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Multiple forms of cyclohexanone oxygenase from Nocardia globerula CL1.

D B Norris, P W Trudgill

    European Journal of Biochemistry
    |March 16, 1976
    PubMed
    Summary

    Nocardia globerula CL1 possesses two distinct forms of cyclohexanone monooxygenase, differing in pH and temperature stability. These enzyme variants may provide an ecological advantage to the bacterium.

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    Area of Science:

    • Biochemistry
    • Microbial enzymology
    • Molecular biology

    Background:

    • Cyclohexanone 1,2-monooxygenase is an enzyme found in Nocardia globerula CL1.
    • This enzyme is crucial for microbial metabolism and has potential biotechnological applications.

    Purpose of the Study:

    • To investigate the distinct forms of cyclohexanone monooxygenase in Nocardia globerula CL1.
    • To characterize the biochemical and physical properties of these enzyme variants.
    • To explore the potential ecological significance of multiple enzyme forms.

    Main Methods:

    • Enzyme isolation and purification using preparative polyacrylamide gel electrophoresis.
    • Characterization of kinetic, spectral, pH-activity, and temperature stability profiles.
    • Quantification of enzyme levels in soluble protein extracts.

    Main Results:

    • Two electrophoretically distinct forms of cyclohexanone monooxygenase were identified and separated.
    • Both forms exhibited similar kinetic, spectral, and physical properties.
    • Differences were observed in their pH-activity profiles and temperature stability.
    • Cyclohexanone oxygenase represented 8% of the induced cells' soluble protein.

    Conclusions:

    • The two cyclohexanone monooxygenase forms are intrinsic to Nocardia globerula CL1, not purification artifacts.
    • The high abundance of this enzyme suggests potential gene duplication, conferring an ecological advantage.
    • Further research is needed to determine if these are conformational isoenzymes or products of divergent evolution.

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