Purification and properties of a nicotinamide adenine dinucleotide-linked cyclohexanol dehydrogenase from aNocardia species

Stirling, Lynne A.; Perry, Jerome J.

doi:10.1007/bf02602889

Cited by 4 publications

(3 citation statements)

References 19 publications

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“…CDH from R. erythropolis has a unique substrate specificity in comparison with previously reported (secondary) alcohol dehydrogenases (63)(64)(65). The enzyme has a preference for substituted cyclohexanols and does not catalyze the oxidation of primary or short chain aliphatic secondary alcohols.…”

Section: Discussionmentioning

confidence: 80%

Stereoselective Carveol Dehydrogenase from Rhodococcus erythropolis DCL14

Werf

Ven

Barbirato

et al. 1999

Journal of Biological Chemistry

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A novel nicotinoprotein, catalyzing the dichlorophenolindophenol-dependent oxidation of carveol to carvone, was purified to homogeneity from Rhodococcus erythropolis DCL14. The enzyme is specifically induced after growth on limonene and carveol. Dichlorophenolindophenol-dependent carveol dehydrogenase (CDH) is a homotetramer of 120 kDa with each subunit containing a tightly bound NAD(H) molecule. The enzyme is optimally active at pH 5.5 and 50°C and displays a broad substrate specificity with a preference for substituted cyclohexanols. When incubated with a diastereomeric mixture of (4R)

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Section: Discussionmentioning

confidence: 80%

Stereoselective Carveol Dehydrogenase from Rhodococcus erythropolis DCL14

Werf

Ven

Barbirato

et al. 1999

Journal of Biological Chemistry

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“…Characterization of the cyclohexanol dehydrogenase from each of the species of Xanthobacter with respect to pH optima and molecular weight indicated the two enzymes to be distinctly different from one another. A similar feature shared by the two enzymes was their preferred requirement of NAD+ for enzyme activity, a property displayed by other secondary alcohol dehydrogenases which have so far been characterized (16,17). Analysis of cell extracts from the cyclohexane-grown Xanthobacter sp.…”

Section: Figmentioning

confidence: 83%

Comparative Study of the Ability of Three Xanthobacter Species To Metabolize Cycloalkanes

Magor

Warburton

Trower

et al. 1986

Appl Environ Microbiol

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The ability of three species of Xanthobacter to metabolize cyclohexane and its derivatives has been compared. Xanthobacter flavus was unable to utilize any of the cycloalkanes under investigation. X. autotrophicus was unable to utilize cyclohexane but was able to grow with a limited range of substituted cycloalkanes, including cyclohexanol and cyclohexanone. Comparison of a previously isolated cyclohexane growing Xanthobacter sp. with X. flavus and X. autotrophicus indicated it to be closely related to X. autotrophicus. Studies with cell-free extracts have indicated that the route of metabolism for cyclohexanol by X. autotrophicus is the same as that shown for the cyclohexane growing Xanthobacter sp., proceeding via cyclohexanol-4cyclohexanone-* ecaprolactone-*-* adipic acid. A comparison of the cyclohexanol dehydrogenase found in X. autotrophicus with that found in the cyclohexane-growing Xanthobacter sp. indicated these enzymes to be distinctly different from one another on the basis of substrate specificity, molecular weight, and pH optima. The cyclohexanone monooxygenase enzymes found in the two bacteria were also found to be different when the pH optima and cofactor specificity of the two enzymes were compared. Preliminary genetic studies on the cyclohexane-growing Xanthobacter sp. have indicated that there are no plasmids present in this bacterium. The presence of RP4 in the Xanthobacter sp. can be detected following its conjugation with an RP4-carrying Escherichia coli strain.

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“…Apart from a report by Stirling and Perry [17] concerning the purification and properties of the cyclohexanol dehydrogenase from the cyclohexane-utilising Nocardiu sp., there is no detailed information describing the purification and properties of the enzymes involved in the oxidation of non-substituted cycloalkanes. There have also been few reports describing in detail the degradative enzymes involved in the metabolism of other hydrocarbons by the different species of Xanthobucter genus; the characterisation of a haloalkane dehalogenase from X .…”

Section: Fig 1 Reaction Scheme For the Cyclohexanone-monooxygenllsementioning

confidence: 99%

Characterization of an FMN‐containing cyclohexanone monooxygenase from a cyclohexane‐grown Xanthobacter sp.

Trower

Buckland²,

Griffin

1989

European Journal of Biochemistry

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A soluble cyclohexanone monooxygenase was purified 16.1 -fold to homogeneity from a Xunthobacter sp. grown upon cyclohexane as sole source of carbon and energy. The native enzyme is a 50-kDa single polypeptide chain associated with FMN rather than F A D as flavin prosthetic group in a 1 : 1 stoichiometric relationship. The monooxygenase catalyses the transformation of cyclohexanone to the lactone I-oxa-2-oxocycloheptane in an oxygen ring insertion reaction. Only related cycloalkanone substrates are accepted for oxygenation, no activity is shown towards straight-chain alkanones. Enzyme activity is strongly inhibited by sulphydryl-reactive agents, but is relatively insensitive to metal chelators, electron transport inhibitors and the metal ions Fe3+ and C u 2 + . Cyclohexanone monooxygenase has K, values for cyclohexanone and NADPH of <0.5 pM and 12.5 pM respectively. Kinetic investigations under steady-state conditions demonstrate that the flavoprotein prosthetic group, FMN, is involved in the monooxygenase catalytic mechanism. The systematic name for the enzyme is cyclohexanone, NADPH : oxygen oxidoreductase (6-hydroxylating, 1,2-lactonizing) (EC 1.14.13.22). [5] and substituted cycloalkanes [6]. Members of the genusThe degradation of cyclohexane by a Xunthobucter sp. has been shown to proceed with an initial hydroxylation to form cyclohexanol [5]. This product is then oxidised to adipic acid via cyclohexanone, I-oxa-2-oxocycloheptane and 6-hydroxyhexanoate. Critical to the ring cleavage of cyclohexanone is its transformation to the seven-membered lactone l-oxa-2-oxocycloheptane, a reaction previously shown to be catalysed by an inducible, soluble, NADPH-dependent monooxygenase enzyme [5] (Fig.

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Purification and properties of a nicotinamide adenine dinucleotide-linked cyclohexanol dehydrogenase from aNocardia species

Cited by 4 publications

References 19 publications

Stereoselective Carveol Dehydrogenase from Rhodococcus erythropolis DCL14

Stereoselective Carveol Dehydrogenase from Rhodococcus erythropolis DCL14

Comparative Study of the Ability of Three Xanthobacter Species To Metabolize Cycloalkanes

Characterization of an FMN‐containing cyclohexanone monooxygenase from a cyclohexane‐grown Xanthobacter sp.

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