EC 1.2.1.100 - 5-formyl-3-hydroxy-2-methylpyridine 4-carboxylate 5-dehydrogenase

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IntEnz Enzyme Nomenclature
EC 1.2.1.100

Names

Accepted name:
5-formyl-3-hydroxy-2-methylpyridine 4-carboxylate 5-dehydrogenase
Other name:
mlr6793 (locus name)
Systematic name:
5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate:NAD+ 5-oxidoreductase

Reaction

Comments:

The enzyme, characterized from the bacteria Pseudomonas sp. MA-1 and Mesorhizobium loti, participates in the degradation of pyridoxine (vitamin B6).

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot:

References

  1. Lee, Y. C., Nelson, M. J., Snell, E. E.
    Enzymes of vitamin B6 degradation. Purification and properties of isopyridoxal dehydrogenase and 5-formyl-3-hydroxy-2-methylpyridine-4-carboxylic-acid dehydrogenase.
    J. Biol. Chem. 261 : 15106-15111 (1986). [PMID: 3533936]
  2. Yokochi, N., Yoshikane, Y., Matsumoto, S., Fujisawa, M., Ohnishi, K., Yagi, T.
    Gene identification and characterization of 5-formyl-3-hydroxy-2-methylpyridine 4-carboxylic acid 5-dehydrogenase, an NAD+-dependent dismutase.
    J. Biochem. 145 : 493-503 (2009). [PMID: 19218190]
  3. Mugo, A. N., Kobayashi, J., Mikami, B., Yoshikane, Y., Yagi, T., Ohnishi, K.
    Crystal structure of 5-formyl-3-hydroxy-2-methylpyridine 4-carboxylic acid 5-dehydrogenase, an NAD?-dependent dismutase from Mesorhizobium loti.
    Biochem. Biophys. Res. Commun. 456 : 35-40 (2015). [PMID: 25446130]

[EC 1.2.1.100 created 2018]