Aminopeptidases

Supporting information

Aminopeptidases catalyze the removal of amino acids from the amino terminus of proteins and peptides. They express different substrate specificities - for example, leucyl aminopeptidase preferentially cleaves leucine residues whilst arginyl aminopeptidase releases arginine and lysine residues. Aminopeptidases are generally classed as metalloproteases, and are often associated with zinc.

Aminopeptidases were some of the earliest proteases characterized. They are classified by various characteristics, including the number of amino acids they cleave from the amino terminus; the relative efficiency with which they remove the amino acids; and cellular location - some are secreted, some are not. Other qualities, such as susceptibility to bestatin inhibition, also help characterize these enzymes.

Due to their integral role in protein maturation and peptide degradation, aminopeptidases are key to cellular protein turnover, which in turn can affect cell growth and survival. Inhibiting these enzymes suggests therapeutic benefits in the treatment of cancer, since the build-up of peptides and reduction in the levels of free amino acids can impede tumor cell survival. Hormone levels are also influenced by aminopeptidase activity - for example, pyroglutamyl aminopeptidase II degrades thyrotropin-releasing hormone, inactivating it. Other roles include regulation of angiogenesis (aminopeptidase N); inflammatory processes (leukotriene A4 hydrolase, aminopeptidase B); and blood pressure (aminopeptidase A).

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Gene Species Gene Symbol Gene Accession No. Protein Accession No.
METAP1 Human METAP1 NM_015143 P53582
Mouse Metap1 NM_175224 Q8BP48
Rat Metap1 NM_001106476 NP_001099946
METAP2 Human METAP2 NM_006838 P50579
Mouse Metap2 NM_019648 O08663
Rat Metap2 NM_022539 P38062

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