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

Fraas, Sonja; Steinbach, Alma K.; Tabbert, Anja; Harder, Jens; Ermler, Ulrich; Tittmann, Kai; Meyer, Axel; Kroneck, Peter M.H.

doi:10.1016/j.molcatb.2009.03.021

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

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Harder, Jens
Department of Microbiology, Max Planck Institute for Marine Microbiology, Max Planck Society;

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Citation

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.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0024-D7C4-D

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