabolism of nicotine. FEBS J. 273 (2006) 1528-1536. [PMID: 16689938]
Accepted name: coenzyme F420H2 oxidase
Reaction: 2 reduced coenzyme F420 + O2 = 2 oxidized coenzyme F420 + 2 H2O
Glossary: oxidized coenzyme F420 = N-(N-{O-[5-(8-hydroxy-2,4-dioxo-2,3,4,10-tetrahydropyrimido[4,5-b]quinolin-10-yl)-5-deoxy-L-ribityl-1-phospho]-(S)-lactyl}-γ-L-glutamyl)-L-glutamate
Other name(s): FprA
Systematic name: reduced coenzyme F420:oxygen oxidoreductase
Comments: The enzyme contains FMN and a binuclear iron center. The enzyme from the archaeon Methanothermobacter marburgensis is Si-face specific with respect to C-5 of coenzyme F420 [2].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Seedorf, H., Dreisbach, A., Hedderich, R., Shima, S. and Thauer, R.K. F420H2 oxidase (FprA) from Methanobrevibacter arboriphilus, a coenzyme F420-dependent enzyme involved in O2 detoxification. Arch. Microbiol. 182 (2004) 126-137. [PMID: 15340796]
2. Seedorf, H., Kahnt, J., Pierik, A.J. and Thauer, R.K. Si-face stereospecificity at C5 of coenzyme F420 for F420H2 oxidase from methanogenic Archaea as determined by mass spectrometry. FEBS J. 272 (2005) 5337-5342. [PMID: 16218963]
3. Seedorf, H., Hagemeier, C.H., Shima, S., Thauer, R.K., Warkentin, E. and Ermler, U. Structure of coenzyme F420H2 oxidase (FprA), a di-iron flavoprotein from methanogenic Archaea catalyzing the reduction of O2 to H2O. FEBS J. 274 (2007) 1588-1599. [PMID: 17480207]
Accepted name: glyphosate oxidoreductase
Reaction: 2 glyphosate + O2 = 2 aminomethylphosphonate + 2 glyoxylate
Glossary: glyphosate = N-(phosphonomethyl)glycine
Other name(s): gox (gene name)
Systematic name: glyphosate oxidoreductase (aminomethylphosphonate-forming)
Comments: The enzyme, characterized from the bacterium Ochrobactrum sp. G-1, contains an FAD cofactor. The catalytic cycle starts with a reduction of the FAD cofactor by one molecule of glyphosate, yielding reduced FAD and a Schiff base of aminomethylphosphonate with glyoxylate that is hydrolysed to the single components. The reduced FAD is reoxidized by oxygen, generating water and an oxygenated flavin intermediate, which catalyses the oxygenation of a second molecule of glyphosate, forming the second pair of aminomethylphosphonate and glyoxylate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Barry, G. F. and Kishore. G. M. Glyphosate tolerant plants. US patent US5463175, (1995).
2. Sviridov, A.V., Shushkova, T.V., Zelenkova, N.F., Vinokurova, N.G., Morgunov, I.G., Ermakova, I.T. and Leontievsky, A.A. Distribution of glyphosate and methylphosphonate catabolism systems in soil bacteria Ochrobactrum anthropi and Achromobacter sp. Appl. Microbiol. Biotechnol. 93 (2012) 787-796. [PMID: 21789492]
Accepted name: sarcosine oxidase (5,10-methylenetetrahydrofolate-forming)
Reaction: sarcosine + 5,6,7,8-tetrahydrofolate + O2 = glycine + 5,10-methylenetetrahydrofolate + H2O2
Other name(s): TSOX; sarcosine oxidase (ambigious); heterotetrameric sarcosine oxidase
Systematic name: sarcosine, 5,6,7,8-tetrahydrofolate:O2 oxidoreductase (demethylating,5,10-methylenetetrahydrofolate-forming)
Comments: The enzyme, found in some bacterial species, is composed of four different subunits and two active sites connected by a large "reaction chamber". An imine intermediate is transferred between the sites, eliminating the production of toxic formaldehyde. The enzyme contains three cofactors: noncovalently bound FAD and NAD+, and FMN that is covalently bound to a histidine residue. In the absence of folate the enzyme catalyses the reaction of EC 1.5.3.1, sarcosine oxidase (formaldehyde-forming).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9029-22-5
References:
1. Hayashi, S., Nakamura, S. and Suzuki, M. Corynebacterium sarcosine oxidase: a unique enzyme having covalently-bound and noncovalently-bound flavins. Biochem. Biophys. Res. Commun. 96 (1980) 924-930. [PMID: 6158947]
2. Suzuki, M. Purification and some properties of sarcosine oxidase from Corynebacterium sp. U-96. J. Biochem. (Tokyo) 89 (1981) 599-607. [PMID: 7240129]
3. Chlumsky, L.J., Zhang, L., Ramsey, A.J. and Jorns, M.S. Preparation and properties of recombinant corynebacterial sarcosine oxidase: evidence for posttranslational modification during turnover with sarcosine. Biochemistry 32 (1993) 11132-11142. [PMID: 7692961]
4. Chlumsky, L.J., Sturgess, A.W., Nieves, E. and Jorns, M.S. Identification of the covalent flavin attachment site in sarcosine oxidase. Biochemistry 37 (1998) 2089-2095. [PMID: 9485355]
5. Eschenbrenner, M., Chlumsky, L.J., Khanna, P., Strasser, F. and Jorns, M.S. Organization of the multiple coenzymes and subunits and role of the covalent flavin link in the complex heterotetrameric sarcosine oxidase. Biochemistry 40 (2001) 5352-5367. [PMID: 11330998]
Accepted name: fructosyl amine oxidase (glucosone-forming)
Reaction: an N-(1-deoxy-D-fructos-1-yl)amine + O2 + H2O = D-glucosone + an amine + H2O2 (overall reaction)
(1a) an N-(1-deoxy-D-fructos-1-yl)amine + O2 = a 2-[(3S,4R,5R)-3,4,5,6-tetrahydroxy-2-oxohexylidene]amine + H2O2
(1b) a 2-[(3S,4R,5R)-3,4,5,6-tetrahydroxy-2-oxohexylidene]amine + H2O = D-glucosone + an amine (spontaneous)
Other name(s): amadoriase
Systematic name: N-(1-deoxy-D-fructos-1-yl)amine:oxygen 2-oxidoreductase (glucosone-forming)
Comments: Reducing sugars such as glucose react with amino groups in proteins via the spontaeous Maillard reaction, forming an unstable product that undergoes spontaneous rearrangement to a keto amine compound. These reactions are known as glycation reactions, and the stable products are known as Amadori products. This enzyme, which contains an FAD cofactor, catalyses a deglycation reaction that regenerates the amine reactant. By-products are glucosone and hydrogen peroxide. The enzymes have been reported from fungi and bacteria, but not from higher eukaryotes. Specific enzymes differ in their substrate specificity. cf. EC 1.5.3.26, fructosyl amine oxidase (fructosamine-forming).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Horiuchi, T., Kurokawa, T. and Saito, N. Purification and properties of fructosyl-amino acid oxidase from Corynebacterium sp. 2-4-1. Agr Biol Chem Tokyo 53 (1989) 103-110.
