The hydrolysis of the chromogenic peptide Pro-Thr-Glu-Phe-Phe(4-NO2)-Arg-Leu at the Phe-Phe(4-NO2) bond by nine aspartic proteinases of animal origin and seven enzymes from micro-organisms is described [Phe(4-NO2) is p-nitro-L-phenylalanine]. A further series of six peptides was synthesized in which the residue in the P3 position was systematically varied from hydrophobic to hydrophilic. The Phe-Phe(4-NO2) bond was established as the only peptide bond cleaved, and kinetic constants were obtained for the hydrolysis of these peptide substrates by a representative selection of aspartic proteinases of animal and microbial origin. The value of these water-soluble substrates for structure-function investigations is discussed.
A systematic series of synthetic chromophoric substrates for aspartic proteinases
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B M Dunn, M Jimenez, B F Parten, M J Valler, C E Rolph, J Kay; A systematic series of synthetic chromophoric substrates for aspartic proteinases. Biochem J 1 August 1986; 237 (3): 899–906. doi: https://doi.org/10.1042/bj2370899
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