| Literature DB >> 15544570 |
Anthony L Albiston1, Siying Ye, Siew Yeen Chai.
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.Mesh:
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Year: 2004 PMID: 15544570 DOI: 10.2174/0929866043406643
Source DB: PubMed Journal: Protein Pept Lett ISSN: 0929-8665 Impact factor: 1.890