2. Takahashi, M., Pischetsrieder, M. and Monnier, V.M. Molecular cloning and expression of amadoriase isoenzyme (fructosyl amine:oxygen oxidoreductase, EC 1.5.3) from Aspergillus fumigatus. J. Biol. Chem. 272 (1997) 12505-12507. [PMID: 9139700]
3. Hirokawa, K. and Kajiyama, N. Recombinant agrobacterium AgaE-like protein with fructosyl amino acid oxidase activity. Biosci. Biotechnol. Biochem. 66 (2002) 2323-2329. [PMID: 12506967]
4. Wu, X. and Monnier, V.M. Enzymatic deglycation of proteins. Arch. Biochem. Biophys. 419 (2003) 16-24. [PMID: 14568004]
5. Sakaue, R., Nakatsu, T., Yamaguchi, Y., Kato, H. and Kajiyama, N. Crystallization and preliminary crystallographic analysis of bacterial fructosyl amino acid oxidase. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 61 (2005) 196-198. [PMID: 16510992]
Accepted name: fructosyl amine oxidase (fructosamine-forming)
Reaction: an N-(1-deoxy-D-fructos-1-yl)amine + O2 + H2O = (1-deoxy-D-fructos-1-yl)amine + an aldehyde + H2O2
Systematic name: N-(1-deoxy-D-fructos-1-yl)amine:oxygen oxidoreductase (fructosamine-forming)
Comments: Reducing sugars such as glucose react with amino groups in proteins via the spontaeous Maillard reaction, forming an unstable product that undergoes spontaneous rearrangement to a keto amine compound. These reactions are known as glycation reactions, and the stable products are known as Amadori products. This enzyme, characterized from a Pseudomonas sp. strain, cleaves the Amadori products at the alkylamine bond. All other known fructosyl amine oxidases cleave the ketoamine bond (cf. EC 1.5.3.25, fructosyl amine oxidase (glucosone-forming)).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Gerhardinger, C., Marion, M.S., Rovner, A., Glomb, M. and Monnier, V.M. Novel degradation pathway of glycated amino acids into free fructosamine by a Pseudomonas sp. soil strain extract. J. Biol. Chem. 270 (1995) 218-224. [PMID: 7814378]
2. Saxena, A.K., Saxena, P. and Monnier, V.M. Purification and characterization of a membrane-bound deglycating enzyme (1-deoxyfructosyl alkyl amino acid oxidase, EC 1.5.3) from a Pseudomonas sp. soil strain. J. Biol. Chem. 271 (1996) 32803-32809. [PMID: 8955117]
3. Wu, X. and Monnier, V.M. Enzymatic deglycation of proteins. Arch. Biochem. Biophys. 419 (2003) 16-24. [PMID: 14568004]
Accepted name: 2-(methylaminoethyl)phosphonate oxidase
Reaction: 2-(methylaminoethyl)phosphonate + O2 + H2O = phosphonoacetaldehyde + methylamine + H2O2
Other name(s): pbfD (gene name); N-methyl-(2-aminoethyl)phosphonate oxidase
Systematic name: 2-(methylaminoethyl)phosphonate oxidase:oxygen oxidoreductase (phosphonoacetaldehyde-forming)
Comments: Contaions FAD. The enzyme also acts, with lower efficiency, on 2-aminoethylphosphonate, generating phosphonoacetaldehyde and ammonia. The enzyme from Acinetobacter baumannii also transformed 2-(dimethylaminoethyl)phosphonate with appreciable efficiency, generating dimethylamine in place of methylamine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Zangelmi, E., Ruffolo, F., Dinhof, T., Gerdol, M., Malatesta, M., Chin, J.P., Rivetti, C., Secchi, A., Pallitsch, K. and Peracchi, A. Deciphering the role of recurrent FAD-dependent enzymes in bacterial phosphonate catabolism. iScience 26 (2023) 108108. [PMID: 37876809]
Accepted name: pyrimidodiazepine synthase
Reaction: 2-amino-6-acetyl-3,7,8,9-tetrahydro-3H-pyrimido[4,5-b][1,4]diazepin-4-one + glutathione disulfide + H2O = 6-pyruvoyltetrahydropterin + 2 glutathione
For diagram of reaction click here.
