A spectrophotometric assay for the characterization of the S' subsite specificity of alpha-chymotrypsin.
The partitioning of maleylphenylalanine-alpha-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 alpha-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.
D000818:Animals; D001665:Binding Sites; D002417:Cattle; D002851:Chromatography, High Pressure Liquid; D002918:Chymotrypsin / Q000378:metabolism*; D010455:Peptides / Q000378:metabolism; D010649:Phenylalanine / Q000031:analogs & derivatives / Q000378:metabolism; D012995:Solubility; D013053:Spectrophotometry; D013379:Substrate Specificity
D010455:Peptides; D010649:Phenylalanine; C047139:maleylphenylalanine methyl ester; D002918:Chymotrypsin