KEGG   ENZYME: 1.1.99.42Help
Entry
EC 1.1.99.42                Enzyme                                 

Name
4-pyridoxic acid dehydrogenase;
mlr6792 (locus name)
Class
Oxidoreductases;
Acting on the CH-OH group of donors;
With unknown physiological acceptors
BRITE hierarchy
Sysname
4-pyridoxate:acceptor 5-oxidoreductase
Reaction(IUBMB)
4-pyridoxate + acceptor = 5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate + reduced acceptor [RN:R02993]
Reaction(KEGG)
Substrate
4-pyridoxate [CPD:C00847];
acceptor [CPD:C00028]
Product
5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate [CPD:C06050];
reduced acceptor [CPD:C00030]
Comment
The enzyme, characterized from the bacteria Pseudomonas sp. MA-1 and Mesorhizobium loti, participates in the degradation of pyridoxine (vitamin B6). It is membrane bound and contains FAD. The enzyme has been assayed in vitro in the presence of the artificial electron acceptor dichloroindophenol (DCPIP).
History
EC 1.1.99.42 created 2018
Pathway
ec00750  Vitamin B6 metabolism
ec01120  Microbial metabolism in diverse environments
Orthology
K18611  4-pyridoxate dehydrogenase
Genes
MLO: mlr6792
MLN: A9174_14040
MCI: Mesci_2016
MAM: Mesau_02084
MESW: A9K65_010520
Taxonomy
Reference
1  [PMID:6348042]
  Authors
Yagi T, Kishore GM, Snell EE
  Title
The bacterial oxidation of vitamin B6. 4-Pyridoxic acid dehydrogenase: a membrane-bound enzyme from Pseudomonas MA-1.
  Journal
J Biol Chem 258:9419-25 (1983)
Reference
2  [PMID:18216065]
  Authors
Ge F, Yokochi N, Yoshikane Y, Ohnishi K, Yagi T
  Title
Gene identification and characterization of the pyridoxine degradative enzyme 4-pyridoxic acid dehydrogenase from the nitrogen-fixing symbiotic bacterium Mesorhizobium loti MAFF303099.
  Journal
J Biochem 143:603-9 (2008)
DOI:10.1093/jb/mvn010
  Sequence
[mlo:mlr6792]
Other DBs
ExplorEnz - The Enzyme Database: 1.1.99.42
IUBMB Enzyme Nomenclature: 1.1.99.42
ExPASy - ENZYME nomenclature database: 1.1.99.42
BRENDA, the Enzyme Database: 1.1.99.42

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