Carboxypeptidase T (IPR033810)

Short name: Carboxypeptidase_T

Overlapping homologous superfamilies


Domain relationships


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) [PMID: 7674922]. 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 [PMID: 10708864]. 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 [PMID: 7674954]. 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 [PMID: 17511606]. CPT has increased thermal stability in presence of Ca2+ ions, and two disulfide bridges which give an additional stabilization factor.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.