Abstract
The partitioning of maleylphenylalanine-α-chymotrypsin formed using maleylphenylalanine methyl ester as acyl donor between amino acid-derived nucleophiles and water was determined spectrophotometrically. The interpretation of the results obtained from graphical analysis gave evidence of a high conformational specificity of α-chymotrypsin towards basic amino acid derivatives in the P′ 1 position including significant differences between the amide and methyl ester of arginine. Amides of neutral amino acids with large side-chains show higher nucleophile reactivity in comparison with glycine amide.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular Enzymology
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