[Membrane-bound alanine aminopeptidase from Acinetobacter calcoaceticus. 4. Amino acid chloromethyl ketones as pH-dependent, substrate-derived inhibitors of cysteine protease].
The alanine aminopeptidase (AAP) from A. calcoaceticus is a metal-ion-dependent cysteine protease bound to the inner membranes of the cells. Amino acid chloromethyl ketones are highly specific inhibitors of the enzyme. The AAP is inhibited at pH 7.5 (pH-optimum) by mixed-type inhibition. A competitive inhibition type results if the pH value is decreased to 6.2. In contrast, the inhibition of the AAP by substrate-derived chloromethyl ketones is of the irreversible type at pH 8.25.
Jahreis
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Institut für Biochemie, Martin-Luther-Universität Halle-Wittenberg, FRG.
Aurich
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H
D016954:Acinetobacter calcoaceticus / Q000187:drug effects / Q000201:enzymology*; D000590:Amino Acid Chloromethyl Ketones / Q000494:pharmacology*; D000626:Aminopeptidases / Q000037:antagonists & inhibitors*; D001426:Bacterial Proteins / Q000037:antagonists & inhibitors*; D001667:Binding, Competitive; D018826:CD13 Antigens; D002462:Cell Membrane / Q000201:enzymology; D015853:Cysteine Proteinase Inhibitors / Q000494:pharmacology*; D006863:Hydrogen-Ion Concentration; D013379:Substrate Specificity
D000590:Amino Acid Chloromethyl Ketones; D001426:Bacterial Proteins; D015853:Cysteine Proteinase Inhibitors; D000626:Aminopeptidases; D018826:CD13 Antigens
Eine membrangebundene Alanylaminopeptidase aus Acinetobacter calcoaceticus: 4. Aminosäurechlormethylketone als pH-abhängige, substratanaloge Cysteinprotease-Inhibitoren.