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 1.5.99 With other acceptors
Accepted name: pyrroline-2-carboxylate reductase
Reaction: L-proline + NAD(P)+ = 1-pyrroline-2-carboxylate + NAD(P)H + H+
Other name(s): δ1-pyrroline-2-carboxylate reductase
Systematic name: L-proline:NAD(P)+ 2-oxidoreductase
Comments: Reduces 1-pyrroline-2-carboxylate to L-proline and also 1,2-didehydropiperidine-2-carboxylate to L-pipecolate.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, 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.
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, 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, 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]
Accepted name: 1-pyrroline-5-carboxylate dehydrogenase
Reaction: (S)-1-pyrroline-5-carboxylate + NAD(P)+ + 2 H2O = L-glutamate + NAD(P)H + H+
For diagram of reaction, click here
Other name(s): Δ1-pyrroline-5-carboxylate dehydrogenase; 1-pyrroline dehydrogenase; pyrroline-5-carboxylate dehydrogenase; pyrroline-5-carboxylic acid dehydrogenase; L-pyrroline-5-carboxylate-NAD+ oxidoreductase; 1-pyrroline-5-carboxylate:NAD+ oxidoreductase; Δ1-pyrroline-5-carboxylic acid dehydrogenase
Systematic name: (S)-1-pyrroline-5-carboxylate:NAD+ oxidoreductase
Comments: This enzyme can oxidize a number of 1-pyrrolines, e.g. 3-hydroxy-1-pyrroline-5-carboxylate is converted into 4-hydroxyglutamate and (R)-1-pyrroline-5-carboxylate is converted into D-glutamate. While NAD+ appears to be the better electron acceptor, NADP+ can also act, but more slowly [1,3]. In many organisms, ranging from bacteria to mammals, proline is oxidized to glutamate in a two-step process involving this enzyme and EC 1.5.99.8, proline dehydrogenase [3]. In many bacterial species, both activities are carried out by a single bifunctional enzyme [3,4].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9054-82-4
References:
1. Adams, E. and Goldstone, A. Hydroxyproline metabolism. IV. Enzymatic synthesis of γ-hydroxyglutamate from Δ1-pyrroline-3-hydroxy-5-carboxylate. J. Biol. Chem. 235 (1960) 3504-3512. [PMID: 13681370]
2. Strecker, H.J. The interconversion of glutamic acid and proline. III. Δ1-Pyrroline-5-carboxylic acid dehydrogenase. J. Biol. Chem. 235 (1960) 3218-3223.
3. Forlani, G., Scainelli, D. and Nielsen, E. Δ1-Pyrroline-5-carboxylate dehydrogenase from cultured cells of potato (purification and properties). Plant Physiol. 113 (1997) 1413-1418. [PMID: 12223682]
4. 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]
5. Inagaki, E., Ohshima, N., Sakamoto, K., Babayeva, N.D., Kato, H., Yokoyama, S. and Tahirov, T.H. New insights into the binding mode of coenzymes: structure of Thermus thermophilus Δ1-pyrroline-5-carboxylate dehydrogenase complexed with NADP+. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 63:462 (2007). [PMID: 17554163]
[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; 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 and for its place in C1 metabolism, click here
Other name(s): methylenetetrahydrofolate (reduced nicotinamide adenine dinucleotide phosphate) reductase; 5,10-methylenetetrahydrofolate reductase (NADPH); 5,10-methylenetetrahydrofolic acid reductase; 5,10-CH2-H4folate reductase; methylenetetrahydrofolate reductase (NADPH2); 5-methyltetrahydrofolate:NAD oxidoreductase; 5-methyltetrahydrofolate:NAD+ oxidoreductase; methylenetetrahydrofolate (reduced riboflavin adenine dinucleotide) reductase; 5,10-methylenetetrahydrofolate reductase; methylenetetrahydrofolate reductase; N5,10-methylenetetrahydrofolate reductase; 5,10-methylenetetrahydropteroylglutamate reductase; N5,N10-methylenetetrahydrofolate reductase; methylenetetrahydrofolic acid reductase; 5-methyltetrahydrofolate:(acceptor) oxidoreductase (incorrect); 5,10-methylenetetrahydrofolate reductase (FADH2); MetF; methylenetetrahydrofolate reductase (NADPH); 5-methyltetrahydrofolate:NADP+ oxidoreductase
Systematic name: 5-methyltetrahydrofolate:NAD(P)+ oxidoreductase
Comments: A flavoprotein (FAD). Menadione can also serve as an electron acceptor.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 71822-25-8
References:
1. 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]
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. 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]
4. 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]
Accepted name: δ1-piperideine-2-carboxylate reductase
Reaction: L-pipecolate + NADP+ = δ1-piperideine-2-carboxylate + NADPH + H+
Other name(s): 1,2-didehydropipecolate reductase; P2C reductase; 1,2-didehydropipecolic reductase
Systematic name: L-pipecolate:NADP+ 2-oxidoreductase
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]
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: 1,2-dihydrovomilenine + NADP+ = vomilenine + NADPH + H+
For diagram click here.
