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2.6.1.30 |
Description |
Pyridoxamine--pyruvate transaminase |
Alternative names |
pyridoxamine-pyruvate aminotransferase;
Pyridoxamine-pyruvic transaminase;
PM-pyruvate transaminase
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Catalyzed reaction |
pyridoxamine + pyruvate = pyridoxal + L-alanine |
Cofactor |
None. |
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This activity is not, strictly speaking, B6-dependent enzyme, but it is included in the database because:
1) the enzymes with this activity bind pyridoxamine and pyridoxal (two B6 vitamers) as substrates/products;
2) the known enzymes with this activity possess a Fold-type I structure, similar to those of many PLP-dependent transaminases.
The known sequences also retain an active-site lysine residue. |
PDB |
2Z9X; |
Organisms |
-Eubacteria -Plants |
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Family |
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Links |
Enzyme (activities) 2.6.1.30
BRENDA (activities) 2.6.1.30
KEGG (pathways) 2.6.1.30
PLPMDB (PLP mutants) 2.6.1.30
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References |
Yoshikane Y, Yokochi N, Yamasaki M, Mizutani K, Ohnishi K, Mikami B, Hayashi H, Yagi T (2008) Crystal structure of pyridoxamine-pyruvate aminotransferase from Mesorhizobium loti MAFF303099 J Biol Chem 283 1120-7. Yoshikane Y, Yokochi N, Ohnishi K, Hayashi H, Yagi T (2006) Molecular cloning, expression and characterization of pyridoxamine-pyruvate aminotransferase Biochem J 396 499-507. Articles on 2.6.1.30 |
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last changed |
2017/12/13 13:08 |
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