| Primary Identifier | IPR033810 | Type | Domain |
| Short Name | Carboxypeptidase_T |
| description | This entry includes the peptidase M14-like domain of carboxypeptidase (CP) T (CPT; MEROPS identifier M14.007). CPT belongs to the M14 family of metallocarboxypeptidases (MCPs) []. The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity []. CPT has moderate similarity to CPA and CPB, and exhibits dual-substrate specificity by cleaving C-terminal hydrophobic amino acid residues like CPA and C-terminal positively charged residues like CPB []. The substrate specificity difference between CPT and CPA and CPB is ascribed to a few amino acid substitutions at the substrate-binding pocket while the spatial organization of the binding site remains the same as in all Zn-CPs []. CPT has increased thermal stability in presence of Ca2+ions, and two disulfide bridges which give an additional stabilization factor. |
