AI Article Synopsis
- Firefly luciferase shares similarities with fatty acyl-CoA synthetases found in non-luminescent insects.
- Researchers determined the crystal structure of a specific enzyme from fruit flies (CG6178) and created an artificial luciferase named FruitFire by mutating its active site.
- FruitFire significantly improved bioluminescence imaging in mice, demonstrating the potential for engineering bioluminescence in various enzymes from non-luminescent organisms for future applications.
Article Abstract
Firefly 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.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10327219 | PMC |
| http://dx.doi.org/10.1101/2023.06.30.547126 | DOI Listing |
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