Glossary: 2-amino-6-acetyl-3,7,8,9-tetrahydro-3H-pyrimido[4,5-b][1,4]diazepin-4-one = pyrimidodiazepine
Other name(s): PDA synthase; pyrimidodiazepine:oxidized-glutathione oxidoreductase (ring-opening, cyclizing); pyrimidodiazepine:glutathione-disulfide oxidoreductase (ring-opening, cyclizing)
Systematic name: 2-amino-6-acetyl-3,7,8,9-tetrahydro-3H-pyrimido[4,5-b][1,4]diazepin-4-one:glutathione-disulfide oxidoreductase (ring-opening, cyclizing)
Comments: In the reverse direction, the reduction of 6-pyruvoyl-tetrahydropterin is accompanied by the opening of the 6-membered pyrazine ring and the formation of the 7-membered diazepine ring. The pyrimidodiazepine formed is an acetyldihydro derivative. Involved in the formation of the eye pigment drosopterin in Drosophila melanogaster.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 93586-06-2
References:
1. Wiederrecht, G.J. and Brown, G.M. Purification and properties of the enzymes from Drosophila melanogaster that catalyze the conversion of dihydroneopterin triphosphate to the pyrimidodiazepine precursor of the drosopterins. J. Biol. Chem. 259 (1984) 14121-14127. [PMID: 6438092]
2. Kim, J., Suh, H., Kim, S., Kim, K., Ahn, C. and Yim, J. Identification and characteristics of the structural gene for the Drosophila eye colour mutant sepia, encoding PDA synthase, a member of the ω class glutathione S-transferases. Biochem. J. 398 (2006) 451-460. [PMID: 16712527]
Accepted name: electron-transferring-flavoprotein dehydrogenase
Reaction: reduced electron-transferring flavoprotein + ubiquinone = electron-transferring flavoprotein + ubiquinol
Other name(s): ETF-QO; ETF:ubiquinone oxidoreductase; electron transfer flavoprotein dehydrogenase; electron transfer flavoprotein Q oxidoreductase; electron transfer flavoprotein-ubiquinone oxidoreductase; electron transfer flavoprotein reductase
Systematic name: electron-transferring-flavoprotein:ubiquinone oxidoreductase
Comments: An iron-sulfur flavoprotein, forming part of the mitochondrial electron-transfer system.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 86551-03-3
References:
1. Beckmann, J.D. and Frerman, F.E. Electron-transfer flavoprotein-ubiquinone oxidoreductase from pig liver: purification and molecular, redox, and catalytic properties. Biochemistry 24 (1985) 3913-3921. [PMID: 4052375]
2. Ruzicka, F.J. and Beinhert, H. A new iron-sulfur flavoprotein of the respiratory chain. A component of the fatty acid β-oxidation pathway. J. Biol. Chem. 252 (1977) 8440-8445. [PMID: 925004]
Accepted name: proline dehydrogenase
Reaction: L-proline + a quinone = (S)-1-pyrroline-5-carboxylate + a quinol
Other name(s): L-proline dehydrogenase; L-proline:(acceptor) oxidoreductase
Systematic name: L-proline:quinone oxidoreductase
Comments: A flavoprotein (FAD). The electrons from L-proline are transferred to the FAD cofactor, and from there to a quinone acceptor [3]. In many organisms, ranging from bacteria to mammals, proline is oxidized to glutamate in a two-step process involving this enzyme and EC 1.2.1.88, L-glutamate γ-semialdehyde dehydrogenase. Both activities are carried out by the same enzyme in enterobacteria.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9050-70-8
References:
1. Scarpulla, R.C. and Sofer, R.L. Membrane-bound proline dehydrogenase from Escherichia coli. Solubilization, purification, and characterization. J. Biol. Chem. 253 (1978) 5997-6001. [PMID: 355248]
2. Brown, E.D. and Wood, J.M. Redesigned purification yields a fully functional PutA protein dimer from Escherichia coli. J. Biol. Chem. 267 (1992) 13086-13092. [PMID: 1618807]
3. Moxley, M.A., Tanner, J.J. and Becker, D.F. Steady-state kinetic mechanism of the proline:ubiquinone oxidoreductase activity of proline utilization A (PutA) from Escherichia coli. Arch. Biochem. Biophys. 516 (2011) 113-120. [PMID: 22040654]
Accepted name: hydroxyproline dehydrogenase
Reaction: trans-4-hydroxy-L-proline + a quinone = (3R,5S)-3-hydroxy-1-pyrroline-5-carboxylate + a quinol
Other name(s): HYPDH; OH-POX; hydroxyproline oxidase; PRODH2 (gene name)
Systematic name: trans-4-hydroxy-L-proline:quinone oxidoreductase
Comments: A flavoprotein (FAD). The enzyme from human also has low activity with L-proline (cf. EC 1.5.5.2, proline dehydrogenase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Cooper, S.K., Pandhare, J., Donald, S.P. and Phang, J.M. A novel function for hydroxyproline oxidase in apoptosis through generation of reactive oxygen species. J. Biol. Chem. 283 (2008) 10485-10492. [PMID: 18287100]
2. Summitt, C.B., Johnson, L.C., Jonsson, T.J., Parsonage, D., Holmes, R.P. and Lowther, W.T. Proline dehydrogenase 2 (PRODH2) is a hydroxyproline dehydrogenase (HYPDH) and molecular target for treating primary hyperoxaluria. Biochem. J. 466 (2015) 273-281. [PMID: 25697095]
Accepted name: methylenetetrahydrofolate reductase (ferredoxin)
Reaction: 5-methyltetrahydrofolate + 2 oxidized ferredoxin = 5,10-methylenetetrahydrofolate + 2 reduced ferredoxin + 2 H+
For diagram of reaction click here
Other name(s): 5,10-methylenetetrahydrofolate reductase
Systematic name: 5-methyltetrahydrofolate:ferredoxin oxidoreductase
