[Interaction of alpha-chymotrypsin with dimethylsulfoxide: a change of substrate could change the mechanism of interaction].
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 S2-site of substrate binding to the active site of the enzyme.
Eremeev
N L
NL
Faculty of Chemistry, Moscow State University, Vorob'evy gory, Moscow, 119992 Russia. eremeev@enzyme.chem.msu.ru
D002918:Chymotrypsin / Q000737:chemistry / Q000378:metabolism*; D004121:Dimethyl Sulfoxide / Q000737:chemistry / Q000378:metabolism*; D007700:Kinetics; D011489:Protein Denaturation; D013379:Substrate Specificity
D002918:Chymotrypsin; C117608:alpha-chymotrypsin; D004121:Dimethyl Sulfoxide