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2000
Volume 15, Issue 6
  • ISSN: 0929-8665
  • E-ISSN: 1875-5305

Abstract

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.

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/content/journals/ppl/10.2174/092986608784966949
2008-07-01
2025-05-06
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/content/journals/ppl/10.2174/092986608784966949
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  • Article Type:
    Research Article
Keyword(s): Amidase; Enantioselectivity; Modelling; Mutation; R-Ketoprofen
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