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Membrane bound members of the M1 family : more than aminopeptidases

Albiston, Anthony L., Ye, Siying and Chai, Siew Yeen 2004, Membrane bound members of the M1 family : more than aminopeptidases, Protein and peptide letters, vol. 11, no. 5, pp. 491-500, doi: 10.2174/0929866043406643.

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Title Membrane bound members of the M1 family : more than aminopeptidases
Author(s) Albiston, Anthony L.
Ye, Siying
Chai, Siew Yeen
Journal name Protein and peptide letters
Volume number 11
Issue number 5
Start page 491
End page 500
Total pages 10
Publisher Bentham Science Publishers
Place of publication Bussum, The Netherlands
Publication date 2004-10
ISSN 0929-8665
1875-5305
Keyword(s) aminopeptidase
APA
APN
TRH-DE
ERAAP
Angiotensin IV
IRAP
Summary 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.
Language eng
DOI 10.2174/0929866043406643
Field of Research 119999 Medical and Health Sciences not elsewhere classified
Socio Economic Objective 970111 Expanding Knowledge in the Medical and Health Sciences
HERDC Research category C1.1 Refereed article in a scholarly journal
Persistent URL http://hdl.handle.net/10536/DRO/DU:30040945

Document type: Journal Article
Collection: School of Medicine
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