Aminopeptidase P: cation activation and inhibitor sensitivity are substrate-dependent.
Lloyd
G S
GS
Department of Biochemistry and Molecular Biology, University of Leeds, U.K.
Turner
A J
AJ
D000595:Amino Acid Sequence; D000626:Aminopeptidases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D000806:Angiotensin-Converting Enzyme Inhibitors / Q000494:pharmacology*; D000818:Animals; D001920:Bradykinin / Q000378:metabolism; D017315:Cilazapril / Q000031:analogs & derivatives / Q000494:pharmacology; D015773:Enalaprilat / Q000494:pharmacology; D007668:Kidney / Q000201:enzymology; D007700:Kinetics; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000378:metabolism; D017257:Ramipril / Q000031:analogs & derivatives / Q000494:pharmacology; D013373:Substance P / Q000378:metabolism; D013379:Substrate Specificity; D013552:Swine
D000806:Angiotensin-Converting Enzyme Inhibitors; D009842:Oligopeptides; C088188:glycyl-prolyl-hydroxyproline; D017315:Cilazapril; D013373:Substance P; C052549:ramiprilat; D000626:Aminopeptidases; C022750:X-Pro aminopeptidase; D015773:Enalaprilat; D017257:Ramipril; D001920:Bradykinin; C045980:cilazaprilat