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Effects of hydrostatic pressure on horse liver alcohol dehydrogenase (HLADH): a new way of analyzing kinetic study
M Trovaslet1, M D Legoy, S Dallet-Choisy
1Laboratoire de Biotechnologie et de Chimie Bioorganique, Université de La Rochelle, La Rochelle, France.
Abstract:
Oxidation of ethanol by horse liver alcohol dehydrogenase (HLADH) is monitored under pressure (0.1 MPa - 225 MPa). The pressure-induced modifications of catalytic activity are followed by plotting reaction velocities as a function of substrates concentrations in the traditional double reciprocal form: then, pressure is treated as an activator (p < 100 MPa) or an inhibitor (p<225 MPa). Surprising typical patterns of Lineweaver-Burk curves are observed and interpreted. These results suggest that this approach could be a powerful tool to study enzyme's structure-activity relationship.
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