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


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.


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

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