Enzyme

Download
EC Tree
     1. Oxidoreductases
        1.1 Acting on the CH-OH group of donors
            1.1.99 With unknown physiological acceptors
ID:1.1.99.42
Description:4-pyridoxate dehydrogenase.

3D structure

Click one PDB to see exact 3D structure provided by NGL.

Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.

References

External Links

UniProtKB Enzyme Link: UniProtKB 1.1.99.42
BRENDA Enzyme Link: BRENDA 1.1.99.42
KEGG Enzyme Link: KEGG1.1.99.42
BioCyc Enzyme Link: BioCyc 1.1.99.42
ExPASy Enzyme Link: ExPASy1.1.99.42
EC2PDB Enzyme Link: EC2PDB 1.1.99.42
ExplorEnz Enzyme Link: ExplorEnz 1.1.99.42
PRIAM enzyme-specific profiles Link: PRIAM 1.1.99.42
IntEnz Enzyme Link: IntEnz 1.1.99.42
MEDLINE Enzyme Link: MEDLINE 1.1.99.42
MSA:

1.1.99.42;

Phylogenetic Tree:

1.1.99.42;

Uniprot:
M-CSA:
RHEA:17085 4-pyridoxate + A = 5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate + AH2
RULE(radius=1) [*:1]-[CH2;+0:2]-[OH;+0:3]>>[*:1]-[CH;+0:2]=[O;H0;+0:3]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
The bacterial oxidation of vitamin B6. 4-Pyridoxic acid dehydrogenase: a membrane-bound enzyme from Pseudomonas MA-1.Yagi T, Kishore GM, Snell EE1983 Aug 106348042
Gene identification and characterization of the pyridoxine degradative enzyme 4-pyridoxic acid dehydrogenase from the nitrogen-fixing symbiotic bacterium Mesorhizobium loti MAFF303099.Ge F, Yokochi N, Yoshikane Y, Ohnishi K, Yagi T2008 May18216065