GUINEA-PIG MEMBRANE-BOUND AMINOPEPTIDASE-P IS A MEMBER OF THE PROLINE PEPTIDASE FAMILY

被引：18

作者：

DENSLOW, ND ^{[1
]}

RYAN, JW ^{[1
]}

NGUYEN, HP ^{[1
]}

机构：

[1] UNIV MIAMI,SCH MED,DEPT MED,MIAMI,FL 33101

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1994年 / 205卷 / 03期

关键词：

D O I：

10.1006/bbrc.1994.2877

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Members of the newly recognized proline peptidase family share the ability to hydrolyze imide bonds and share six blocks of highly homologous amino acid sequences. We have found that guinea pig lung and kidney forms of aminopeptidase P, both forms bound to membranes via glycosyl phosphatidylinositol lipid anchors, share at least three of the six conserved blocks of amino acid sequences. In addition, aminopeptidase P acts as an aminoacylproline hydrolase and thus appears to be a member of the proline peptidase family. (C) 1994 Academic Press, Inc.

引用

页码：1790 / 1795

页数：6

共 20 条

[1] BASIC LOCAL ALIGNMENT SEARCH TOOL [J].