Comments: An iron-sulfur flavoprotein that also contains zinc. The enzyme from Clostridium formicoaceticum catalyses the reduction of methylene blue, menadione, benzyl viologen, rubredoxin or FAD with 5-methyltetrahydrofolate and the oxidation of reduced ferredoxin or FADH2 with 5,10-methylenetetrahydrofolate. However, unlike EC 1.5.1.53, methylenetetrahydrofolate reductase (NADPH); EC 1.5.1.54, methylenetetrahydrofolate reductase (NADH); or EC 1.5.1.20, methylenetetrahydrofolate reductase [NAD(P)H], there is no activity with either NADH or NADP.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Clark, J.E. and Ljungdahl, L.G. Purification and properties of 5,10-methylenetetrahydrofolate reductase, an iron-sulfur flavoprotein from Clostridium formicoaceticum. J. Biol. Chem. 259 (1984) 10845-10849. [PMID: 6381490]
Accepted name: coenzyme F420 oxidoreductase (ferredoxin)
Reaction: reduced coenzyme F420 + 2 oxidized ferredoxin = oxidized coenzyme F420 + 2 reduced ferredoxin + 2 H+
For diagram of reaction, click here
Glossary: oxidized coenzyme F420 = N-(N-{O-[5-(8-hydroxy-2,4-dioxo-2,3,4,10-tetrahydropyrimido[4,5-b]quinolin-10-yl)-5-deoxy-L-ribityl-1-phospho]-(S)-lactyl}-γ-L-glutamyl)-L-glutamate
Other name(s): Fd:F420 oxidoreductase; FpoF protein; ferredoxin:F420 oxidoreductase
Systematic name: coenzyme F420:ferredoxin oxidoreductase
Comments: The enzyme from the archaeon Methanosarcina mazei contains iron-sulfur centres and FAD.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Welte, C. and Deppenmeier, U. Re-evaluation of the function of the F420 dehydrogenase in electron transport of Methanosarcina mazei. FEBS J. 278 (2011) 1277-1287. [PMID: 21306561]
Accepted name: N,N-dimethylglycine/sarcosine dehydrogenase (ferredoxin)
Reaction: (1) N,N-dimethylglycine + 2 oxidized ferredoxin + H2O = sarcosine + formaldehyde + 2 reduced ferredoxin + 2 H+
(2) sarcosine + 2 oxidized ferredoxin + H2O = glycine + formaldehyde + 2 reduced ferredoxin + 2 H+
Other name(s): ddhC (gene name); dgcA (gene name)
Systematic name: N,N-dimethylglycine/sarcosine:ferredoxin oxidoreductase (demethylating)
Comments: This bacterial enzyme is involved in degradation of glycine betaine. The enzyme contains non-covalently bound FAD and NAD(P) cofactors, and catalyses the demethylation of both N,N-dimethylglycine and sarcosine, releasing formaldehyde and forming glycine as the final product. The enzyme can utilize both NAD+ and NADP+, but the catalytic efficiency with NAD+ is ~5-fold higher. The native electron acceptor of the enzyme is a membrane-bound clostridial-type ferredoxin, which transfers the electrons to an electron-transfer flavoprotein (ETF).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Wargo, M.J., Szwergold, B.S. and Hogan, D.A. Identification of two gene clusters and a transcriptional regulator required for Pseudomonas aeruginosa glycine betaine catabolism. J. Bacteriol. 190 (2008) 2690-2699. [PMID: 17951379]
2. Yang, T., Shao, Y.H., Guo, L.Z., Meng, X.L., Yu, H. and Lu, W.D. Role of N,N-dimethylglycine and its catabolism to sarcosine in Chromohalobacter salexigens DSM 3043. Appl. Environ. Microbiol. 86 (2020) . [PMID: 32631860]
Accepted name: dimethylamine dehydrogenase
Reaction: dimethylamine + H2O + electron-transfer flavoprotein = methylamine + formaldehyde + reduced electron-transferring flavoprotein
Systematic name: dimethylamine:electron-transferring flavoprotein oxidoreductase
Comments: Contains FAD and a [4Fe-4S] cluster.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, CAS registry number: 68247-64-3
References:
1. Yang, C.C., Packman, L.C. and Scrutton, N.S. The primary structure of Hyphomicrobium X dimethylamine dehydrogenase. Relationship to trimethylamine dehydrogenase and implications for substrate recognition. Eur. J. Biochem. 232 (1995) 264-271. [PMID: 7556160]
Accepted name: trimethylamine dehydrogenase
Reaction: trimethylamine + H2O + electron-transfer flavoprotein = dimethylamine + formaldehyde + reduced electron-transferring flavoprotein
Systematic name: trimethylamine:electron-transferring flavoprotein oxidoreductase (demethylating)
Comments: A number of alkyl-substituted derivatives of trimethylamine can also act as electron donors; phenazine methosulfate and 2,6-dichloroindophenol can act as electron acceptors. Contains FAD and a [4Fe-4S] cluster.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 39307-09-0
References:
1. Colby, J. and Zatman, L.J. The purification and properties of a bacterial trimethylamine dehydrogenase. Biochem. J. 121 (1971) 9P-10P.
2. Steenkamp, D.J. and Singer, T.P. Participation of the iron-sulphur cluster and of the covalently bound coenzyme of trimethylamine dehydrogenase in catalysis. Biochem. J. 169 (1978) 361-369. [PMID: 204297]
3. Huang, L.X., Rohlfs, R.J. and Hille, R. The reaction of trimethylamine dehydrogenase with electron transferring flavoprotein. J. Biol. Chem. 270 (1995) 23958-23965. [PMID: 7592591]
4. Jones, M., Talfournier, F., Bobrov, A., Grossmann, J.G., Vekshin, N., Sutcliffe, M.J. and Scrutton, N.S. Electron transfer and conformational change in complexes of trimethylamine dehydrogenase and electron transferring flavoprotein. J. Biol. Chem. 277 (2002) 8457-8465. [PMID: 11756429]
5. Scrutton, N.S. and Sutcliffe, M.J. Trimethylamine dehydrogenase and electron transferring flavoprotein. Subcell. Biochem. 35 (2000) 145-181. [PMID: 11192721]
