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• W2014231806 endingPage "2760" @default.
• W2014231806 startingPage "2753" @default.
• W2014231806 abstract "ABSTRACT A gene, badH , whose predicted product is a member of the short-chain dehydrogenase/reductase family of enzymes, was recently discovered during studies of anaerobic benzoate degradation by the photoheterotrophic bacterium Rhodopseudomonas palustris . Purified histidine-tagged BadH protein catalyzed the oxidation of 2-hydroxycyclohexanecarboxyl coenzyme A (2-hydroxychc-CoA) to 2-ketocyclohexanecarboxyl-CoA. These compounds are proposed intermediates of a series of three reactions that are shared by the pathways of cyclohexanecarboxylate and benzoate degradation used by R. palustris . The 2-hydroxychc-CoA dehydrogenase activity encoded by badH was dependent on the presence of NAD + ; no activity was detected with NADP + as a cofactor. The dehydrogenase activity was not sensitive to oxygen. The enzyme has apparent K m values of 10 and 200 μM for 2-hydroxychc-CoA and NAD + , respectively. Western blot analysis with antisera raised against purified His-BadH identified a 27-kDa protein that was present in benzoate- and cyclohexanecarboxylate-grown but not in succinate-grown R. palustris cell extracts. The active form of the enzyme is a homotetramer. badH was determined to be the first gene in an operon, termed the cyclohexanecarboxylate degradation operon, containing genes required for both benzoate and cyclohexanecarboxylate degradation. A nonpolar R. palustris badH mutant was unable to grow on benzoate or cyclohexanecarboxylate but had wild-type growth rates on succinate. Cells blocked in expression of the entire cyclohexanecarboxylate degradation operon excreted cyclohex-1-ene-1-carboxylate into the growth medium when given benzoate. This confirms that cyclohex-1-ene-1-carboxyl-CoA is an intermediate of anaerobic benzoate degradation by R. palustris . This compound had previously been shown not to be formed by Thauera aromatica , a denitrifying bacterium that degrades benzoate by a pathway that is slightly different from the R. palustris pathway. 2-Hydroxychc-CoA dehydrogenase does not participate in anaerobic benzoate degradation by T. aromatica and thus may serve as a useful indicator of an R. palustris -type benzoate degradation pathway." @default.
• W2014231806 created "2016-06-24" @default.
• W2014231806 creator A5077489422 @default.
• W2014231806 creator A5082704150 @default.
• W2014231806 date "2000-05-15" @default.
• W2014231806 modified "2023-10-16" @default.
• W2014231806 title "2-Hydroxycyclohexanecarboxyl Coenzyme A Dehydrogenase, an Enzyme Characteristic of the Anaerobic Benzoate Degradation Pathway Used by <i>Rhodopseudomonas palustris</i>" @default.
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• W2014231806 doi "https://doi.org/10.1128/jb.182.10.2753-2760.2000" @default.
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