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| PROSITE documentation PDOC00714 |
Aspartate and glutamate racemases signatures
Aspartate racemase (EC 5.1.1.13) and glutamate racemase (EC 5.1.1.3) are two evolutionary related bacterial enzymes that do not seem to require a cofactor for their activity [1]. Glutamate racemase, which interconverts L-glutamate into D-glutamate, is required for the biosynthesis of peptidoglycan and some peptide-based antibiotics such as gramicidin S.
In addition to characterized aspartate and glutamate racemases, this family also includes a hypothetical protein from Erwinia carotovora and one from Escherichia coli (ygeA).
Two conserved cysteines are present in the sequence of these enzymes. They are expected to play a role in catalytic activity by acting as bases in proton abstraction from the substrate. We developed signature patterns for both cysteines.
Last update:May 2004 / Text revised.
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PROSITE methods (with tools and information) covered by this documentation:
| 1 | Authors | Gallo K.A. Knowles J.R. |
| Title | Purification, cloning, and cofactor independence of glutamate racemase from Lactobacillus. | |
| Source | Biochemistry 32:3981-3990(1993). | |
| PubMed ID | 8385993 |
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