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  • Title: Kinetic studies on the mechanism and the specificity of peptide semisynthesis catalyzed by the serine proteases alpha-chymotrypsin and beta-trypsin.
    Author: Riechmann L, Kasche V.
    Journal: Biochem Biophys Res Commun; 1984 Apr 30; 120(2):686-91. PubMed ID: 6732779.
    Abstract:
    The mechanism of peptide semisynthesis catalyzed by alpha-chymotrypsin and beta-trypsin has been investigated. The dependence of the apparent ratio of the second order rate constants for the deacylation of the acyl-enzyme intermediate by water and other nucleophiles (amino acid amides) on the nucleophile concentration indicates a mechanism that involves two acyl-enzymes. One with and one without bound nucleophile that both can be deacylated by water. The nucleophile specificity in peptide semisynthesis catalyzed by the proteases was found to reflect the P1-specificity in the corresponding hydrolytic reaction.
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