Catalytic Scope of the Thiamine-Dependent Multifunctional Enzyme Cyclohexane-1,2-dione Hydrolase

Kurzanzeige
dc.contributor.authorLoschonsky, Sabrina
dc.contributor.authorWaltzer, Simon
dc.contributor.authorFraas, Sonja
dc.contributor.authorWacker, Tobias
dc.contributor.authorAndrade, Susana L. A.
dc.contributor.authorKroneck, Peter M. H.
dc.contributor.authorMüller, Michael
dc.date.accessioned2015-02-25T14:59:49Z
dc.date.available2015-02-25T14:59:49Z
dc.date.issued2014eng
dc.description.abstractThe thiamine diphosphate (ThDP)-dependent enzyme cyclohexane-1,2-dione hydrolase (CDH) was expressed in Escherichia coli and purified by affinity chromatography (Ni-NTA). Recombinant CDH showed the same C-C bond-cleavage and C-C bond-formation activities as the native enzyme. Furthermore, we have shown that CDH catalyzes the asymmetric cross-benzoin reaction of aromatic aldehydes and (decarboxylated) pyruvate (up to quantitative conversion, 92–99 % ee). CDH accepts also hydroxybenzaldehydes and nitrobenzaldehydes; these previously have not (or only in rare cases) been known as substrates of other ThDP-dependent enzymes. On a semipreparative scale, sterically demanding 4-(tert-butyl)benzaldehyde and 2-naphthaldehyde were transformed into the corresponding 2-hydroxy ketone products in high yields. Additionally, certain benzaldehydes with electron withdrawing substituents were identified as potential inhibitors of the ligase activity of CDH.eng
dc.description.versionpublished
dc.identifier.doi10.1002/cbic.201300673eng
dc.identifier.urihttp://kops.uni-konstanz.de/handle/123456789/30066
dc.language.isoengeng
dc.subjectasymmetric catalysis, C-C bond-formation, carboligation, enzyme catalysis, ThDPeng
dc.subject.ddc570eng
dc.titleCatalytic Scope of the Thiamine-Dependent Multifunctional Enzyme Cyclohexane-1,2-dione Hydrolaseeng
dc.typeJOURNAL_ARTICLEeng
dspace.entity.typePublication
kops.citation.bibtex
@article{Loschonsky2014Catal-30066,
  year={2014},
  doi={10.1002/cbic.201300673},
  title={Catalytic Scope of the Thiamine-Dependent Multifunctional Enzyme Cyclohexane-1,2-dione Hydrolase},
  number={3},
  volume={15},
  issn={1439-4227},
  journal={ChemBioChem},
  pages={389--392},
  author={Loschonsky, Sabrina and Waltzer, Simon and Fraas, Sonja and Wacker, Tobias and Andrade, Susana L. A. and Kroneck, Peter M. H. and Müller, Michael}
}
kops.citation.iso690LOSCHONSKY, Sabrina, Simon WALTZER, Sonja FRAAS, Tobias WACKER, Susana L. A. ANDRADE, Peter M. H. KRONECK, Michael MÜLLER, 2014. Catalytic Scope of the Thiamine-Dependent Multifunctional Enzyme Cyclohexane-1,2-dione Hydrolase. In: ChemBioChem. 2014, 15(3), pp. 389-392. ISSN 1439-4227. eISSN 1439-7633. Available under: doi: 10.1002/cbic.201300673deu
kops.citation.iso690LOSCHONSKY, Sabrina, Simon WALTZER, Sonja FRAAS, Tobias WACKER, Susana L. A. ANDRADE, Peter M. H. KRONECK, Michael MÜLLER, 2014. Catalytic Scope of the Thiamine-Dependent Multifunctional Enzyme Cyclohexane-1,2-dione Hydrolase. In: ChemBioChem. 2014, 15(3), pp. 389-392. ISSN 1439-4227. eISSN 1439-7633. Available under: doi: 10.1002/cbic.201300673eng
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kops.sourcefieldChemBioChem. 2014, <b>15</b>(3), pp. 389-392. ISSN 1439-4227. eISSN 1439-7633. Available under: doi: 10.1002/cbic.201300673deu
kops.sourcefield.plainChemBioChem. 2014, 15(3), pp. 389-392. ISSN 1439-4227. eISSN 1439-7633. Available under: doi: 10.1002/cbic.201300673deu
kops.sourcefield.plainChemBioChem. 2014, 15(3), pp. 389-392. ISSN 1439-4227. eISSN 1439-7633. Available under: doi: 10.1002/cbic.201300673eng
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temp.internal.duplicates<p>Keine Dubletten gefunden. Letzte Überprüfung: 10.12.2014 16:06:13</p>deu

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