Firefly luciferase is a bifunctional enzyme: ATP-dependent monooxygenase and a long chain fatty acyl-CoA synthetase

FEBS Lett. 2003 Apr 10;540(1-3):251-4. doi: 10.1016/s0014-5793(03)00272-2.

Abstract

Firefly luciferase can catalyze the formation of fatty acyl-CoA via fatty acyl-adenylate from fatty acid in the presence of ATP, Mg(2+) and coenzyme A (CoA). A long chain fatty acyl-CoA (C(16)-C(20)), produced by luciferase from a North American firefly (Photinus pyralis) and a Japanese firefly (Luciola cruciata), was isolated and identified by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry analysis. Of a number of substrates tested, linolenic acid (C(18:3)) and arachidonic acid (C(20:4)) appear to be suitable for acyl-CoA synthesis. This evidence suggests that firefly luciferase within peroxisomes of the cells in the photogenic organ may be a bifunctional enzyme, catalyzing not only the bioluminescence reaction but also the fatty acyl-CoA synthetic reaction.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acyltransferases / metabolism*
  • Adenosine Triphosphate / metabolism*
  • Animals
  • Chromatography, High Pressure Liquid
  • Chromatography, Thin Layer
  • Coleoptera / enzymology*
  • Luciferases / metabolism*
  • Luminescence
  • Mixed Function Oxygenases / metabolism*

Substances

  • Adenosine Triphosphate
  • Mixed Function Oxygenases
  • Luciferases
  • Acyltransferases
  • acyl protein synthetase