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  • Title: Effect of P2' substituents on kinetic constants for hydrolysis by cysteine proteinases.
    Author: García-Echeverría C, Rich DH.
    Journal: Biochem Biophys Res Commun; 1992 Sep 16; 187(2):615-9. PubMed ID: 1530620.
    Abstract:
    Intramolecularly quenched fluorogenic peptide substrates with the general sequence: DABCYL-Lys-Phe-Gly-Gly-Xxx-Ala-EDANS have been utilized to explore the effect of the hydrophobicity of amino acid side chains in the P2' position on the steady-state kinetic constants for papain catalyzed hydrolysis. The results demonstrate that subsite interactions between the enzyme and the peptide substrate modulate the enzyme specificity by slowing the release of the C-terminal product. This series of substrates can be used to characterize substrate specificity studies of other cysteine proteinases.
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