Structural highlights
Function
[CBPO_HUMAN] Carboxypeptidase which preferentially cleaves C-terminal acidic residues from peptides and proteins. Can also cleave C-terminal hydrophobic amino acids, with a preference for small residues over large residues.[1] [MCPI_NERVS] Metallocarboxypeptidase inhibitor. Has an inhibitory effect on bovine CPA1 and CPB2, human CPA1, CPA2, CPA4, CPB1 and CPB2, and porcine CPB1. Does not inhibit D.melanogaster svr (carboxypeptidase D). Shows no activity against serine proteases subtilisin or bovine trypsin, cysteine protease papain, and aspartyl protease porcine pepsin.[2] [UniProtKB:P01075]
References
- ↑ Lyons PJ, Fricker LD. Carboxypeptidase O is a glycosylphosphatidylinositol-anchored intestinal peptidase with acidic amino acid specificity. J Biol Chem. 2011 Nov 11;286(45):39023-32. doi: 10.1074/jbc.M111.265819. Epub, 2011 Sep 15. PMID:21921028 doi:http://dx.doi.org/10.1074/jbc.M111.265819
- ↑ Covaleda G, Alonso Del Rivero M, Chavez MA, Aviles FX, Reverter D. Crystal structure of a novel metallo-carboxypeptidase inhibitor from the marine mollusk Nerita versicolor in complex with human carboxypeptidase A4. J Biol Chem. 2012 Jan 31. PMID:22294694 doi:10.1074/jbc.M111.330100
