The Enzyme Database

Your query returned 1 entry.    printer_iconPrintable version

EC 1.14.13.241     
Accepted name: 5-pyridoxate monooxygenase
Reaction: 3-hydroxy-4-hydroxymethyl-2-methylpyridine-5-carboxylate + NADPH + H+ + O2 = 2-(acetamidomethylene)-3-(hydroxymethyl)succinate + NADP+
Glossary: 3-hydroxy-4-hydroxymethyl-2-methylpyridine-5-carboxylate = 5-pyridoxate
Other name(s): 5-pyridoxate,NADPH:oxygen oxidoreductase (decyclizing); 5-pyridoxate oxidase (misleading); 5-pyridoxate dioxygenase (incorrect)
Systematic name: 5-pyridoxate,NADPH:oxygen oxidoreductase (ring-opening)
Comments: Contains FAD. The enzyme, characterized from the bacterium Arthrobacter sp. Cr-7, participates in the degradation of pyridoxine (vitamin B6). Although the enzyme was initially thought to be a dioxygenase, oxygen-tracer experiments have suggested that it is a monooxygenase, incorporating only one oxygen atom from molecular oxygen into the product. The second oxygen atom originates from a water molecule, which is regenerated during the reaction and thus does not show up in the reaction equation.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD, CAS registry number: 37256-70-5
References:
1.  Sparrow, L.G., Ho, P.P.K., Sundaram, T.K., Zach, D., Nyns, E.J. and Snell, E.E. The bacterial oxidation of vitamin B6. VII. Purification, properties, and mechanism of action of an oxygenase which cleaves the 3-hydroxypyridine ring. J. Biol. Chem. 244 (1969) 2590–2600. [PMID: 4306031]
2.  Nelson, M.J. and Snell, E.E. Enzymes of vitamin B6 degradation. Purification and properties of 5-pyridoxic-acid oxygenase from Arthrobacter sp. J. Biol. Chem 261 (1986) 15115–15120. [PMID: 3771566]
3.  Chaiyen, P. Flavoenzymes catalyzing oxidative aromatic ring-cleavage reactions. Arch. Biochem. Biophys. 493 (2010) 62–70. [DOI] [PMID: 19728986]
[EC 1.14.13.241 created 2018 (EC 1.14.12.5 created 1972, incorporated 2018)]
 
 


Data © 2001–2019 IUBMB
Web site © 2005–2019 Andrew McDonald