Metabolism of monoterpenes: demonstration of the hydroxylation of (+)-sabinene to (+)-cis-sabinol by an enzyme preparation from sage (Salvia officinalis) leaves

Arch Biochem Biophys. 1987 Jul;256(1):179-93. doi: 10.1016/0003-9861(87)90436-x.


A microsomal preparation from the epidermis of Salvia officinalis leaves catalyzed the NADPH- and O2-dependent hydroxylation of the monoterpene olefin (+)-sabinene to (+)-cis-sabinol. The reaction catalyzed is a key step in the biosynthesis of C3-oxygenated thujane monoterpenes, and the hydroxylase is highly specific for (+)-sabinene as substrate. The hydroxylase from leaf homogenates was solubilized and characterized with regard to reaction conditions, inhibitors, and activators. Activity was partially inhibited by rabbit anti-rat cytochrome P-450 and by CO, and the latter inhibition was reversed by 450 nm light. A CO-difference spectrum and type I substrate binding spectrum were obtained. The hydroxylase meets most of the established criteria for a cytochrome P-450-dependent mixed function oxygenase and represents one of very few enzyme systems of this type to be isolated from leaves of a higher plant.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Bicyclic Monoterpenes
  • Carbon Monoxide / pharmacology
  • Cytochrome P-450 Enzyme System / metabolism
  • Hydroxylation
  • Microsomes / metabolism
  • Mixed Function Oxygenases / antagonists & inhibitors
  • Mixed Function Oxygenases / metabolism
  • Monoterpenes*
  • NADPH-Ferrihemoprotein Reductase / metabolism
  • Phospholipids / metabolism
  • Plants / enzymology
  • Plants / metabolism*
  • Solubility
  • Substrate Specificity
  • Terpenes / biosynthesis*
  • Terpenes / metabolism*


  • Bicyclic Monoterpenes
  • Monoterpenes
  • Phospholipids
  • Terpenes
  • sabinol
  • sabinene
  • Carbon Monoxide
  • Cytochrome P-450 Enzyme System
  • Mixed Function Oxygenases
  • NADPH-Ferrihemoprotein Reductase