Membrane bound members of the M1 family: More than aminopeptidases

被引：65

作者：

Albiston, AL ^{[1
]}

Ye, SY ^{[1
]}

Chai, SY ^{[1
]}

机构：

[1] Univ Melbourne, Howard Florey Inst Expt Physiol & Med, Parkville, Vic 3010, Australia

来源：

PROTEIN AND PEPTIDE LETTERS | 2004年 / 11卷 / 05期

关键词：

aminopeptidase; APA; APN; TRH-DE; ERAAP; angiotensin IV; IRAP;

D O I：

10.2174/0929866043406643

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：

In mammals the M1 aminopeptidase family consists of nine different proteins, five of which are integral membrane proteins. The aminopeptidases are defined by two motifs in the catalytic domain; a zinc binding motif HEXXH-(X-18)-E and an exopeptidase motif GXMEN. Aminopeptidases of this family are able to cleave a broad range of peptides down to only to a single peptide. This ability to either generate or degrade active peptide hormones is the focus of this review. In addition to their capacity to degrade a range of peptides a number of these aminopeptidases have novel functions that impact on cell signalling and will be discussed.

引用

页码：491 / 500

页数：10

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