Jahreis G, Aurich H
Institut für Biochemie, Bereich Medizin, Martin-Luther-Universität Halle-Wittenberg, Saale.
Biomed Biochim Acta. 1990;49(5):339-45.
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.
醋酸钙不动杆菌的丙氨酸氨基肽酶受到对羟基汞苯甲酸、埃尔曼试剂、N-溴代琥珀酰亚胺等巯基试剂以及1,10-菲咯啉等金属螯合剂的抑制。该丙氨酸氨基肽酶受到具有疏水侧链的L-氨基酸（如亮氨酸、苯丙氨酸和缬氨酸）的竞争性抑制。杆菌肽（Ki = 2.0×10⁻⁶ mol/l）对丙氨酸氨基肽酶的抑制作用强于嘌呤霉素（Ki = 8.0×10⁻⁶ mol/l）。相比之下，气单胞菌氨基肽酶（EC 3.4.11.10）受到贝司他汀（Ki = 1.8×10⁻⁸ mol/l）的抑制作用强于醋酸钙不动杆菌的膜结合丙氨酸氨基肽酶。然而，贝司他汀与膜结合酶醋酸钙不动杆菌-丙氨酸氨基肽酶和微粒体氨基肽酶M（EC 3.4.11.2）的结合，其Ki值为8×10⁻⁶ mol/l，处于同一范围。
