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
Protein & Peptide Letters
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.
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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 |
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