Biochimica et Biophysica Acta 1988-04-14

Substrate specificity of an acylaminopeptidase that catalyzes the cleavage of the blocked amino termini of peptides.

W M Jones, J M Manning

文献索引：Biochim. Biophys. Acta 953(3) , 357-60, (1988)

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摘要

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.