Fatty acid hydroxylase of the fungus Fusarium oxysporum is possibly a fused protein of cytochrome P-450 and its reductase

Biochem Biophys Res Commun. 1994 Jul 15;202(1):586-90. doi: 10.1006/bbrc.1994.1968.


Fatty acid subterminal (omega-1 approximately omega-3) hydroxylase of the fungus Fusarium oxysporum was solubilized from the microsomal fraction and partially purified. The hydroxylase activity was recovered into a single active fraction, and its spectral nature showed the presence of cytochrome P-450 (P-450). Fatty acid hydroxylase activity was markedly restored upon addition of FAD, FMN, and/or hemin to the eluted fraction. The fraction also exhibited other properties characteristic of both a hemeprotein and a flavin-containing reductase. These results are highly indicative that the fungal hydroxylase is a fused protein containing both P-450 and its reductase domains. In this aspect the fungal enzyme resembles bacterial P-450BM3, although it is membrane-bound unlike the bacterial counterpart.

MeSH terms

  • Chromatography, Affinity
  • Cytochrome P-450 CYP4A
  • Cytochrome P-450 Enzyme System / chemistry
  • Cytochrome P-450 Enzyme System / isolation & purification
  • Cytochrome P-450 Enzyme System / metabolism*
  • Fusarium / enzymology*
  • Kinetics
  • Microsomes / enzymology*
  • Mixed Function Oxygenases / chemistry
  • Mixed Function Oxygenases / isolation & purification
  • Mixed Function Oxygenases / metabolism*
  • Multienzyme Complexes / chemistry
  • Multienzyme Complexes / isolation & purification*
  • Multienzyme Complexes / metabolism
  • NADPH-Ferrihemoprotein Reductase / chemistry
  • NADPH-Ferrihemoprotein Reductase / isolation & purification
  • NADPH-Ferrihemoprotein Reductase / metabolism*
  • Solubility
  • Spectrophotometry


  • Multienzyme Complexes
  • Cytochrome P-450 Enzyme System
  • Mixed Function Oxygenases
  • Cytochrome P-450 CYP4A
  • NADPH-Ferrihemoprotein Reductase