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Dissecting the paradoxical effects of hydrogen bond mutations in the ketosteroid isomerase oxyanion hole

The catalytic importance of enzyme active-site interactions is frequently assessed by mutating specific residues and measuring the resulting rate reductions. This approach has been used in bacterial ketosteroid isomerase to probe the energetic importance of active-site hydrogen bonds donated to the...

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Détails bibliographiques
Auteurs principaux: Kraut, Daniel A., Sigala, Paul A., Fenn, Timothy D., Herschlag, Daniel
Format: Artigo
Langue:Inglês
Publié: National Academy of Sciences 2010
Sujets:
Accès en ligne:https://ncbi.nlm.nih.gov/pmc/articles/PMC2836627/
https://ncbi.nlm.nih.gov/pubmed/20080683
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.0911168107
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