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Rational design of ...
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Ottosson, JennyKTH,Bioteknologi
(author)
Rational design of enantio selective enzymes requires considerations of entropy
- Article/chapterEnglish2001
Publisher, publication year, extent ...
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Wiley,2001
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Numbers
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LIBRIS-ID:oai:DiVA.org:kth-13385
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https://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-13385URI
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https://doi.org/10.1110/ps.13501DOI
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Language:English
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Summary in:English
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Subject category:ref swepub-contenttype
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Subject category:art swepub-publicationtype
Notes
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QC 20100616
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Entropy was shown to play an equally important role as enthalpy for how enantioselectivity changes when redesigning an enzyme. By studying the temperature dependence of the enantiomeric ratio E of an enantioselective enzyme, its differential activation enthalpy (Delta (R-S)DeltaH(double dagger)) and entropy (Delta (R-S)DeltaS(double dagger)) components can be determined. This was done for the resolution of 3-methyl-2-butanol catalyzed by Candida antarctica lipase B and five variants with one or two point mutations. Delta (R-S)DeltaS(double dagger) was in all cases equally significant as Delta (R-S)DeltaH(double dagger) to E. One variant, T103G, displayed an increase in E, the others a decrease. The altered enantioselectivities of the variants were all related to simultaneous changes in Delta (R-S)DeltaH(double dagger) and Delta (R-S)DeltaS(double dagger). Although the changes in Delta (R-S)DeltaH(double dagger) and Delta (R-S)DeltaS(double dagger) were of a compensatory nature the compensation was not perfect, thereby allowing modifications of E. Both the W104H and the T103G variants displayed larger Delta (R-S)DeltaH(double dagger). than wild type but exhibited a decrease or increase, respectively, in E due to their different relative increase in Delta (R-S)DeltaS(double dagger).
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Rotticci-Mulder, C
(author)
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Rotticci, D
(author)
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Hult, KarlKTH,Bioteknologi(Swepub:kth)u1nzlwuj
(author)
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KTHBioteknologi
(creator_code:org_t)
Related titles
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In:Protein Science: Wiley10:9, s. 1769-17740961-83681469-896X
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