Membrane Bound Members of the M1 Family: More Than Aminopeptidases

Title: Membrane Bound Members of the M1 Family: More Than Aminopeptidases

Volume: 11 Issue: 5

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

Affiliation:

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

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.

Cite this article as:

Albiston L. Anthony, Ye Siying and Chai Yeen Siew, Membrane Bound Members of the M1 Family: More Than Aminopeptidases, Protein & Peptide Letters 2004; 11 (5) . https://dx.doi.org/10.2174/0929866043406643

DOI https://dx.doi.org/10.2174/0929866043406643	Print ISSN 0929-8665
Publisher Name Bentham Science Publisher	Online ISSN 1875-5305