Title : Novel activity of angiotensin-converting enzyme. Hydrolysis of cholecystokinin and gastrin analogues with release of the amidated C-terminal dipeptide.

Pub. Date : 1989 Aug 15

PMID : 2554881






6 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 ACE (angiotensin-converting enzyme; peptidyl dipeptidase A; EC 3.4.15.1), cleaves C-terminal dipeptides from active peptides containing a free C-terminus. Dipeptides angiotensin-converting enzyme Oryctolagus cuniculus
2 ACE (angiotensin-converting enzyme; peptidyl dipeptidase A; EC 3.4.15.1), cleaves C-terminal dipeptides from active peptides containing a free C-terminus. Dipeptides angiotensin-converting enzyme Oryctolagus cuniculus
3 The cleavage of CCK-8 and gastrin analogues was inhibited by ACE inhibitors (Captopril and EDTA), but not by other enzyme inhibitors (phosphoramidon, thiorphan, bestatin etc.). Captopril angiotensin-converting enzyme Oryctolagus cuniculus
4 The cleavage of CCK-8 and gastrin analogues was inhibited by ACE inhibitors (Captopril and EDTA), but not by other enzyme inhibitors (phosphoramidon, thiorphan, bestatin etc.). Edetic Acid angiotensin-converting enzyme Oryctolagus cuniculus
5 Hydrolysis of [Leu15]gastrin-(14-17)-peptide [Boc (t-butoxycarbonyl)-Trp-Leu-Asp-Phe-NH2] in the presence of ACE was found to be dependent on the chloride-ion concentration. boc (t-butoxycarbonyl)-trp-leu-asp-phe-nh2 angiotensin-converting enzyme Oryctolagus cuniculus
6 Hydrolysis of [Leu15]gastrin-(14-17)-peptide [Boc (t-butoxycarbonyl)-Trp-Leu-Asp-Phe-NH2] in the presence of ACE was found to be dependent on the chloride-ion concentration. Chlorides angiotensin-converting enzyme Oryctolagus cuniculus