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 terms
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Aminopeptidases / chemistry
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Aminopeptidases / classification
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Aminopeptidases / genetics
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Aminopeptidases / metabolism*
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Animals
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CD13 Antigens / chemistry
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CD13 Antigens / metabolism
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Cystinyl Aminopeptidase
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Humans
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Membrane Proteins / chemistry
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Membrane Proteins / classification
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Membrane Proteins / genetics
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Membrane Proteins / metabolism*
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Minor Histocompatibility Antigens
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Pyrrolidonecarboxylic Acid / analogs & derivatives*
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Pyrrolidonecarboxylic Acid / chemistry
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Pyrrolidonecarboxylic Acid / metabolism
Substances
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Membrane Proteins
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Minor Histocompatibility Antigens
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Aminopeptidases
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ERAP1 protein, human
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CD13 Antigens
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Cystinyl Aminopeptidase
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leucyl-cystinyl aminopeptidase
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pyroglutamyl-peptidase II
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Pyrrolidonecarboxylic Acid