The amidase from Sulfolobus solfataricus enantioselectively hydrolyzes S-ketoprofen amide to its corresponding acid. We identify three independent SsAH mutants that hydrolyze R-ketoprofen amide and built computational models of their three-dimensional structure. Interestingly the mutations do not specifically affect residues near the active site, or directly interacting with the substrate.
Keywords: Enantioselectivity, Amidase, Mutation, Modelling, R-Ketoprofen
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Published on: 01 March, 2012
Page: [617 - 623]