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| PROSITE documentation PDOC00714 |
Aspartate and glutamate racemases signatures
Description:
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.
Technical section:
PROSITE methods (with tools and information) covered by this documentation:
| ASP_GLU_RACEMASE_1, PS00923; Aspartate and glutamate racemases signature 1 (PATTERN) |
| Consensus pattern: |
[IVA]-[LIVM]-x-C-x(0,1)-N-[ST]-[MSA]-[STH]-[LIVFYSTANK]
The C is an active site residue |
| Sequences known to belong to this class detected by the pattern: |
ALL |
| Other sequence(s) detected in Swiss-Prot: |
5. |
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|
| Matching PDB structures:
1B73 1B74 1ZUW 2JFN ... [ALL] |
| ASP_GLU_RACEMASE_2, PS00924; Aspartate and glutamate racemases signature 2 (PATTERN) |
| Consensus pattern: |
[LIVM](2)-x-[AG]-C-T-[DEH]-[LIVMFY]-[PNGRS]-x-[LIVM]
The C is an active site residue |
| Sequences known to belong to this class detected by the pattern: |
ALL |
| Other sequence(s) detected in Swiss-Prot: |
NONE. |
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|
| Matching PDB structures:
1B73 1B74 1ZUW 2JFN ... [ALL] |
Reference:
| 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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