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5.1.1.10 |
| Description |
Amino-acid racemase. |
| Catalyzed reaction |
An L-amino acid = a D-amino acid. |
| Cofactor |
Pyridoxal-phosphate. |
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The occasional genes annotated with this function in public databases are either non-PLP dependent racemases, or non-validated PLP enzymes resembling alanine racemase (family 5.1.1.1_a) or serine racemase (family 5.1.1.18). |
| Organisms |
-Bacteria |
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| Links |
Enzyme (activities) 5.1.1.10
BRENDA (activities) 5.1.1.10
KEGG (pathways) 5.1.1.10
PLPMDB (PLP mutants) 5.1.1.10
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| References |
Reynolds, K.; Martin, J.; Shen, S. J.; Esaki, N.; Soda, K.; Floss, H. G. (1991) Mechanistic studies of two amino acid racemases of broad substrate specificity from Pseudomonas striata and Aeromonas caviae J Basic Microbiol 31 177-88. Roise, D.; Soda, K.; Yagi, T.; Walsh, C. T. (1984) Inactivation of the Pseudomonas striata broad specificity amino acid racemase by D and L isomers of beta-substituted alanines: kinetics, stoichiometry, active site peptide, and mechanistic studies Biochemistry 23 5195-201.. Soda, K.; Osumi, T. (1969) Crystalline amino acid racemase with low substrate specificity Biochem Biophys Res Commun 35 363-8.. |
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| last changed |
2008/01/15 14:19 |
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