Accepted name: sarcosine dehydrogenase
Reaction: sarcosine + 5,6,7,8-tetrahydrofolate + oxidised [electron-transfer flavoprotein] = glycine + 5,10-methylenetetrahydrofolate + reduced [electron-transfer flavoprotein]
Other name(s): sarcosine N-demethylase; monomethylglycine dehydrogenase; sarcosine:(acceptor) oxidoreductase (demethylating); sarcosine:electron-transfer flavoprotein oxidoreductase (demethylating)
Systematic name: sarcosine, 5,6,7,8-tetrahydrofolate:electron-transferflavoprotein oxidoreductase (demethylating,5,10-methylenetetrahydrofolate-forming)
Comments: A flavoprotein (FMN) found in eukaryotes. In the absence of tetrahydrofolate the enzyme produces formaldehyde. cf. EC 1.5.3.1, sarcosine oxidase (formaldehyde-forming), and EC 1.5.3.24, sarcosine oxidase (5,10-methylenetetrahydrofolate-forming).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37228-65-2, 93389-49-2
References:
1. Hoskins, D.D. and MacKenzie, C.G. Solubilization and electron transfer flavoprotein requirement of mitochondrial sarcosine dehydrogenase and dimethylglycine dehydrogenase. J. Biol. Chem. 236 (1961) 177-183. [PMID: 13716069]
2. Frisell, W.R. and MacKenzie, C.G. Separation and purification of sarcosine dehydrogenase and dimethylglycine dehydrogenase. J. Biol. Chem. 237 (1962) 94-98. [PMID: 13895406]
3. Wittwer, A.J. and Wagner, C. Identification of the folate-binding proteins of rat liver mitochondria as dimethylglycine dehydrogenase and sarcosine dehydrogenase. Flavoprotein nature and enzymatic properties of the purified proteins. J. Biol. Chem. 256 (1981) 4109-4115. [PMID: 6163778]
4. Steenkamp, D.J. and Husain, M. The effect of tetrahydrofolate on the reduction of electron transfer flavoprotein by sarcosine and dimethylglycine dehydrogenases. Biochem. J. 203 (1982) 707-715. [PMID: 6180732]
Accepted name: dimethylglycine dehydrogenase
Reaction: N,N-dimethylglycine + 5,6,7,8-tetrahydrofolate + electron-transfer flavoprotein = sarcosine + 5,10-methylenetetrahydrofolate + reduced electron-transfer flavoprotein
Glossary: sarcosine = N-methylglycine
Other name(s): N,N-dimethylglycine oxidase; N,N-dimethylglycine:(acceptor) oxidoreductase (demethylating); Me2GlyDH; N,N-dimethylglycine:electron-transfer flavoprotein oxidoreductase (demethylating)
Systematic name: N,N-dimethylglycine,5,6,7,8-tetrahydrofolate:electron-transferflavoprotein oxidoreductase (demethylating,5,10-methylenetetrahydrofolate-forming)
Comments: A flavoprotein, containing a histidyl(Nπ)-(8α)FAD linkage at position 91 in the human protein. An imine intermediate is channeled from the FAD binding site to the 5,6,7,8-tetrahydrofolate binding site through a 40 Å tunnel [5,8,9]. In the absence of 5,6,7,8-tetrahydrofolate the enzyme forms formaldehyde [5,9].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37256-30-7
References:
1. Frisell, W.R. and MacKenzie, C.G. Separation and purification of sarcosine dehydrogenase and dimethylglycine dehydrogenase. J. Biol. Chem. 237 (1962) 94-98. [PMID: 13895406]
2. Hoskins, D.D. and MacKenzie, C.G. Solubilization and electron transfer flavoprotein requirement of mitochondrial sarcosine dehydrogenase and dimethylglycine dehydrogenase. J. Biol. Chem. 236 (1961) 177-183. [PMID: 13716069]
3. Wittwer, A.J. and Wagner, C. Identification of the folate-binding proteins of rat liver mitochondria as dimethylglycine dehydrogenase and sarcosine dehydrogenase. Purification and folate-binding characteristics. J. Biol. Chem. 256 (1981) 4102-4108. [PMID: 6163777]
4. Wittwer, A.J. and Wagner, C. Identification of the folate-binding proteins of rat liver mitochondria as dimethylglycine dehydrogenase and sarcosine dehydrogenase. Flavoprotein nature and enzymatic properties of the purified proteins. J. Biol. Chem. 256 (1981) 4109-4115. [PMID: 6163778]
5. Porter, D.H., Cook, R.J. and Wagner, C. Enzymatic properties of dimethylglycine dehydrogenase and sarcosine dehydrogenase from rat liver. Arch. Biochem. Biophys. 243 (1985) 396-407. [PMID: 2417560]
6. Brizio, C., Brandsch, R., Bufano, D., Pochini, L., Indiveri, C. and Barile, M. Over-expression in Escherichia coli, functional characterization and refolding of rat dimethylglycine dehydrogenase. Protein Expr. Purif. 37 (2004) 434-442. [PMID: 15358367]
7. Brizio, C., Brandsch, R., Douka, M., Wait, R. and Barile, M. The purified recombinant precursor of rat mitochondrial dimethylglycine dehydrogenase binds FAD via an autocatalytic reaction. Int. J. Biol. Macromol. 42 (2008) 455-462. [PMID: 18423846]
8. Luka, Z., Pakhomova, S., Loukachevitch, L.V., Newcomer, M.E. and Wagner, C. Folate in demethylation: the crystal structure of the rat dimethylglycine dehydrogenase complexed with tetrahydrofolate. Biochem. Biophys. Res. Commun. 449 (2014) 392-398. [PMID: 24858690]
9. Augustin, P., Hromic, A., Pavkov-Keller, T., Gruber, K. and Macheroux, P. Structure and biochemical properties of recombinant human dimethylglycine dehydrogenase and comparison to the disease-related H109R variant. FEBS J. 283 (2016) 3587-3603. [PMID: 27486859]
Accepted name: methylenetetrahydromethanopterin dehydrogenase
Reaction: 5,10-methylenetetrahydromethanopterin + oxidized coenzyme F420 = 5,10-methenyltetrahydromethanopterin + reduced coenzyme F420
For diagram of reaction click here.
