Species: Pseudomonas sp. MA-1
2-methyl-3-hydroxypyridine-5-carboxylate oxygenase has been purified from Pseudomonas sp. MA-1 and characterized [Sparrow69, Burg70]. The enzyme contains 2 moles of FAD per mole protein, and FMN cannot substitute [Sparrow69]. It is also highly specific for 3-hydroxy-2-methylpyridine-5-carboxylate, and molecular oxygen cannot be replaced by oxidized DCPIP. The enzyme is sensitive to oxidation, and loses activity reapidly in the absence of a reducing agent such as mercaptopethanol. Both NADH and NADPH can be used for reduction of the FAD-enzyme complex [Sparrow69].
Molecular Weight of Polypeptide: 166 kD (experimental) [Sparrow69 ]
Enzymatic reaction of: 2-methyl-3-hydroxypyridine-5-carboxylate oxygenase
Synonyms: 3-hydroxy-2-methylpyridine-5-carboxylate oxygenase
EC Number: 188.8.131.52
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
The reaction is physiologically favored in the direction shown.
Alternative Substrates for 3-hydroxy-2-methylpyridine-5-carboxylate: 3-hydroxy-4-hydroxymethyl-2-methylpyridine-5-carboxylate [Sparrow69 ]
In Pathways: vitamin B6 degradation
Inhibitors (Competitive): 3-hydroxy-4-hydroxymethyl-2-methylpyridine-5-carboxylate [Burg70] , 6-methylnicotinate [Burg70]
pH(opt): 6.5-8 [Sparrow69]
Sparrow69: 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
©2014 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493