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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
2008-8-5
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pubmed:abstractText |
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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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:issn |
0929-8665
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
15
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
617-23
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pubmed:meshHeading |
pubmed-meshheading:18680459-Amidohydrolases,
pubmed-meshheading:18680459-Amino Acid Sequence,
pubmed-meshheading:18680459-Archaeal Proteins,
pubmed-meshheading:18680459-Catalysis,
pubmed-meshheading:18680459-Catalytic Domain,
pubmed-meshheading:18680459-Hydrolysis,
pubmed-meshheading:18680459-Ketoprofen,
pubmed-meshheading:18680459-Models, Molecular,
pubmed-meshheading:18680459-Molecular Sequence Data,
pubmed-meshheading:18680459-Molecular Structure,
pubmed-meshheading:18680459-Mutation,
pubmed-meshheading:18680459-Protein Structure, Tertiary,
pubmed-meshheading:18680459-Sequence Homology, Amino Acid,
pubmed-meshheading:18680459-Stereoisomerism,
pubmed-meshheading:18680459-Substrate Specificity,
pubmed-meshheading:18680459-Sulfolobus solfataricus
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pubmed:year |
2008
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pubmed:articleTitle |
Characterization of mutants of Sulfolobus solfataricus signature amidase able to hydrolyse R-ketoprofen amide.
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pubmed:affiliation |
CNR - Instituto di Chimica Biomolecolare, "Sapienza" University of Rome, Rome, Italy.
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pubmed:publicationType |
Journal Article
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