title: Substrate specificity of an acylaminopeptidase that catalyzes the cleavage of the blocked amino termini of peptides.
abstract: An acylaminopeptidase purified from human red cells cleaves acetylated dipeptides in the decreasing order of acetyl-Ala, acetyl-Met, acetyl-Ser, acetyl-Gly and acetyl-Val. In addition, it was also found that the nature of the second amino-acid residue influenced the rate of cleavage of the blocked N-terminus: charged residues at the second position lead to reduced rates of cleavage. The possible use of this enzyme for structural studies on blocked peptide or protein substrates is evaluated.
mesh_terms: D000409:Alanine / Q000031:analogs & derivatives / Q000097:blood; D000626:Aminopeptidases / Q000097:blood*; D004151:Dipeptides / Q000378:metabolism*; D004912:Erythrocytes / Q000201:enzymology*; D005998:Glycine / Q000031:analogs & derivatives / Q000378:metabolism; D006801:Humans; D008715:Methionine / Q000031:analogs & derivatives / Q000378:metabolism; D012694:Serine / Q000031:analogs & derivatives / Q000378:metabolism; D013379:Substrate Specificity; D014633:Valine / Q000031:analogs & derivatives / Q000378:metabolism
chemical_list: D004151:Dipeptides; C010530:N-acetylalanine; D012694:Serine; C006379:N-acetylmethionine; D008715:Methionine; D000626:Aminopeptidases; C055588:acylaminopeptidases; D014633:Valine; D000409:Alanine; D005998:Glycine; C006368:aceturic acid; C055589:N-acetylvaline; C012162:N-acetylserine