Other name(s): N5,N10-methylenetetrahydromethanopterin dehydrogenase; 5,10-methylenetetrahydromethanopterin dehydrogenase
Systematic name: 5,10-methylenetetrahydromethanopterin:coenzyme-F420 oxidoreductase
Comments: Coenzyme F420 is a 7,8-didemethyl-8-hydroxy-5-deazariboflavin derivative; methanopterin is a pterin analogue. The enzyme is involved in the formation of methane from CO2 in the methanogen Methanothermobacter thermautotrophicus.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Hartzell, P.L., Zvilius, G., Escalante-Semerena, J.C. and Donnelly, M.I. Coenzyme F420 dependence of the methylenetetrahydromethanopterin dehydrogenase of Methanobacterium thermoautotrophicum. Biochem. Biophys. Res. Commun. 133 (1985) 884-890. [PMID: 4084309]
2. te Brömmelstroet, B.W., Geerts, W.J., Keltjens, J.T., van der Drift, C. and Vogels, G.D. Purification and properties of 5,10-methylenetetrahydromethanopterin dehydrogenase and 5,10-methylenetetrahydromethanopterin reductase, two coenzyme F420-dependent enzymes, from Methanosarcina barkeri. Biochim. Biophys. Acta 1079 (1991) 293-302. [PMID: 1911853]
Accepted name: 5,10-methylenetetrahydromethanopterin reductase
Reaction: 5-methyltetrahydromethanopterin + oxidized coenzyme F420 = 5,10-methylenetetrahydromethanopterin + reduced coenzyme F420
For diagram of reaction click here.
Other name(s): 5,10-methylenetetrahydromethanopterin cyclohydrolase; N5,N10-methylenetetrahydromethanopterin reductase; methylene-H4MPT reductase; coenzyme F420-dependent N5,N10-methenyltetrahydromethanopterin reductase; N5,N10-methylenetetrahydromethanopterin:coenzyme-F420 oxidoreductase
Systematic name: 5-methyltetrahydromethanopterin:coenzyme-F420 oxidoreductase
Comments: Catalyses an intermediate step in methanogenesis from CO2 and H2 in methanogenic archaebacteria.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Ma, K. and Thauer, R.K. Purification and properties of N5,N10-methylenetetrahydromethanopterin reductase from Methanobacterium thermoautotrophicum (strain Marburg). Eur. J. Biochem. 191 (1990) 187-193. [PMID: 2379499]
2. te Brömmelstroet, B.W., Geerts, W.J., Keltjens, J.T., van der Drift, C. and Vogels, G.D. Purification and properties of 5,10-methylenetetrahydromethanopterin dehydrogenase and 5,10-methylenetetrahydromethanopterin reductase, two coenzyme F420-dependent enzymes, from Methanosarcina barkeri. Biochim. Biophys. Acta 1079 (1991) 293-302. [PMID: 1911853]
3. Ma, K. and Thauer, R.K. Single step purification of methylenetetrahydromethanopterin reductase from Methanobacterium thermoautotrophicum by specific binding to blue sepharose CL-6B. FEBS Lett. 268 (1990) 59-62. [PMID: 1696553]
4. te Brömmelstroet, B.W., Hensgens, C.M., Keltjens, J.T., van der Drift, C. and Vogels, G.D. Purification and properties of 5,10-methylenetetrahydromethanopterin reductase, a coenzyme F420-dependent enzyme, from Methanobacterium thermoautotrophicum strain ΔH*. J. Biol. Chem. 265 (1990) 1852-1857. [PMID: 2298726]
5. te Brömmelstroet, B.W., Hensgens, C.M., Geerts, W.J., Keltjens, J.T., van der Drift, C. and Vogels, G.D. Purification and properties of 5,10-methenyltetrahydromethanopterin cyclohydrolase from Methanosarcina barkeri. J. Bacteriol. 172 (1990) 564-571. [PMID: 2298699]
Accepted name: coenzyme F420:methanophenazine dehydrogenase
Reaction: reduced coenzyme F420 + methanophenazine = oxidized coenzyme F420 + dihydromethanophenazine
Glossary: methanophenazine = 2-{[(6E,10E,14E)-3,7,11,15,19-pentamethylicosa-6,10,14,18-tetraen-1-yl]oxy}phenazine
dihydromethanophenazine = 2-{[(6E,10E,14E)-3,7,11,15,19-pentamethylicosa-6,10,14,18-tetraen-1-yl]oxy}-5,10-dihydrophenazine
Other name(s): F420H2 dehydrogenase; fpoBCDIF (gene names)
Systematic name: reduced coenzyme F420:methanophenazine oxidoreductase
Comments: The enzyme, found in some methanogenic archaea, is responsible for the reoxidation of coenzyme F420, which is reduced during methanogenesis, and for the reduction of methanophenazine to dihydromethanophenazine, which is required by EC 1.8.98.1, dihydromethanophenazine:CoB-CoM heterodisulfide reductase. The enzyme is membrane-bound, and is coupled to proton translocation across the cytoplasmic membrane, generating a proton motive force that is used for ATP generation.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Brodersen, J., Gottschalk, G. and Deppenmeier, U. Membrane-bound F420H2-dependent heterodisulfide reduction in Methanococcus volta. Arch. Microbiol. 171 (1999) 115-121. [PMID: 9914308]
2. Baumer, S., Ide, T., Jacobi, C., Johann, A., Gottschalk, G. and Deppenmeier, U. The F420H2 dehydrogenase from Methanosarcina mazei is a Redox-driven proton pump closely related to NADH dehydrogenases. J. Biol. Chem. 275 (2000) 17968-17973. [PMID: 10751389]
3. Deppenmeier, U. The membrane-bound electron transport system of Methanosarcina species. J. Bioenerg. Biomembr. 36 (2004) 55-64. [PMID: 15168610]
4. Abken H. J. and Deppenmeier, U. Purification and properties of an F420H2 dehydrogenase from Methanosarcina mazei Gö1. FEMS Microbiol. Lett. 154 (2006) 231-237.
