Metabolic conditions determining the composition and catalytic activity of cytochrome P-450 monooxygenases in Candida tropicalis

J Bacteriol. 1984 Jan;157(1):297-302. doi: 10.1128/jb.157.1.297-302.1984.


In the microsomal fraction of Candida tropicalis cells, two distinct monooxygenases were detected, depending on the growth conditions. The distinction of the two monooxygenases was evident from: (i) the absorption maxima in the reduced CO difference spectra of the terminal oxidases (cytochromes P-450 and P-448); (ii) the contents of the monooxygenase components (cytochromes P-450/P-448, NADPH-cytochrome c (P-450) reductase, and cytochrome b5) and (iii) the catalytic activity of the complete system (aliphatic hydroxylation and N-demethylation activity). The occurrence of the respective monooxygenases could be related to the carbon source (n-alkanes or glucose). Oxygen limitation led to a significant increase of cytochrome P-450/P-448 content, independent of the carbon source utilized by the cells. An improved method for the isolation of microsomes enabled us to demonstrate the presence of cytochrome P-448 in glucose-grown cells.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alkanes / metabolism
  • Candida / analysis
  • Candida / enzymology*
  • Catalysis
  • Culture Media / metabolism
  • Cytochrome P-450 Enzyme System
  • Cytochromes / analysis
  • Glucose / metabolism
  • Microsomes / analysis
  • Microsomes / enzymology
  • Oxygenases / analysis
  • Oxygenases / metabolism*


  • Alkanes
  • Culture Media
  • Cytochromes
  • Cytochrome P-450 Enzyme System
  • Oxygenases
  • Glucose