title: Effects of hydrostatic pressure on horse liver alcohol dehydrogenase (HLADH): a new way of analyzing kinetic study.
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.
authors.affiliation: Laboratoire de Biotechnologie et de Chimie Bioorganique, Université de La Rochelle, La Rochelle, France.
authors.forename: M
authors.initials: M
authors.lastname: Trovaslet
authors.forename: M D
authors.initials: MD
authors.lastname: Legoy
authors.forename: S
authors.initials: S
authors.lastname: Dallet-Choisy
mesh_terms: D000426:Alcohol Dehydrogenase / Q000737:chemistry* / Q000378:metabolism*; D000818:Animals; D002384:Catalysis; D000431:Ethanol / Q000378:metabolism; D006736:Horses; D006874:Hydrostatic Pressure; D007700:Kinetics; D008099:Liver; D010084:Oxidation-Reduction
chemical_list: D000431:Ethanol; D000426:Alcohol Dehydrogenase