title: The empirical valence bond as an effective strategy for computer-aided enzyme design.
abstract: The ability of the empirical valence bond (EVB) to be used in screening active site residues in enzyme design is explored in a preliminary way. This validation is done by comparing the ability of this approach to evaluate the catalytic contributions of various residues in chorismate mutase. It is demonstrated that the EVB model can serve as an accurate tool in the final stages of computer-aided enzyme design (CAED). The ability of the model to predict quantitatively the catalytic power of enzymes should augment the capacity of current approaches for enzyme design.
authors.affiliation: Department of Chemistry, University of Southern California, Los Angeles, USA.
authors.forename: Alexandra
authors.initials: A
authors.lastname: Vardi-Kilshtain
authors.forename: Maite
authors.initials: M
authors.lastname: Roca
authors.forename: Arieh
authors.initials: A
authors.lastname: Warshel
mesh_terms: D019943:Amino Acid Substitution; D001120:Arginine / Q000378:metabolism; D001665:Binding Sites; D002384:Catalysis; D002826:Chorismate Mutase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D003198:Computer Simulation; D017076:Computer-Aided Design; D019281:Dimerization; D004789:Enzyme Activation; D004798:Enzymes / Q000737:chemistry* / Q000235:genetics; D007700:Kinetics; D008956:Models, Chemical; D008958:Models, Molecular; D055672:Static Electricity; D013329:Structure-Activity Relationship; D013816:Thermodynamics; D014633:Valine / Q000378:metabolism; D014867:Water / Q000737:chemistry
chemical_list: D004798:Enzymes; D014867:Water; D001120:Arginine; D002826:Chorismate Mutase; D014633:Valine