5 articles
Aminopeptidase P
Aminopeptidase P, also called Xaa-Pro aminopeptidase (EC 3.4.11.9), is a metalloprotease that cleaves N-terminal amino acids linked to proline, found in bacteria, archaea, and mammals.
Leucyl aminopeptidase
Leucyl aminopeptidase, also known as leucine aminopeptidase or cytosol aminopeptidase, is a metal-dependent enzyme of peptidase family M17 that cleaves amino acids from the N-termini of proteins, favoring leucine.
Metal-dependent aminopeptidase
Metal-dependent aminopeptidases are exopeptidase enzymes that remove amino acids one at a time from peptide N-terminus, using one or two bound metal ions, most often zinc, to catalyze hydrolysis.
Methionine aminopeptidase 2
Methionine aminopeptidase 2 (MetAP2), a dimetallohydrolase removing N-terminal methionine from proteins, is a drug target in angiogenesis, cancer, and obesity; inhibitors include fumagillin, TNP-470, beloranib, and M8891, none yet approved.
Peptidase M17, peptidase B
Peptidase M17 (leucyl aminopeptidase, peptidase B, EC 3.4.11.1) is a hexameric zinc-dependent aminopeptidase family with a binuclear metal center that cleaves N-terminal leucine-like residues; a validated antimalarial and antibacterial drug target.