8-dimethylallylnaringenin 2'-hydroxylase, the Crucial Cytochrome P450 Mono-Oxygenase for Lavandulylated Flavanone Formation in Sophora Flavescens Cultured Cells

Phytochemistry. 2001 Nov;58(5):671-6. doi: 10.1016/s0031-9422(01)00270-9.

Abstract

8-dimethylallylnaringenin (8-DMAN) 2'-hydroxylase, which is indispensable for the formation of a lavandulylated flavanone, sophoraflavanone G, was detected in cell suspension cultures of Sophora flavescens. The enzyme catalyzes the 2'-hydroxylation of 8-DMAN to leachianone G, and is tightly bound to the membrane. It required NADPH and molecular oxygen as cofactors, and was inhibited by several cytochrome P450 inhibitors such as carbon monoxide and cytochrome c, indicating that the reaction is mediated by a cytochrome P450 monooxygenase. The optimum pH of 8-DMAN 2'-hydroxylase was 8.5, and the enzyme hydroxylated only 8-DMAN. Apparent Km values for 8-DMAN and NADPH of the enzyme were 55 and 34 microM, respectively.

MeSH terms

  • Carbon Monoxide / metabolism
  • Cells, Cultured / enzymology
  • Cytochrome P-450 Enzyme System / metabolism*
  • Flavanones*
  • Flavonoids / metabolism*
  • Hydroxylation
  • Mixed Function Oxygenases / metabolism*
  • NADP / metabolism
  • Sophora / enzymology*
  • Sophora / metabolism

Substances

  • Flavanones
  • Flavonoids
  • NADP
  • Carbon Monoxide
  • Cytochrome P-450 Enzyme System
  • vexibinol
  • Mixed Function Oxygenases
  • 8-dimethylallylnaringenin 2'-hydroxylase
  • flavanone