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

Fraas, S., Steinbach, A. K., Tabbert, A., Harder, J., Ermler, U., Tittmann, K., et al. (2009). Cyclohexane-1,2-dione hydrolase: A new tool to degrade alicyclic compounds. Journal of Molecular Catalysis B: Enzymatic, 61(1-2), 47-49. doi:10.1016/j.molcatb.2009.03.021.

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 Creators:
Fraas, Sonja1, Author
Steinbach, Alma K.1, Author
Tabbert, Anja1, Author
Harder, Jens2, Author           
Ermler, Ulrich3, Author                 
Tittmann, Kai4, Author
Meyer, Axel1, Author
Kroneck, Peter M.H.1, Author
Affiliations:
1Fachbereich Biologie, Universität Konstanz, 78457 Konstanz, Germany, ou_persistent22              
2Department of Microbiology, Max Planck Institute for Marine Microbiology, Max Planck Society, ou_2481695              
3Department of Molecular Biology, Swedish University of Agricultural Sciences, Uppsala Biomedical Center, Sweden, ou_persistent22              
4Albrecht-von-Haller-Institut, Georg-August-Universität Göttingen, 37077 Göttingen, Germany, ou_persistent22              

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Free keywords: Cyclic alcohols; Cyclohexane-1,2-dione hydrolase; Thiamine diphosphate; Flavoenzyme
 Abstract: 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 flavoenzyme cyclohexane-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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Language(s): eng - English
 Dates: 2009-04-102009-11-01
 Publication Status: Issued
 Pages: 3
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/j.molcatb.2009.03.021
 Degree: -

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Title: Journal of Molecular Catalysis B: Enzymatic
Source Genre: Journal
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Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 61 (1-2) Sequence Number: - Start / End Page: 47 - 49 Identifier: ISSN: 1381-1177
CoNE: https://pure.mpg.de/cone/journals/resource/954925621185