FruitFire: a luciferase based on a fruit fly metabolic enzyme [preprint]
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AbstractFirefly luciferase is homologous to fatty acyl-CoA synthetases from insects that are not bioluminescent. Here, we determined the crystal structure of the fruit fly fatty acyl-CoA synthetase CG6178 to 2.5 Å. Based on this structure, we mutated a steric protrusion in the active site to create the artificial luciferase FruitFire, which prefers the synthetic luciferin CycLuc2 to D-luciferin by >1000-fold. FruitFire enabled in vivo bioluminescence imaging in the brains of mice using the pro-luciferin CycLuc2-amide. The conversion of a fruit fly enzyme into a luciferase capable of in vivo imaging underscores the potential for bioluminescence with a range of adenylating enzymes from nonluminescent organisms, and the possibilities for application-focused design of enzyme-substrate pairs.
SourceAdams ST, Zephyr J, Bohn MF, Schiffer CA, Miller SC. FruitFire: a luciferase based on a fruit fly metabolic enzyme. bioRxiv [Preprint]. 2023 Jun 30:2023.06.30.547126. doi: 10.1101/2023.06.30.547126. PMID: 37425765; PMCID: PMC10327219.
Permanent Link to this Itemhttp://hdl.handle.net/20.500.14038/52363
NotesThis article is a preprint. Preprints are preliminary reports of work that have not been certified by peer review.
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