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

FEBS Letters

Oba, Yuichi¹  Inouye, Satoshi²  Ojika, Makoto¹ 

[1] Graduate School of Bioagricultural Sciences, Nagoya University, Chikusa-ku, Nagoya 464-8601, Japan;Yokohama Research Center, Chisso Co., 5-1 Okawa, Kanazawa-ku, Yokohama 236-8605, Japan

关键词: Bioluminescence;    Luciferin;    CoA ligase;    Adenylation;    Intermediate;    β-Oxidation;    CoA;    coenzyme A;    HPLC;    high performance liquid chromatography;    MALDI-TOF-MS;    matrix-assisted laser desorption/ionization time-of-flight mass spectrometry;    TLC;    thin-layer chromatography;   

DOI  :  10.1016/S0014-5793(03)00272-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 (C₁₆–C₂₀), 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.

【 授权许可】

Unknown