Slow-binding inhibition of soybean lipoxygenase-1 by luteolin

Arch Pharm Res. 2012 Oct;35(10):1811-6. doi: 10.1007/s12272-012-1014-x. Epub 2012 Nov 9.

Abstract

Luteolin, isolated from the seeds of Perilla frutescens (perilla seeds), inhibited the peroxidation of linoleic acid catalyzed by soybean lipoxygenase-1 (EC 1.13.11.12, Type 1) with an IC(50) of 5.0 M (1.43 μg/mL) noncompetitively. The progress curves for an enzyme reaction indicate that luteolin shows slow binding kinetics. Both the initial velocity and steady-state rate in the progress curve were decreased with increasing the concentration of luteolin. The kinetic parameters, which described the inhibition by luteolin, were evaluated by nonlinear regression fits.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Chromatography, High Pressure Liquid
  • Glycine max / enzymology*
  • Kinetics
  • Lipid Peroxidation / drug effects
  • Lipoxygenase / metabolism*
  • Lipoxygenase Inhibitors / isolation & purification
  • Lipoxygenase Inhibitors / pharmacology*
  • Luteolin / isolation & purification
  • Luteolin / pharmacology*
  • Molecular Structure
  • Oxidation-Reduction
  • Perilla / chemistry*
  • Protein Binding
  • Seeds / chemistry
  • Time Factors

Substances

  • Lipoxygenase Inhibitors
  • Lipoxygenase
  • Luteolin