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Membrane bound members of the M1 family : more than aminopeptidases

journal contribution
posted on 2004-10-01, 00:00 authored by A Albiston, Siying Ye, S Chai
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.

History

Journal

Protein and peptide letters

Volume

11

Issue

5

Pagination

491 - 500

Publisher

Bentham Science Publishers

Location

Bussum, The Netherlands

ISSN

0929-8665

eISSN

1875-5305

Language

eng

Publication classification

C1.1 Refereed article in a scholarly journal