[A membrane-bound alanine aminopeptidase from Acinetobacter calcoaceticus. 3. Inhibition of the enzyme].
The alanine aminopeptidase from Acinetobacter calcoaceticus is inhibited by SH-reagents like p-hydroxymercuribenzote, Ellman's reagent, N-bromosuccinimide, and metal chelating agents like 1,10-phenanthroline. The AAP is competitively inhibited by L-amino acids such as leucine, phenylalanine, and valine having hydrophobic side chains. Bacitracin (Ki = 2.0.10(-6) mol/l) inhibits AAP stronger than puromycin (Ki = 8.0.10(-6) mol/l). In contrast, the Aeromonas aminopeptidase (EC 3.4.11.10) is stronger inhibited by bestatin (Ki = 1.8.10(-8) mol/l) than the membrane-bound AAP from Acinetobacter calcoaceticus. However, the binding of bestatin by both membrane-bound enzymes. Acinetobacter-AAP and microsomal aminopeptidase M (EC 3.4.11.2), with Ki values of 8.10(-6) mol/l is in the same range.
Jahreis
G
G
Institut für Biochemie, Bereich Medizin, Martin-Luther-Universität Halle-Wittenberg, Saale.
Aurich
H
H
D000188:Actinobacillus / Q000187:drug effects / Q000201:enzymology*; D000596:Amino Acids / Q000032:analysis; D000626:Aminopeptidases / Q000378:metabolism*; D001667:Binding, Competitive; D001974:Bromosuccinimide / Q000494:pharmacology; D018826:CD13 Antigens; D002462:Cell Membrane / Q000201:enzymology; D006902:Hydroxymercuribenzoates / Q000494:pharmacology; D010618:Phenanthrolines / Q000494:pharmacology; D013438:Sulfhydryl Compounds / Q000494:pharmacology
D000596:Amino Acids; D006902:Hydroxymercuribenzoates; D010618:Phenanthrolines; D013438:Sulfhydryl Compounds; C030601:4-hydroxymercuribenzoate; D000626:Aminopeptidases; D018826:CD13 Antigens; D001974:Bromosuccinimide; C025205:1,10-phenanthroline