EC 184.108.40.206 Enzyme
3-hydroxy-2-methylpyridine-5-carboxylate,NAD(P)H:oxygen oxidoreductase (decyclizing);
methylhydroxypyridinecarboxylate oxidase (misleading);
2-methyl-3-hydroxypyridine 5-carboxylic acid dioxygenase (incorrect);
methylhydroxypyridine carboxylate dioxygenase (incorrect);
3-hydroxy-3-methylpyridinecarboxylate dioxygenase [incorrect];
3-hydroxy-2-methylpyridinecarboxylate dioxygenase (incorrect)
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor
3-hydroxy-2-methylpyridine-5-carboxylate,NAD(P)H:oxygen oxidoreductase (ring-opening)
3-hydroxy-2-methylpyridine-5-carboxylate + NAD(P)H + H+ + O2 = 2-(acetamidomethylidene)succinate + NAD(P)+ [RN:
Contains FAD. The enzyme, characterized from the bacteria Pseudomonas sp. MA-1 and Mesorhizobium loti, participates in the degradation of pyridoxine (vitamin B6). Although the enzyme was initially thought to be a dioxygenase, oxygen-tracer experiments have shown that it is a monooxygenase, incorporating only one oxygen atom from molecular oxygen. The second oxygen atom that is incorporated into the product originates from a water molecule, which is regenerated during the reaction and thus does not show up in the reaction equation.
EC 220.127.116.11 created 2018 (EC 18.104.22.168 created 1972, incorporated 2018)
Vitamin B6 metabolism
Microbial metabolism in diverse environments
2-methyl-3-hydroxypyridine 5-carboxylic acid dioxygenase
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Sparrow LG, Ho PP, Sundaram TK, Zach D, Nyns EJ, Snell EE
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 244:2590-600 (1969)
Chaiyen P, Ballou DP, Massey V
Gene cloning, sequence analysis, and expression of 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase.
Proc Natl Acad Sci U S A 94:7233-8 (1997)
Oonanant W, Sucharitakul J, Yuvaniyama J, Chaiyen P
Crystallization and preliminary X-ray crystallographic analysis of 2-methyl-3-hydroxypyridine-5-carboxylic acid (MHPC) oxygenase from Pseudomonas sp. MA-1.
Acta Crystallogr Sect F Struct Biol Cryst Commun 61:312-4 (2005)
Yuan B, Yokochi N, Yoshikane Y, Ohnishi K, Yagi T
Molecular cloning, identification and characterization of 2-methyl-3-hydroxypyridine-5-carboxylic-acid-dioxygenase-coding gene from the nitrogen-fixing symbiotic bacterium Mesorhizobium loti.
J Biosci Bioeng 102:504-10 (2006)
McCulloch KM, Mukherjee T, Begley TP, Ealick SE
Structure of the PLP degradative enzyme 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase from Mesorhizobium loti MAFF303099 and its mechanistic implications.
Biochemistry 48:4139-49 (2009)
Tian B, Tu Y, Strid A, Eriksson LA
Hydroxylation and ring-opening mechanism of an unusual flavoprotein monooxygenase, 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase: a theoretical study.
Chemistry 16:2557-66 (2010)
Tian B, Strid A, Eriksson LA
Catalytic roles of active-site residues in 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase: an ONIOM/DFT study.
J Phys Chem B 115:1918-26 (2011)
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