分子克隆揭示的两种激肽酶I型酶的结构特征

Structural features of two kininase I-type enzymes revealed by molecular cloning.

作者信息

Skidgel R A, Tan F

机构信息

Laboratory of Peptide Research, University of Illinois College of Medicine, Chicago 60612.

出版信息

Agents Actions Suppl. 1992;38 ( Pt 1):359-67. doi: 10.1007/978-3-0348-7321-5_45.

DOI:10.1007/978-3-0348-7321-5_45

PMID:1466286

Abstract

Kininase I-type carboxypeptidases remove a single C-terminal Arg residue from kinins. The circulating kininase I (carboxypeptidase N) contains two types of subunits: a 50 kDa catalytic subunit and an 83 kDa carrier subunit which protects the active subunit in blood. The 83 kDa subunit contains 12 leucine-rich tandem repeats, similar in sequence to other proteins with binding functions. Human carboxypeptidase M is a widely distributed "tissue kininase I" bound to plasma membranes. It has 41% sequence identity with the 50 kDa subunit of carboxypeptidase N and may regulate the activity of kinins and other peptides at the cell surface.

摘要

激肽酶I型羧肽酶从激肽中去除单个C末端精氨酸残基。循环中的激肽酶I（羧肽酶N）包含两种类型的亚基：一个50 kDa的催化亚基和一个83 kDa的载体亚基，后者可在血液中保护活性亚基。83 kDa的亚基包含12个富含亮氨酸的串联重复序列，其序列与其他具有结合功能的蛋白质相似。人羧肽酶M是一种广泛分布的与质膜结合的“组织激肽酶I”。它与羧肽酶N的50 kDa亚基具有41%的序列同一性，可能在细胞表面调节激肽和其他肽的活性。