4.5 Article

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

Journal

FEBS LETTERS
Volume 540, Issue 1-3, Pages 251-254

Publisher

ELSEVIER SCIENCE BV
DOI: 10.1016/S0014-5793(03)00272-2

Keywords

bioluminescence; luciferin; CoA ligase; adenylation; intermediate; beta-oxidation

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Firefly luciferase can catalyze the formation of fatty acyl-CoA via fatty acyl-adenylate from fatty acid in the presence of ATP, Mg2+ 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 (Lu-ciola 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. (C) 2003 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.

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