肽基二肽水解酶（血管紧张素I转换酶）的一些酶学性质。

Some enzymatic properties of peptidyl dipeptide hydrolase (angiotensin I-converting enzyme).

作者信息

Oshima G, Nagasawa K

出版信息

J Biochem. 1977 Jan;81(1):57-63. doi: 10.1093/oxfordjournals.jbchem.a131450.

DOI:10.1093/oxfordjournals.jbchem.a131450

PMID:191438

Abstract

Peptidyldipeptide hydrolase [angiotensin I-converting enzyme, EC 3.4.15.1] was inhibited by inorganic and organic phosphorus compounds tested, except for beta-glycerophosphate, 5'-AMP, and 5'-ADP, at the reagent concentrations used. Orthophosphate and pyrophosphate nonspecifically inhibited the enzyme activity. The enzyme was also inhibited specifically by carboxylates. The degree of inhibition by aliphatic monocarboxylates increased in proportion to their chain length up to C14. Aromatic and omega-phenylalkylcarboxylates also inhibited the enzyme activity. The enzyme was noncompetitively inhibited by acetate, 3-phenylpropionate and laurate. The Ki's for acetate, 3-phenylpropionate, and laurate were 60, 3.3, and 2.5 mM, respectively.

摘要

在所使用的试剂浓度下，除β-甘油磷酸、5'-AMP和5'-ADP外，所测试的无机和有机磷化合物均能抑制肽基二肽水解酶[血管紧张素I转换酶，EC 3.4.15.1]。正磷酸盐和焦磷酸盐非特异性抑制酶活性。该酶也受到羧酸盐的特异性抑制。脂肪族单羧酸盐的抑制程度随其链长增加直至C14呈比例增加。芳香族和ω-苯基烷基羧酸盐也抑制酶活性。该酶受到乙酸盐、3-苯基丙酸盐和月桂酸盐的非竞争性抑制。乙酸盐、3-苯基丙酸盐和月桂酸盐的Ki值分别为60 mM、3.3 mM和2.5 mM。