Journal
RUSSIAN JOURNAL OF BIOORGANIC CHEMISTRY
Volume 29, Issue 5, Pages 434-440Publisher
MAIK NAUKA/INTERPERIODICA/SPRINGER
DOI: 10.1023/A:1026097308513
Keywords
alpha-chymotrypsin in water-DMSO mixtures; mechanism of interaction with DMSO
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The kinetic behavior of alpha-chymotrypsin was studied in water-DMSO mixtures at concentrations of the organic solvent that do not cause irreversible denaturation of the enzyme. Various substrates (N-substituted derivatives of L-tyrosine) were found to display substantially different kinetic patterns of interaction with alpha-chymotrypsin, which can be described by totally different kinetic schemes. The differences were ascribed to competition between the N-acyl group of the substrate and the DMSO molecule at the S-2 site of substrate binding to the active site of the enzyme.
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