Firefly luciferase is a bifunctional enzyme: ATP-dependent monooxygenase and a long chain fatty acyl-CoA synthetase.
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.
Oba
Yuichi
Y
Graduate School of Bioagricultural Sciences, Nagoya University, Chikusa-ku, Nagoya 464-8601, Japan.
Ojika
Makoto
M
Inouye
Satoshi
S
D000217:Acyltransferases / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000378:metabolism*; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D002855:Chromatography, Thin Layer; D001517:Coleoptera / Q000201:enzymology*; D008156:Luciferases / Q000378:metabolism*; D049449:Luminescence; D006899:Mixed Function Oxygenases / Q000378:metabolism*
D000255:Adenosine Triphosphate; D006899:Mixed Function Oxygenases; D008156:Luciferases; D000217:Acyltransferases; C034919:acyl protein synthetase