Systematic name: 1,2-dihydrovomilenine:NADP+ oxidoreductase
Comments: Forms part of 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]
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+ = 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, 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]
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)
Accepted name: sarcosine oxidase
Reaction: sarcosine + H2O + O2 = glycine + formaldehyde + H2O2
Systematic name: sarcosine:oxygen oxidoreductase (demethylating)
Comments: A flavoprotein (FAD). The flavin is both covalently and non-covalently bound in a molar ratio of 1:1.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, 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. 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.
3. Suzuki, M. Purification and some properties of sarcosine oxidase from Corynebacterium sp. U-96. J. Biochem. (Tokyo) 89 (1981) 599-607. [PMID: 7240129]
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
For diagram of reaction click here.
Other name(s): L-6-hydroxynicotine oxidase; 6-hydroxy-L-nicotine oxidase; 6-hydroxy-L-nicotine:oxygen oxidoreductase
Systematic name: (S)-6-hydroxynicotine:oxygen oxidoreductase
Comments: A flavoprotein (FAD).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 37256-29-4
References:
1. 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]
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]
Accepted name: (R)-6-hydroxynicotine oxidase
Reaction: (R)-6-hydroxynicotine + H2O + O2 = 1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2
For diagram of reaction click here.
Other name(s): D-6-hydroxynicotine oxidase; 6-hydroxy-D-nicotine oxidase
Systematic name: (R)-6-hydroxynicotine:oxygen oxidoreductase
Comments: A flavoprotein (FAD).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 37233-46-8
References:
1. 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]
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]
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 + H2O + O2 = sarcosine + formaldehyde + H2O2
Systematic name: N,N-dimethylglycine:oxygen oxidoreductase (demethylating)
Comments: A flavoprotein (FAD). Does not oxidize sarcosine.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, 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.
[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, 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; 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, 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, EXPASY, KEGG, Metacyc, UM-BBD, 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, EXPASY, KEGG, Metacyc, UM-BBD, 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: pyrimidodiazepine synthase
Reaction: a pyrimidodiazepine + glutathione disulfide + H2O = 6-pyruvoyltetrahydropterin + 2 glutathione
Other name(s): PDA synthase; pyrimidodiazepine:oxidized-glutathione oxidoreductase (ring-opening, cyclizing)
Systematic name: pyrimidodiazepine:glutathione-disulfide oxidoreductase (ring-opening, cyclizing)
Comments: In the reverse direction of reaction, 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 involved 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.
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: methylenetetrahydrofolate reductase (ferredoxin)
Reaction: 5-methyltetrahydrofolate + 2 oxidized ferredoxin = 5,10-methylenetetrahydrofolate + 2 reduced ferredoxin + 2 H+
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 1.5.1.20, methylenetetrahydrofolate reductase [NAD(P)H], there is no activity with NAD(P)H.
