PMID: 4312Mar 16, 1976

Multiple forms of cyclohexanone oxygenase from Nocardia globerula CL1

European Journal of Biochemistry
D B Norris, P W Trudgill


The cyclohexanone 1,2-monooxygenase of Nocardia globerula CL1 exists as two electrophoretically distinct forms. These are present in crude cell extracts and are not artifacts of enzyme purification or electrophoresis. They have been separated in mg amounts by preparative polyacrylamide gel electrophoresis and shown to have essentially identical kinetic, spectral and physical characteristics. They do differ in pH-activity profile and temperature stability. Whether or not they are conformational isoenzymes or arise by gene duplication and divergent evolution has not been established. Cyclohexanone oxygenase constitutes 8% of the soluble protein of induced cells. This high level would correlate well with the presence of duplicate genes. It is proposed that the presence of a large amount of cyclohexanone oxygenase may confer an ecological advantage on the organism.


Mar 16, 1976·European Journal of Biochemistry·M Griffin, P W Trudgill
Jun 14, 1968·Annals of the New York Academy of Sciences·D Wellner, M B Hayes
Sep 1, 1969·Analytical Biochemistry·J R Florini, R P Brivio
Jan 1, 1963·Biochemistry·R L PRAIRIE, P TALALAY
Dec 28, 1964·Annals of the New York Academy of Sciences·B J DAVIS
Mar 29, 1965·Biochimica Et Biophysica Acta·L J ROGERS
Aug 1, 1960·Biochemical and Biophysical Research Communications·R SHAPIRA, S PARKER
Nov 2, 1961·Annals of the New York Academy of Sciences·E MARGOLIASH, J LUSTGARTEN

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Drug Stability
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