InterPro domain: IPR034005

This entry includes the following members of peptidase subfamily M3A: peptidyl dipeptidase DCP (EC 3.4.15.5; MEROPS identifier M03.005; also known as dipeptidyl carboxypeptidase) and oligopeptidase A (OpdA; EC 3.4.24.70; MEROPS identifier M03.004). DCP releases dipeptides from the C-termini of various peptides and proteins, the smallest substrate being N-blocked tripeptides and unblocked tetrapeptides. DCP from E. coli is inhibited by the anti-hypertensive drug captopril, an inhibitor of the mammalian angiotensin converting enzyme (ACE, also called peptidyl dipeptidase A) [ 1 , 2 ]. Oligopeptidase A (OpdA) may play a specific role in the degradation of signal peptides after they are released from precursor forms of secreted proteins. It can also cleave N-acetyl-L-Ala [ 3 ].

1. Catalytic properties of recombinant dipeptidyl carboxypeptidase from Escherichia coli: a comparative study with angiotensin I-converting enzyme. Biol. Chem. 390, 931-40
2. Crystal structure of the E. coli dipeptidyl carboxypeptidase Dcp: further indication of a ligand-dependent hinge movement mechanism. J. Mol. Biol. 349, 99-112
3. Dipeptidyl carboxypeptidase and oligopeptidase A from Escherichia coli and Salmonella typhimurium. Meth. Enzymol. 248, 567-79