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: 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, EXPASY, KEGG, Metacyc, UM-BBD, 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, EXPASY, KEGG, Metacyc, PDB, UM-BBD, 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 + H2O + electron-transfer flavoprotein = glycine + formaldehyde + reduced electron-transfer flavoprotein
Other name(s): sarcosine N-demethylase; monomethylglycine dehydrogenase; sarcosine:(acceptor) oxidoreductase (demethylating)
Systematic name: sarcosine:electron-transfer flavoprotein oxidoreductase (demethylating)
Comments: A flavoprotein (FMN). Tetrahydrofolate is also a substrate, being converted to N5,N10-methylenetetrahydrofolate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
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. 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 + electron-transfer flavoprotein + H2O = sarcosine + formaldehyde + reduced electron-transfer flavoprotein
Other name(s): N,N-dimethylglycine oxidase; N,N-dimethylglycine:(acceptor) oxidoreductase (demethylating); Me2GlyDH
Systematic name: N,N-dimethylglycine:electron-transfer flavoprotein oxidoreductase (demethylating)
Comments: A flavoprotein, containing a histidyl(N3)-(8α)FAD linkage
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
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. 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]
4. 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]
EC 1.5.99.13 D-proline dehydrogenase
EC 1.5.99.14 6-hydroxypseudooxynicotine dehydrogenase
[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 dehydrogenase
Reaction: (S)-nicotine + acceptor + H2O = (S)-6-hydroxynicotine + reduced acceptor
For diagram of reaction click here.
Other name(s): nicotine oxidase; D-nicotine oxidase; nicotine:(acceptor) 6-oxidoreductase (hydroxylating)
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, EXPASY, KEGG, Metacyc, UM-BBD, 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, 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)]
Accepted name: proline dehydrogenase
Reaction: L-proline + acceptor = (S)-1-pyrroline-5-carboxylate + reduced acceptor
Other name(s): L-proline dehydrogenase; L-proline:(acceptor) oxidoreductase
Systematic name: L-proline:acceptor oxidoreductase
Comments: A flavoprotein (FAD). In many organisms, ranging from bacteria to mammals, proline is oxidized to glutamate in a two-step process involving this enzyme and EC 1.5.1.12, 1-pyrroline-5-carboxylate dehydrogenase [2]. Both activities are carried out by the same enzyme in enterobacteria [2,3].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, 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. Forlani, G., Scainelli, D. and Nielsen, E. Δ1-Pyrroline-5-carboxylate dehydrogenase from cultured cells of potato (purification and properties). Plant Physiol. 113 (1997) 1413-1418. [PMID: 12223682]
3. 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]
Accepted name: methylenetetrahydromethanopterin dehydrogenase
Reaction: 5,10-methylenetetrahydromethanopterin + coenzyme F420 = 5,10-methenyltetrahydromethanopterin + reduced coenzyme F420
For diagram of reaction click here
Glossary: coenzyme F420
tetrahydromethanopterin
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 Methanobacterium thermoautotrophicum.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: 100357-01-5
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]
[EC 1.5.99.10 Transferred entry: now EC 1.5.8.1, dimethylamine dehydrogenase (EC 1.5.99.10 created 1999, deleted 2002)]
Accepted name: 5,10-methylenetetrahydromethanopterin reductase
Reaction: 5-methyltetrahydromethanopterin + coenzyme F420 = 5,10-methylenetetrahydromethanopterin + reduced coenzyme F420
For diagram of reaction click here.
Glossary: coenzyme F420
tetrahydromethanopterin
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 bacteria.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, 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: cytokinin dehydrogenase
Reaction: N6-dimethylallyladenine + 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
Other name(s): N6-dimethylallyladenine:(acceptor) oxidoreductase; 6-N-dimethylallyladenine:acceptor oxidoreductase; OsCKX2; CKX; cytokinin oxidase/dehydrogenase
Systematic name: N6-dimethylallyladenine: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 dimethylallyl or other 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, EXPASY, KEGG, Metacyc, UM-BBD, 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]