A novel ketone monooxygenase from Pseudomonas cepacia. Purification and properties.

@article{Britton1977ANK,
  title={A novel ketone monooxygenase from Pseudomonas cepacia. Purification and properties.},
  author={L. N. Britton and A. J. Markovetz},
  journal={The Journal of biological chemistry},
  year={1977},
  volume={252 23},
  pages={
          8561-6
        }
}
A ketone monooxygenase was purified from cells of Pseudomonas cepacia grown on 2-tridecanone as sole carbon source. Enzyme stability is maintained by the addition of ethanol, EDTA, and dithiothreitol. Stoichiometric studies show that for 1 mol of undecyl acetate formed, 1 mol of O2 is consumed and 1 mol of NADPH is oxidized. The monooxygenase, purified to homogeneity, has a molecular weight of approximately 123,000 and consists of two equal subunits with molecular weights of 55,000. The enzyme… Expand
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