Aminopeptidases Catalyze the Cleavage of amino acids from the amino terminus of many proteins. Many aminopeptidase activities have been described, and they appear to be widely distributed in the plant and animal kingdoms.Many, but not all, of these peptidases are zinc metalloenzymes and are inhibited by the transition-state analog bestatin. Some are monomeric, and others are assemblies of relatively high mass (50 kDa) subunits.  Methionine aminopeptidases are critical for the maturation of most proteins in eukaryotic and prokaryotic cells.Other aminopeptidases are essential for digestive and intracellular protein metabolism, including destabilization of- and hence regulation of levels of- hormones. By virtue of their ability to remove NH2-terminal residues at differential rates, it has also recently been proposed that aminopeptidases are involved in regulation of rates of hydrolysis of proteins that are degraded by the ubiquitin-dependent pathwayThey are essential for protein maturation, degradation of nonhormonal and hormonal peptides, and possibly determination of protein stability, etc. Many disease states are associated with impaired proteolytic function.


1.Taylor A. FASEB J. 1993 Feb 1;7(2):290-8.