Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.16.2 (PCP)
3,761 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The N-terminal amino-acid sequence of pig dipeptidyl-peptidase II (EC 3.4.14.2; DPP II) recently published (Huang, K., Takagaki, M., Kani, K. and Ohkubo, I. (1996) Biochim. Biophys. Acta 1290, 149-156) proves that the enzyme is homologous with lysosomal Pro-X carboxypeptidase (EC 3.4.16.2), and belongs to peptidase family S28 in clan SC. This is consistent with a number of biochemical similarities between these two prolyl bond-cleaving serine peptidases. DPP II is not related to granzymes, as was suggested by Huang et al.
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PMID:Dipeptidyl-peptidase II is related to lysosomal Pro-X carboxypeptidase. 894 82

Much attention has recently been given to a class of proteases that cleave proteins and peptides after proline residues. This class includes dipeptidyl peptidase IV (DPP IV; also termed CD26), fibroblast activation protein alpha (FAP; seprase), DPP7 (DPP II; quiescent cell proline dipeptidase), DPP8, DPP9, and prolyl carboxypeptidase (PCP; angiotensinase C). More distant members include prolyl oligopeptidase (POP; post proline cleaving enzyme) and acylaminoacylpeptidase (AAP; acylpeptide hydrolase). The DPPs and related proteins contain both membrane-bound and soluble members and span a broad range of expression patterns, tissue distributions and compartmentalization. These proteins have important roles in regulation of signaling by peptide hormones, and are emerging targets for diabetes, oncology and other indications.
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PMID:Prolyl peptidases: a serine protease subfamily with high potential for drug discovery. 1294 25