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 while 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).

Applications
Several studies have shown that inhibitors of leucyl aminopeptidase, such as
bestatin and hPheP[Ch2]Phe, block the growth P. falciparum malaria parasites
within erythrocytes in culture