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 |
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Description: | 4-pyridoxate dehydrogenase. |
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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.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: | |
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Phylogenetic Tree: | |
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 |
Title | Authors | Date | PubMed ID |
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The bacterial oxidation of vitamin B6. 4-Pyridoxic acid dehydrogenase: a membrane-bound enzyme from Pseudomonas MA-1. | Yagi T, Kishore GM, Snell EE | 1983 Aug 10 | 6348042 |
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 T | 2008 May | 18216065 |