[EC 1.5.99.2 Transferred entry: dimethylglycine dehydrogenase. Now EC 1.5.8.4, dimethylglycine dehydrogenase (EC 1.5.99.2 created 1972, deleted 2012)]
Accepted name: L-pipecolate dehydrogenase
Reaction: L-pipecolate + acceptor = (S)-2,3,4,5-tetrahydropyridine-2-carboxylate + reduced acceptor
Glossary: (S)-2-amino-6-oxohexanoate = L-2-aminoadipate 6-semialdehyde = L-allysine
L-1-piperideine 6-carboxylate = (S)-2,3,4,5-tetrahydropyridine-2-carboxylate = (S)-1,6-didehydropiperidine-2-carboxylate
Other name(s): L-pipecolate:(acceptor) 1,6-oxidoreductase
Systematic name: L-pipecolate:acceptor 1,6-oxidoreductase
Comments: The product reacts with water to form 2-aminoadipate 6-semialdehyde, i.e. 2-amino-6-oxohexanoate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9076-63-5
References:
1. Baginsky, B.L. and Rodwell, V.W. Metabolism of pipecolic acid in a Pseudomonas species. V. Pipecolate oxidase and dehydrogenase. J. Bacteriol. 94 (1967) 1034-1039. [PMID: 6051341]
Accepted name: nicotine 6-hydroxylase
Reaction: (S)-nicotine + acceptor + H2O = (S)-6-hydroxynicotine + reduced acceptor
For diagram of reacion, click here
Other name(s): nicotine oxidase; D-nicotine oxidase; nicotine:(acceptor) 6-oxidoreductase (hydroxylating); L-nicotine oxidase; nicotine dehydrogenase (incorrect)
Systematic name: nicotine:acceptor 6-oxidoreductase (hydroxylating)
Comments: A metalloprotein (FMN). The enzyme can act on both the naturally found (S)-enantiomer and the synthetic (R)-enantiomer of nicotine, with retention of configuration in both cases [4].
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, CAS registry number: 37256-31-8
References:
1. Behrman, E.J. and Stanier, R.Y. The bacterial oxidation of nicotinic acid. J. Biol. Chem. 228 (1957) 923-945. [PMID: 13475371]
2. Decker, K. and Bleeg, H. Induction and purification of stereospecific nicotine oxidizing enzymes from Arthrobacter oxidans. Biochim. Biophys. Acta 105 (1965) 313-324. [PMID: 5849820]
3. Hochstein, L.I. and Dalton, B.P. The purification and properties of nicotine oxidase. Biochim. Biophys. Acta 139 (1967) 56-68. [PMID: 4962139]
4. Hochstein, L.I. and Rittenberg, S.C. The bacterial oxidation of nicotine. II. The isolation of the first oxidative product and its identification as (1)-6-hydroxynicotine. J. Biol. Chem. 234 (1959) 156-160. [PMID: 13610912]
Accepted name: methylglutamate dehydrogenase
Reaction: N-methyl-L-glutamate + acceptor + H2O = L-glutamate + formaldehyde + reduced acceptor
Other name(s): N-methylglutamate dehydrogenase; N-methyl-L-glutamate:(acceptor) oxidoreductase (demethylating)
Systematic name: N-methyl-L-glutamate:acceptor oxidoreductase (demethylating)
Comments: A number of N-methyl-substituted amino acids can act as donor; 2,6-dichloroindophenol is the best acceptor.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37217-26-8
References:
1. Hersh, L.B., Stark, M.J., Worthen, S. and Fiero, M.K. N-Methylglutamate dehydrogenase: kinetic studies on the solubilized enzyme. Arch. Biochem. Biophys. 150 (1972) 219-226. [PMID: 5028076]
Accepted name: spermidine dehydrogenase
Reaction: spermidine + acceptor + H2O = propane-1,3-diamine + 4-aminobutanal + reduced acceptor
Glossary: spermidine
Other name(s): spermidine:(acceptor) oxidoreductase
Systematic name: spermidine:acceptor oxidoreductase
Comments: A flavohemoprotein (FAD). Ferricyanide, 2,6-dichloroindophenol and cytochrome c can act as acceptor. 4-Aminobutanal condenses non-enzymically to 1-pyrroline.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9076-64-6
References:
1. Tabor, C.W. and Kellogg, P.D. Identification of flavin adenine dinucleotide and heme in a homogeneous spermidine dehydrogenase from Serratia marcescens. J. Biol. Chem. 245 (1970) 5424-5433.
2. Tabor, H. and Tabor, C.W. Biosynthesis and metabolism of 1,4-diaminobutane, spermidine, spermine, and related amines. IIE2a Speridine dehydrogenase. Adv. Enzymol. Relat. Areas Mol. Biol. 36 (1972) 225-226.
[EC 1.5.99.7 Transferred entry: now EC 1.5.8.2, trimethylamine dehydrogenase (EC 1.5.99.7 created 1976, deleted 2002)]
[EC 1.5.99.8 Transferred entry: proline dehydrogenase. Now EC 1.5.5.2, proline dehydrogenase. (EC 1.5.99.8 created 1980, transferred 2013 to 1.5.5.2, deleted 2013)]
[EC 1.5.99.9 Transferred entry: methylenetetrahydromethanopterin dehydrogenase. As the acceptor is known the enzyme has been transferred to EC 1.5.98.1, methylenetetrahydromethanopterin dehydrogenase (EC 1.5.99.9 created 1989, modified 2004, deleted 2013)]
[EC 1.5.99.10 Transferred entry: now EC 1.5.8.1, dimethylamine dehydrogenase (EC 1.5.99.10 created 1999, deleted 2002)]
[EC 1.5.99.11 Transferred entry: methylenetetrahydromethanopterin dehydrogenase. As the acceptor is known the enzyme has been transferred to EC 1.5.98.2,5,10-methylenetetrahydromethanopterin reductase (EC 1.5.99.11 created 2000, modified 2004, deleted 2013)]
Accepted name: cytokinin dehydrogenase
Reaction: N6-prenylyladenine + acceptor + H2O = adenine + 3-methylbut-2-enal + reduced acceptor
Glossary: zeatin = (E)-2-methyl-4-(9H-purin-6-ylamino)but-2-en-1-ol = (E)-N6-(4-hydroxy-3-methylbut-2-enyl)adenine
prenyl = 3-methylbut-2-en-1-yl
Other name(s): N6-dimethylallyladenine:(acceptor) oxidoreductase; 6-N-dimethylallyladenine:acceptor oxidoreductase; OsCKX2; CKX; cytokinin oxidase/dehydrogenase
Systematic name: N6-prenyladenine:acceptor oxidoreductase
