ENZYME entry: EC 3.4.13.22
| Accepted Name |
| D-Ala-D-Ala dipeptidase.
|
| Alternative Name(s) |
| D-alanyl-D-alanine dipeptidase. |
| Reaction catalysed |
| D-Ala-D-Ala + H(2)O <=> 2 D-Ala |
| Cofactor(s) |
| Zinc.
|
| Comment(s) |
- Protects Enterococcus faecium from the antibiotic vancomycin, which
can bind to the -D-Ala-D-Ala sequence at the C-terminus of the
peptidoglycan pentapeptide.
- Reduces the availability of the free dipeptide D-Ala-D-Ala, which is
the precursor for this pentapeptide sequence, allowing D-Ala-(R)-
lactate (for which vancomycin has much less affinity) to be added to
the cell wall instead.
- The enzyme is stereospecific, as L-Ala-L-Ala, D-Ala-L-Ala and L-Ala-
D-Ala are not substrates.
- Belongs to peptidase family M15.
|
| Cross-references |
| BRENDA | 3.4.13.22 |
| EC2PDB | 3.4.13.22 |
| ExplorEnz | 3.4.13.22 |
| PRIAM enzyme-specific profiles | 3.4.13.22 |
| KEGG Ligand Database for Enzyme Nomenclature | 3.4.13.22 |
| IUBMB Enzyme Nomenclature | 3.4.13.22 |
| IntEnz | 3.4.13.22 |
| MEDLINE | Find literature relating to 3.4.13.22 |
| MetaCyc | 3.4.13.22 |
| UniProtKB/Swiss-Prot |
|
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