Protein & Peptide Letters

Prof. Ben M. Dunn  
Department of Biochemistry and Molecular Biology
University of Florida
College of Medicine
P.O. Box 100245
Gainesville, FL
USA
Email: bdunn@ufl.edu

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Membrane Bound Members of the M1 Family: More Than Aminopeptidases

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

Affiliation: Howard Florey Institute of Experimental Physiology and Medicine University of Melbourne, Parkville, 3010 Australia.

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
Page: [491 - 500]
Pages: 10
DOI: 10.2174/0929866043406643
Price: $58