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.
Keywords: Enantioselectivity, Amidase, Mutation, Modelling, R-Ketoprofen
Protein & Peptide Letters
Title: Characterization of Mutants of Sulfolobus solfataricus Signature Amidase Able to Hydrolyse R-Ketoprofen Amide
Volume: 15 Issue: 6
Author(s): Cesare Giordano and Sergio Ammendola
Affiliation:
Keywords: Enantioselectivity, Amidase, Mutation, Modelling, R-Ketoprofen
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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Cite this article as:
Giordano Cesare and Ammendola Sergio, Characterization of Mutants of Sulfolobus solfataricus Signature Amidase Able to Hydrolyse R-Ketoprofen Amide, Protein & Peptide Letters 2008; 15 (6) . https://dx.doi.org/10.2174/092986608784966949
DOI https://dx.doi.org/10.2174/092986608784966949 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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