3-hydroxy-2-methylpyridinecarboxylate dioxygenase

In enzymology, a 3-hydroxy-2-methylpyridinecarboxylate dioxygenase (EC 1.14.12.4) is an enzyme that catalyzes the chemical reaction

3-hydroxy-2-methylpyridinecarboxylate dioxygenase
Identifiers
EC no.1.14.12.4
CAS no.37256-69-2
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
3-hydroxy-2-methylpyridine-5-carboxylate + NAD(P)H + H+ + O2 2-(acetamidomethylene)succinate + NAD(P)+

The 5 substrates of this enzyme are 3-hydroxy-2-methylpyridine-5-carboxylate, NADH, NADPH, H+, and O2, whereas its 3 products are 2-(acetamidomethylene)succinate, NAD+, and NADP+.

This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of two atoms of oxygen into the other donor. The systematic name of this enzyme class is 3-hydroxy-2-methylpyridine-5-carboxylate,NAD(P)H:oxygen oxidoreductase (decyclizing). Other names in common use include methylhydroxypyridinecarboxylate oxidase, 2-methyl-3-hydroxypyridine 5-carboxylic acid dioxygenase, methylhydroxypyridine carboxylate dioxygenase, and 3-hydroxy-3-methylpyridinecarboxylate dioxygenase [incorrect]. This enzyme participates in vitamin B6 metabolism. It employs one cofactor, FAD.

References edit

  • Sparrow LG, Ho PP, Sundaram TK, Zach D, Nyns EJ, Snell EE (1969). "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 (10): 2590–600. PMID 4306031.