Aminopeptidases are a group of enzymes widely distributed among bacteria, fungi, animals and plants that catalyze the cleavage of amino acids from the amino terminus of protein or peptide substrates through hydrolysis of peptide bonds near the N-terminal end of a polypeptide chain. Most aminopeptidases are assembled by relatively high mass (50kDa) subunits exhibiting multimeric structures, whereas some are monomeric. The majority of aminopeptidases are zinc metalloenzymes and hence inhibited by the transition-state analog bestatin. Aminopeptidases have been found in many subcellular organelles as well as in cytoplasm and membrane, where they are involved in diverse proteolytic pathways and play an essential role in protein maturation, degradation of non-hormonal and hormonal peptides and possibly determination of protein stability.
- C4189 Arphamenine B (hemisulfate)Summary: aminopeptidase B inhibitor
- C3708 L-Leucine 4-methoxy-β-naphthylamide (hydrochloride)Summary: substrate for aminopeptidase M and leucine aminopeptidase
- C3622 TNP-470Summary: methionine aminopeptidase-2 (MetAP2) inhibitor
- A8621 Bestatin hydrochlorideTarget: AminopeptidasesSummary: Inhibitor of aminopeptidase N (APN)/CD13 and aminopeptidase B.
- A4408 SC 57461ASummary: LTA4 hydrolase inhibitor,potent and selective
- A4407 FumagillinSummary: Antibiotic and antiangiogenic agent
- A4355 Tosedostat (CHR2797)1 CitationTarget: AminopeptidasesSummary: Aminopeptidase inhibitor
- A2575 BestatinTarget: AminopeptidasesSummary: Aminopeptidase inhibitor