Substrate specificity of an acylaminopeptidase that catalyzes the cleavage of the blocked amino termini of peptides
1988; Elsevier BV; Volume: 953; Linguagem: Inglês
10.1016/0167-4838(88)90045-3
ISSN1878-1454
AutoresWanda M. Jones, James M. Manning,
Tópico(s)Pancreatic function and diabetes
ResumoAn 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.
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