Cyclohexane-1,2-dione hydrolase : A new tool to degrade alicyclic compounds

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2009
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Steinbach, Alma K.
Tabbert, Anja
Harder, Jens
Ermler, Ulrich
Tittmann, Kai
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Journal of Molecular Catalysis / B, Enzymatic. 2009, 61(1-2), pp. 47-49. ISSN 1381-1177. Available under: doi: 10.1016/j.molcatb.2009.03.021
Zusammenfassung

Alicyclic alcohols are naturally occurring compounds which can be degraded by microorganisms via cleavage of the ring C-C bond. Denitrifying Azoarcus sp. strain 22Lin grows on cyclohexane-1,2-diol which serves as electron donor and carbon source. The diol is converted to cyclohexane-1,2-dione followed by hydrolysis to the corresponding semialdehyde and oxidation to adipate. The latter two reactions are catalyzed by the thiamine diphosphate-dependent llavoenzyme cyciohexane-1,2-dione hydrolase, the first α-ketolase known so far. Biochemical and structural properties of this new member of the thiamine diphosphate enzyme family will be presented.

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540 Chemie
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Cyclic alcohols, Cyclohexane-1.2-dione hydrolase, Thiamine diphosphate, Flavoenzyme
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ISO 690FRAAS, Sonja Iris, Alma K. STEINBACH, Anja TABBERT, Jens HARDER, Ulrich ERMLER, Kai TITTMANN, Axel MEYER, Peter M. H. KRONECK, 2009. Cyclohexane-1,2-dione hydrolase : A new tool to degrade alicyclic compounds. In: Journal of Molecular Catalysis / B, Enzymatic. 2009, 61(1-2), pp. 47-49. ISSN 1381-1177. Available under: doi: 10.1016/j.molcatb.2009.03.021
BibTex
@article{Fraas2009Cyclo-9816,
  year={2009},
  doi={10.1016/j.molcatb.2009.03.021},
  title={Cyclohexane-1,2-dione hydrolase : A new tool to degrade alicyclic compounds},
  number={1-2},
  volume={61},
  issn={1381-1177},
  journal={Journal of Molecular Catalysis / B, Enzymatic},
  pages={47--49},
  author={Fraas, Sonja Iris and Steinbach, Alma K. and Tabbert, Anja and Harder, Jens and Ermler, Ulrich and Tittmann, Kai and Meyer, Axel and Kroneck, Peter M. H.}
}
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