Acylpeptide hydrolase: inhibitors and some active site residues of the human enzyme.

摘要: Acylpeptide hydrolase may be involved in N-terminal deacetylation of nascent polypeptide chains and bioactive peptides. The activity this enzyme from human erythrocytes is sensitive to anions such as chloride, nitrate, fluoride. Furthermore, blocked amino acids act competitive inhibitors the enzyme. Acetyl leucine chloromethyl ketone has been employed identify one active site residue His-707. Diisopropylfluorophosphate used a second Ser-587. Chemical modification studies with water-soluble carbodiimide implicate carboxyl group catalytic activity. These results sequence around these residues, especially near Ser-587, suggest that acylpeptide contains triad. presence cysteine vicinity suggested by inactivation sulfhydryl-modifying agents also low amount peptide inhibitor. Ebelactone A, an inhibitor formyl aminopeptidase, bacterial counterpart eukaryotic hydrolase, was found effective findings acylpeptidase member family enzymes extremely diverse functions.