Firefly luciferase is a bifunctional enzyme: ATP‐dependent monooxygenase and a long chain fatty acyl‐CoA synthetase
2003; Wiley; Volume: 540; Issue: 1-3 Linguagem: Inglês
10.1016/s0014-5793(03)00272-2
ISSN1873-3468
AutoresYuichi Oba, Makoto Ojika, S Inouye,
Tópico(s)Photoreceptor and optogenetics research
ResumoFirefly 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.
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