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Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

Membrane Bound Members of the M1 Family: More Than Aminopeptidases

Author(s): Anthony L. Albiston, Siying Ye and Siew Yeen Chai

Volume 11 , Issue 5 , 2004

Page: [491 - 500] Pages: 10

DOI: 10.2174/0929866043406643

Price: $65

Abstract

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-(X18)-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.

Keywords: aminopeptidase, apa, apn, trh-de, eraap, angiotensin iv, irap


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