Work

A systematic series of synthetic chromophoric substrates for aspartic proteinases

Year: 1986

Type: article

Abstract: 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.

Source: Biochemical Journal

DOI: 10.1042/bj2370899

Authors: B M Dunn, M Jimenez, B F Parten, M J Valler, C E Rolph, J Kay

Institutions: University of Florida, University of Wales

Language: English

Topic: Protease and Inhibitor Mechanisms

Subfield: Cancer Research

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funders: Wellcome Trust, National Institutes of Health

Award: MECHANISM OF PEPSIN CATALYSIS AND INHIBITION