KEGG ENZYME: 1.14.13.242

ENZYME: 1.14.13.242

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

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)

R03385 R03386

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

XYG:	R9X41_02015

MLO:

mlr6788

MLN:	A9174_14020

MAM:	Mesau_02080

MESP:

C1M53_04625

MHUA:

MCHK_0410

MJR:	EB229_14135

MERD:

EB233_10985

MLG:	CWB41_10065

MEY:	TM49_03760

MMED:

Mame_00122(xlnD_1)

AUZ:	Sa4125_23940

STEL:

STAQ_12550

STRC:

AA958_31250

MIX:	AB663_000688

CPHY:

B5808_02045

HUM:	DVJ78_00610

LDN:	H9L06_08485

HEA:	HL652_14750

NAEI:

GCM126_31160

» show all

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

[ag:AAB60878]

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

[ag:AAB60878]

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

All links

Pathway (4)   
   KEGG PATHWAY (4)   
Chemical substance (8)   
   KEGG COMPOUND (8)   
Chemical reaction (3)   
   KEGG REACTION (2)   
   KEGG RCLASS (1)   
Gene (45)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (21)   
   KEGG MGENES (23)   
Protein sequence (3)   
   UniProt (3)   
All databases (63)   

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