Secologanin synthase which catalyzes the oxidative cleavage of loganin into secologanin is a cytochrome P450

Phytochemistry. 2000 Jan;53(1):7-12. doi: 10.1016/s0031-9422(99)00471-9.


Secologanin synthase, an enzyme catalyzing the oxidative cleavage of the cyclopentane ring in loganin to form secologanin, was detected in microsomal preparations from cell suspension cultures of Lonicera japonica. The reaction required NADPH and molecular oxygen, and was blocked by carbon monoxide as well as by several other cytochrome P450 inhibitors, indicating that the reaction was mediated by cytochrome P450. Of the substrates examined, only specificity for loganin was demonstrated. A possible reaction mechanism is described.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Carbon Monoxide / pharmacology
  • Chromatography, High Pressure Liquid
  • Cytochrome P-450 Enzyme Inhibitors
  • Cytochrome P-450 Enzyme System / isolation & purification
  • Cytochrome P-450 Enzyme System / metabolism*
  • Enzyme Inhibitors / pharmacology
  • Glucosides / metabolism*
  • Iridoid Glucosides
  • Iridoids*
  • Magnoliopsida / enzymology*
  • Microsomes / enzymology
  • NADP / metabolism
  • Oxidoreductases Acting on CH-CH Group Donors*
  • Oxygen / metabolism
  • Pyrans / metabolism*
  • Substrate Specificity


  • Cytochrome P-450 Enzyme Inhibitors
  • Enzyme Inhibitors
  • Glucosides
  • Iridoid Glucosides
  • Iridoids
  • Pyrans
  • secologanin
  • NADP
  • Carbon Monoxide
  • Cytochrome P-450 Enzyme System
  • secologanin synthase
  • Oxidoreductases Acting on CH-CH Group Donors
  • loganin
  • Oxygen