Membrane Bound Members of the M1 Family: More Than Aminopeptidases

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

Journal Name:Protein & Peptide Letters

Volume 11 , Issue 5 , 2004

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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Article Details

VOLUME: 11
ISSUE: 5
Year: 2004
Page: [491 - 500]
Pages: 10
DOI: 10.2174/0929866043406643
Price: $58