Characterization of Mutants of Sulfolobus solfataricus Signature Amidase Able to Hydrolyse R-Ketoprofen Amide

Authors: Giordano, Cesare; Ammendola, Sergio

Source: Protein and Peptide Letters, Volume 15, Number 6, July 2008 , pp. 617-623(7)

Publisher: Bentham Science Publishers

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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: Amidase; Enantioselectivity; Modelling; Mutation; R-Ketoprofen

Document Type: Research Article


Publication date: July 1, 2008

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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