EC |
1.1.99.42 |
Accepted name: |
4-pyridoxic acid dehydrogenase |
Reaction: |
4-pyridoxate + acceptor = 5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate + reduced acceptor |
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For diagram of pyridoxal catabolism, click here |
Glossary: |
4-pyridoxate = 3-hydroxy-5-(hydroxymethyl)-2-methylpyridine-4-carboxylate
dichloroindophenol = DCPIP = 2,6-dichloro-4-[(4-hydroxyphenyl)imino]cyclohexa-2,5-dien-1-one |
Other name(s): |
mlr6792 (locus name) |
Systematic name: |
4-pyridoxate:acceptor 5-oxidoreductase |
Comments: |
The enzyme, characterized from the bacteria Pseudomonas sp. MA-1 and Mesorhizobium loti, participates in the degradation of pyridoxine (vitamin B6). It is membrane bound and contains FAD. The enzyme has been assayed in vitro in the presence of the artificial electron acceptor dichloroindophenol (DCPIP). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Yagi, T., Kishore, G.M. and Snell, E.E. The bacterial oxidation of vitamin B6. 4-Pyridoxic acid dehydrogenase: a membrane-bound enzyme from Pseudomonas MA-1. J. Biol. Chem. 258 (1983) 9419–9425. [PMID: 6348042] |
2. |
Ge, F., Yokochi, N., Yoshikane, Y., Ohnishi, K. and Yagi, T. Gene identification and characterization of the pyridoxine degradative enzyme 4-pyridoxic acid dehydrogenase from the nitrogen-fixing symbiotic bacterium Mesorhizobium loti MAFF303099. J. Biochem. 143 (2008) 603–609. [DOI] [PMID: 18216065] |
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[EC 1.1.99.42 created 2018] |
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EC |
1.2.3.8 |
Accepted name: |
pyridoxal oxidase |
Reaction: |
pyridoxal + H2O + O2 = 4-pyridoxate + (?) |
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For diagram of pyridoxal catabolism, click here |
Systematic name: |
pyridoxal:oxygen 4-oxidoreductase |
Comments: |
A molybdenum protein. |
Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 76415-81-1 |
References: |
1. |
Hanly, E.W. Preliminary characterization and physical properties of pyridoxal oxidase activity from Drosophila melanogaster. Mol. Gen. Genet. 180 (1980) 455–462. |
2. |
Warner, C.K., Watts, D.T. and Finnerty, V. Molybdenum hydroxylases in Drosophila. I. Preliminary studies of pyridoxal oxidase. Mol. Gen. Genet. 180 (1980) 449–453. |
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[EC 1.2.3.8 created 1984] |
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EC |
3.1.1.27 |
Accepted name: |
4-pyridoxolactonase |
Reaction: |
4-pyridoxolactone + H2O = 4-pyridoxate |
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For diagram of pyridoxal catabolism, click here |
Systematic name: |
4-pyridoxolactone lactonohydrolase |
Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37278-41-4 |
References: |
1. |
Burg, R.W. and Snell, E.E. The bacterial oxidation of vitamin B6. VI. Pyridoxal dehydrogenase and 4-pyridoxolactonase. J. Biol. Chem. 244 (1969) 2585–2589. [PMID: 4306030] |
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[EC 3.1.1.27 created 1972] |
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