KEGG   ENZYME: 1.14.13.242Help
Entry
EC 1.14.13.242              Enzyme                                 

Name
3-hydroxy-2-methylpyridine-5-carboxylate monooxygenase;
MHPCO;
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)
Class
Oxidoreductases;
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
BRITE hierarchy
Sysname
3-hydroxy-2-methylpyridine-5-carboxylate,NAD(P)H:oxygen oxidoreductase (ring-opening)
Reaction(IUBMB)
3-hydroxy-2-methylpyridine-5-carboxylate + NAD(P)H + H+ + O2 = 2-(acetamidomethylidene)succinate + NAD(P)+ [RN:R03385 R03386]
Reaction(KEGG)
Substrate
3-hydroxy-2-methylpyridine-5-carboxylate [CPD:C01270];
NADH [CPD:C00004];
NADPH [CPD:C00005];
H+ [CPD:C00080];
O2 [CPD:C00007]
Product
2-(acetamidomethylidene)succinate [CPD:C01215];
NAD+ [CPD:C00003];
NADP+ [CPD:C00006]
Comment
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.
History
EC 1.14.13.242 created 2018 (EC 1.14.12.4 created 1972, incorporated 2018)
Pathway
ec00750  Vitamin B6 metabolism
ec01120  Microbial metabolism in diverse environments
Orthology
K18071  2-methyl-3-hydroxypyridine 5-carboxylic acid dioxygenase
Genes
MLO: mlr6788
MLN: A9174_14020
MAM: Mesau_02080
Taxonomy
Reference
1  [PMID:4306031]
  Authors
Sparrow LG, Ho PP, Sundaram TK, Zach D, Nyns EJ, Snell EE.
  Title
The bacterial oxidation of vitamin B6. VII. Purification, properties, and mechanism of action of an oxygenase which cleaves the 3-hydroxypyridine ring.
  Journal
J Biol Chem 244:2590-600 (1969)
  Sequence
Reference
2  [PMID:9207074]
  Authors
Chaiyen P, Ballou DP, Massey V
  Title
Gene cloning, sequence analysis, and expression of 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase.
  Journal
Proc Natl Acad Sci U S A 94:7233-8 (1997)
DOI:10.1073/pnas.94.14.7233
  Sequence
Reference
3  [PMID:16511028]
  Authors
Oonanant W, Sucharitakul J, Yuvaniyama J, Chaiyen P
  Title
Crystallization and preliminary X-ray crystallographic analysis of 2-methyl-3-hydroxypyridine-5-carboxylic acid (MHPC) oxygenase from Pseudomonas sp. MA-1.
  Journal
Acta Crystallogr Sect F Struct Biol Cryst Commun 61:312-4 (2005)
DOI:10.1107/S1744309105004367
Reference
4  [PMID:17270714]
  Authors
Yuan B, Yokochi N, Yoshikane Y, Ohnishi K, Yagi T
  Title
Molecular cloning, identification and characterization of 2-methyl-3-hydroxypyridine-5-carboxylic-acid-dioxygenase-coding gene from the nitrogen-fixing symbiotic bacterium Mesorhizobium loti.
  Journal
J Biosci Bioeng 102:504-10 (2006)
DOI:10.1263/jbb.102.504
  Sequence
[mlo:mlr6788]
Reference
5  [PMID:19317437]
  Authors
McCulloch KM, Mukherjee T, Begley TP, Ealick SE
  Title
Structure of the PLP degradative enzyme 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase from Mesorhizobium loti MAFF303099 and its mechanistic implications.
  Journal
Biochemistry 48:4139-49 (2009)
DOI:10.1021/bi900149f
  Sequence
[mlo:mlr6788]
Reference
6  [PMID:20066695]
  Authors
Tian B, Tu Y, Strid A, Eriksson LA
  Title
Hydroxylation and ring-opening mechanism of an unusual flavoprotein monooxygenase, 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase: a theoretical study.
  Journal
Chemistry 16:2557-66 (2010)
DOI:10.1002/chem.200902253
Reference
7  [PMID:21291225]
  Authors
Tian B, Strid A, Eriksson LA
  Title
Catalytic roles of active-site residues in 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase: an ONIOM/DFT study.
  Journal
J Phys Chem B 115:1918-26 (2011)
DOI:10.1021/jp111525p
Other DBs
ExplorEnz - The Enzyme Database: 1.14.13.242
IUBMB Enzyme Nomenclature: 1.14.13.242
ExPASy - ENZYME nomenclature database: 1.14.13.242
BRENDA, the Enzyme Database: 1.14.13.242
CAS: 37256-69-2

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