Comments: A flavoprotein(FAD). Catalyses the oxidation of cytokinins, a family of N6-substituted adenine derivatives that are plant hormones, where the substituent is a prenyl group. Although this activity was previously thought to be catalysed by a hydrogen-peroxide-forming oxidase, this enzyme does not require oxygen for activity and does not form hydrogen peroxide. 2,6-Dichloroindophenol, methylene blue, nitroblue tetrazolium, phenazine methosulfate and Cu(II) in the presence of imidazole can act as acceptors. This enzyme plays a part in regulating rice-grain production, with lower levels of the enzyme resulting in enhanced grain production [2].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 55326-39-1
References:
1. Galuszka, P., Frebort, I., Sebela, M., Jacobsen, S. and Pec, P. Cytokinin oxidase or dehydrogenase? Mechanism of cytokinin degradation in plants. Eur. J. Biochem. 268 (2001) 450-461. [PMID: 11168382]
2. Ashikari, M., Sakakibara, H., Lin, S., Yamamoto, T., Takashi, T., Nishimura, A., Angeles, E.R., Qian, Q., Kitano, H. and Matsuoka, M. Cytokinin oxidase regulates rice grain production. Science 309 (2005) 741-745. [PMID: 15976269]
Accepted name: D-proline dehydrogenase
Reaction: D-proline + oxidized acceptor = 1-pyrroline-2-carboxylate + reduced acceptor
Other name(s): D-Pro DH; D-Pro dehydrogenase; dye-linked D-proline dehydrogenase
Systematic name: D-proline:acceptor oxidoreductase
Comments: A flavoprotein (FAD). The enzyme prefers D-proline and acts on other D-amino acids with lower efficiency.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Tani, Y., Tanaka, K., Yabutani, T., Mishima, Y., Sakuraba, H., Ohshima, T. and Motonaka, J. Development of a D-amino acids electrochemical sensor based on immobilization of thermostable D-proline dehydrogenase within agar gel membrane. Anal Chim Acta 619 (2008) 215-220. [PMID: 18558115]
2. Satomura, T., Kawakami, R., Sakuraba, H. and Ohshima, T. Dye-linked D-proline dehydrogenase from hyperthermophilic archaeon Pyrobaculum islandicum is a novel FAD-dependent amino acid dehydrogenase. J. Biol. Chem. 277 (2002) 12861-12867. [PMID: 11823469]
Accepted name: 6-hydroxypseudooxynicotine dehydrogenase
Reaction: 1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + acceptor + H2O = 1-(2,6-dihydroxypyridin-3-yl)-4-(methylamino)butan-1-one + reduced acceptor
For diagram of reaction click here.
Glossary: 1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one = 6-hydroxypseudooxynicotine
1-(2,6-dihydroxypyridin-3-yl)-4-(methylamino)butan-1-one = 2,6-dihydroxypseudooxynicotine
Systematic name: 1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one:acceptor 6-oxidoreductase (hydroxylating)
Comments: Contains a cytidylyl molybdenum cofactor [3]. The enzyme, which participates in the nicotine degradation pathway, has been characterized from the soil bacterium Arthrobacter nicotinovorans [1,2].
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Freudenberg, W., Konig, K. and Andreesen, J. R. Nicotine dehydrogenase from Arthrobacter oxidans: A molybdenum-containing hydroxylase. FEMS Microbiology Letters 52 (1988) 13-18.
2. Grether-Beck, S., Igloi, G.L., Pust, S., Schilz, E., Decker, K. and Brandsch, R. Structural analysis and molybdenum-dependent expression of the pAO1-encoded nicotine dehydrogenase genes of Arthrobacter nicotinovorans. Mol. Microbiol. 13 (1994) 929-936. [PMID: 7815950]
3. Sachelaru, P., Schiltz, E. and Brandsch, R. A functional mobA gene for molybdopterin cytosine dinucleotide cofactor biosynthesis is required for activity and holoenzyme assembly of the heterotrimeric nicotine dehydrogenases of Arthrobacter nicotinovorans. Appl. Environ. Microbiol. 72 (2006) 5126-5131. [PMID: 16820521]
Accepted name: dihydromethanopterin reductase (acceptor)
Reaction: 5,6,7,8-tetrahydromethanopterin + oxidized acceptor = 7,8-dihydromethanopterin + reduced acceptor
For diagram of reaction click here.
Other name(s): DmrX
Systematic name: 5,6,7,8-tetrahydromethanopterin:acceptor 5,6-oxidoreductase
Comments: This archaeal enzyme catalyses the last step in the biosynthesis of tetrahydromethanopterin, a coenzyme used in methanogenesis. The enzyme, characterized from the archaea Methanosarcina mazei and Methanocaldococcus jannaschii, is an iron-sulfur flavoprotein. cf. EC 1.5.1.47, dihydromethanopterin reductase [NAD(P)+].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Wang, S., Tiongson, J. and Rasche, M.E. Discovery and characterization of the first archaeal dihydromethanopterin reductase, an iron-sulfur flavoprotein from Methanosarcina mazei. J. Bacteriol. 196 (2014) 203-209. [PMID: 23995635]
Accepted name: 2-(methylaminoethyl)phosphonate dehydrogenase (acceptor)
Reaction: 2-(methylaminoethyl)phosphonate + acceptor + H2O = phosphonoacetaldehyde + methylamine + reduced acceptor
Other name(s): pbfC (gene name); N-methyl-2-aminoethylphosphonate dehydrogenase (acceptor)
Systematic name: 2-(methylaminoethyl)phosphonate:acceptor oxidoreductase (phosphonoacetaldehyde-forming)
Comments: Contains FAD. The enzyme from the bacterium Azospirillum sp. B510 reacts about tenfold less efficiently with 2-(ethylaminoethyl)phosphonate and about 400-fold less efficiently with (2-aminoethyl)phosphonate. Oxygen is used poorly as an electron acceptor (at least 50-fold less efficiently than the artificial acceptor DCPIP). The physiological electron acceptor is unknown.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Zangelmi, E., Ruffolo, F., Dinhof, T., Gerdol, M., Malatesta, M., Chin, J.P., Rivetti, C., Secchi, A., Pallitsch, K. and Peracchi, A. Deciphering the role of recurrent FAD-dependent enzymes in bacterial phosphonate catabolism. iScience 26 (2023) 108108. [PMID: 37876809]