Carboxypeptidases are enzymes that hydrolyze C-terminal peptide bonds. The carboxypeptidase family includes metallo-, serine, and cysteine carboxypeptidases. According to their substrate specificity, these enzymes are referred to as carboxypeptidase A (cleaving aliphatic residues) or carboxypeptidase B (cleaving basic amino residues). The protein encoded by this gene is activated by trypsin and acts on carboxypeptidase B substrates. After thrombin activation, the mature protein downregulates fibrinolysis. Polymorphisms have been described for this gene and its promoter region. [provided by RefSeq, Apr 2012].
Kato, Nicholson, Neiman, Rantalainen, Holmes, Barrett, Uhlén, Nilsson, Spector, Schwenk: "Variance decomposition of protein profiles from antibody arrays using a longitudinal twin model." in: Proteome science, Vol. 9, pp. 73, (2011) (PubMed).
Qin, Zeng, Tian, Deng, Ren, Zheng, Li, Li, Liao, Chen: "Involvement of prolylcarboxypeptidase in the effect of rutaecarpine on the regression of mesenteric artery hypertrophy in renovascular hypertensive rats." in: Clinical and experimental pharmacology & physiology, Vol. 36, Issue 3, pp. 319-24, (2009) (PubMed).