| Primary Identifier | IPR043691 | Type | Family |
| Short Name | MpaA |
| description | MpaA is a murein-tripeptide-specific zinc carboxypeptidase that hydrolyses the gamma-D-glutamyl-diaminopimelic acid bond in the murein tripeptide (L-Ala-gamma-D-Glu-meso-Dap), derived from the turnover of murein but it is not active against the murein tetrapeptide (L-Ala-gamma-D-Glu-meso-Dap-D-Ala). MpaA is a dimeric metalloprotein, containing one zinc ion per chain. Crystal structure studies revealed that this protein has high structural similarity to eukaryotic zinc carboxypeptidases and that it has a narrower substrate specificity due to an additional structure that partially occludes the substrate-binding groove []. MpaA belongs to the peptidase M14 family. |
