Our view of the active site of B.subtilis lipase A shows the tetrahedral intermediate of the acylation reaction with 1-(2-naphthyl)-ethyl-acetate, and the catalytic triad which is formed by S77, H156 and D133. The model was built using a crystal structure of B.subtilis lipase A and knowledge of the binding modes of lipases. Molecular modeling techniques used to refine the geometry range from simple molecular mechanics in the early stages to more elaborate combined quantum and molecular mechanical methods in the final stages of optimization. All calculations were performed in the presence of explicit solvent, which is omitted here for sake of a clearer view. For details, see Funke et al., pages 509–514.
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