Firefly luciferase exhibits bimodal action depending on the luciferin chirality

Biochem Biophys Res Commun. 2005 Jun 3;331(2):471-5. doi: 10.1016/j.bbrc.2005.03.202.

Abstract

Firefly luciferase is able to convert L-luciferin into luciferyl-CoA even under ordinary aerobic luciferin-luciferase reaction conditions. The luciferase is able to recognize strictly the chirality of the luciferin structure, serving as the acyl-CoA synthetase for L-luciferin, whereas d-luciferin is used for the bioluminescence reaction. D-Luciferin inhibits the luciferyl-CoA synthetase activity of L-luciferin, whereas L-luciferin retards the bioluminescence reaction of D-luciferin, meaning that both enzyme activities are prevented by the enantiomer of its own substrate.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acyl Coenzyme A / chemistry
  • Acyl Coenzyme A / metabolism
  • Animals
  • Chromatography, High Pressure Liquid
  • Coenzyme A / metabolism
  • Firefly Luciferin / chemistry*
  • Firefly Luciferin / metabolism*
  • Luciferases, Firefly / metabolism*
  • Luminescence
  • Luminescent Proteins
  • Molecular Structure
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
  • Stereoisomerism
  • Substrate Specificity

Substances

  • Acyl Coenzyme A
  • Luminescent Proteins
  • luciferyl-coenzyme A
  • Firefly Luciferin
  • Luciferases, Firefly
  • Coenzyme A