EC 1.14.13.242 - 3-hydroxy-2-methylpyridine-5-carboxylate monooxygenase

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IntEnz Enzyme Nomenclature
EC 1.14.13.242

Names

Accepted name:
3-hydroxy-2-methylpyridine-5-carboxylate monooxygenase
Other names:
2-methyl-3-hydroxypyridine 5-carboxylic acid dioxygenase [incorrect]
3-hydroxy-3-methylpyridinecarboxylate dioxygenase [incorrect]
methylhydroxypyridine carboxylate dioxygenase [incorrect]
methylhydroxypyridinecarboxylate oxidase [misleading]
3-hydroxy-2-methylpyridine-5-carboxylate,NAD(P)H:oxygen oxidoreductase (decyclizing)
MHPCO
3-hydroxy-2-methylpyridinecarboxylate dioxygenase [incorrect]
Systematic name:
3-hydroxy-2-methylpyridine-5-carboxylate,NAD(P)H:oxygen oxidoreductase (ring-opening)

Reaction

Cofactor

Comments:

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 monooxygnase, 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.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ERGO , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0047081
CAS Registry Number: 37256-69-2

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 : 2590-2600 (1969). [PMID: 4306031]
  2. Chaiyen, P., Ballou, D. P., 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 : 7233-7238 (1997). [PMID: 9207074]
  3. 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 : 312-314 (2005). [PMID: 16511028]
  4. 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 : 504-510 (2006). [PMID: 17270714]
  5. McCulloch, K. M., Mukherjee, T., Begley, T. P., Ealick, S. E.
    Structure of the PLP degradative enzyme 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase from Mesorhizobium loti MAFF303099 and its mechanistic implications.
    Biochemistry 48 : 4139-4149 (2009). [PMID: 19317437]
  6. Tian, B., Tu, Y., Strid, A., Eriksson, L. A.
    Hydroxylation and ring-opening mechanism of an unusual flavoprotein monooxygenase, 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase: a theoretical study.
    Chemistry 16 : 2557-2566 (2010). [PMID: 20066695]
  7. Tian, B., Strid, A., Eriksson, L. A.
    Catalytic roles of active-site residues in 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase: an ONIOM/DFT study.
    J Phys Chem B 115 : 1918-1926 (2011). [PMID: 21291225]

[EC 1.14.13.242 created 2018 (EC 1.14.12.4 created 1972, transferred 2018)]