Chemical modification of aminopeptidase P: identification of a critical histidyl residue.
Lim
J
J
Department of Biochemistry & Molecular Biology, University of Leeds, U.K.
Turner
A J
AJ
D000595:Amino Acid Sequence; D000626:Aminopeptidases / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000378:metabolism; D000818:Animals; D001665:Binding Sites; D001920:Bradykinin / Q000494:pharmacology; D004047:Diethyl Pyrocarbonate / Q000494:pharmacology; D004791:Enzyme Inhibitors / Q000494:pharmacology; D006639:Histidine / Q000737:chemistry; D066298:In Vitro Techniques; D051379:Mice; D008969:Molecular Sequence Data; D015394:Molecular Structure; D009842:Oligopeptides / Q000737:chemistry / Q000494:pharmacology; D013552:Swine
D004791:Enzyme Inhibitors; D009842:Oligopeptides; C088188:glycyl-prolyl-hydroxyproline; D006639:Histidine; D000626:Aminopeptidases; C022750:X-Pro aminopeptidase; D004047:Diethyl Pyrocarbonate; D001920:Bradykinin