title: Thermodynamic Activity-Based Interpretation of Enzyme Kinetics.
abstract: The experimentally determined Michaelis constant Kmresults from a combination of two effects: the recognition of the substrate by the enzyme and the interactions between substrate and solvent. For a solvent-independent analysis of substrate specificity, the thermodynamic activity of the substrate, rather than its concentration, must be considered.
authors.affiliation: Institute of Technical Biochemistry, University of Stuttgart, Allmandring 31, 70569 Stuttgart, Germany. Electronic address: Juergen.Pleiss@itb.uni-stuttgart.de.
authors.forename: Jürgen
authors.initials: J
authors.lastname: Pleiss
mesh_terms: D000446:Aldehyde-Lyases / Q000737:chemistry*; D001573:Benzoin / Q000737:chemistry*; D001665:Binding Sites; D003198:Computer Simulation; D004789:Enzyme Activation; D006588:Hexanones / Q000276:immunology*; D008956:Models, Chemical; D011485:Protein Binding; D013379:Substrate Specificity; D013816:Thermodynamics
chemical_list: D006588:Hexanones; C523189:propioin; D000446:Aldehyde-Lyases; C059416:benzaldehyde lyase; D001573:Benzoin