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

The degradation of enterostatin (VPDPR), a potent inhibitor of food intake, by intestinal brush-border membranes, brain membranes, and rat serum has been investigated in the presence of specific inhibitors. Hydrolysis by intestinal membranes was found to be 10 and 100 times faster than in serum and brain membranes, respectively. Enterostatin hydrolysis by intestinal and brain membranes involves the removal of C-terminal arginine by carboxypeptidase P, leading to the production of des-Arg-enterostatin, and the splitting of the Pro2-Asp3 bond by dipeptidyl aminopeptidase IV (DPP IV). A small amount of the potent anorectic peptide Pro2-Asp3-Pro4 was released during hydrolysis of des-Arg-enterostatin by brain membranes and rat serum. In rat serum, enterostatin degradation was mainly due to DPP IV.
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PMID:Metabolism of enterostatin in rat intestine, brain membranes, and serum: differential involvement of proline-specific peptidases. 765 91

The longitudinal distribution of brush-border endopeptidase-24.11, endopeptidase-2, aminopeptidase W, angiotensin-converting enzyme (ACE), dipeptidyl peptidase IV (DPP IV), carboxypeptidase P, and aminopeptidase P in the rat intestine was determined. The jejunum has the highest activities of endopeptidase-24.11 and ACE while the ileum has the highest activities of aminopeptidase W and carboxypeptidase P, and the jejunoileal junction has the highest activity of aminopeptidase P. The jejunum and ileum have similar activities of DPP IV. The profiles of differential hydrolysis of neurotensin and acetylneurotensin (8-13) along the intestine agree with distribution of endopeptidase-24.11 and ACE, suggesting that amino acid sequences of peptides and the substrate specificity of enzymes will determine site-dependent hydrolysis. There is substantial similarity in the intestinal distribution of peptidases in the human, rat, and rabbit.
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PMID:Distribution of brush-border membrane peptidases along the rat intestine. 793 32

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