Sandbox GGC3

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== Function ==
== Function ==
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[[Image:Common_Eastern_Firefly.jpg|thumb|left|upright=1.1|The Common Eastern Firefly in a hand emitting a yellow hue, showing bioluminescence.]]
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[[Image:Common_Eastern_Firefly.jpg|thumb|left|upright=1.1|The Common Eastern Firefly in a hand emitting a yellow hue, showing bioluminescence.[https://www.wnpr.org/post/how-chemistry-behind-fireflys-glow-could-lead-innovations-medicine]]]
The ANL enzymes catalyze two-step reactions: the first an adenylating step in which an acyl-AMP intermediate is produced; the second step in which the adenylate then serves as a substrate for the multistep oxidative decarboxylation of the luciferyl-AMP (LH<sub>2</sub>-AMP) intermediate, resulting in bioluminescence.
The ANL enzymes catalyze two-step reactions: the first an adenylating step in which an acyl-AMP intermediate is produced; the second step in which the adenylate then serves as a substrate for the multistep oxidative decarboxylation of the luciferyl-AMP (LH<sub>2</sub>-AMP) intermediate, resulting in bioluminescence.
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== Relevance ==
== Relevance ==
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[[Image:Photinus_pyralis.jpg|thumb|left|The Common Eastern Firefly expressing bioluminescence seen giving off a yellow-green hue.]]
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[[Image:CommonEasternFirefly.jpg|thumb|left|The Common Eastern Firefly expressing bioluminescence seen giving off a yellow-green hue.[https://www.meigspointnaturecenter.org/today-is-firefly-day/]]]
Firefly luciferase has successfully been shown to act as modulatory bioluminescent indicator in the detection and quantification of protein kinase A activation in living cells <ref name="Newby">Sala-Newby, G. B., & Campbell, A. K. (1991). Engineering a bioluminescent indicator for cyclic AMP-dependent protein kinase. “The Biochemical Journal”, 279 (Pt 3), 727–732. https://doi.org/10.1042/bj2790727</ref>. Further, due to its bioluminescent sensitivity, firefly luciferase has been utilized in assays as a genetic reporter in eukaryotic cells<ref name="de">de Wet, J. R., Wood, K. V., DeLuca, M., Helinski, D. R., & Subramani, S. (1987). Firefly luciferase gene: structure and expression in mammalian cells. Molecular and cellular biology, 7(2), 725–737. https://doi.org/10.1128/mcb.7.2.725</ref><ref name="Escherichia">de Wet, J. R., Wood, K. V., Helinski, D. R., & DeLuca, M. (1985). Cloning of firefly luciferase cDNA and the expression of active luciferase in Escherichia coli. Proceedings of the National Academy of Sciences of the United States of America, 82(23), 7870–7873. https://doi.org/10.1073/pnas.82.23.7870</ref><ref name="Throne">Thorne, N., Shen, M., Lea, W. A., Simeonov, A., Lovell, S., Auld, D. S., & Inglese, J. (2012). Firefly luciferase in chemical biology: a compendium of inhibitors, mechanistic evaluation of chemotypes, and suggested use as a reporter. Chemistry & biology, 19(8), 1060–1072. https://doi.org/10.1016/j.chembiol.2012.07.015</ref>, amongst other things.
Firefly luciferase has successfully been shown to act as modulatory bioluminescent indicator in the detection and quantification of protein kinase A activation in living cells <ref name="Newby">Sala-Newby, G. B., & Campbell, A. K. (1991). Engineering a bioluminescent indicator for cyclic AMP-dependent protein kinase. “The Biochemical Journal”, 279 (Pt 3), 727–732. https://doi.org/10.1042/bj2790727</ref>. Further, due to its bioluminescent sensitivity, firefly luciferase has been utilized in assays as a genetic reporter in eukaryotic cells<ref name="de">de Wet, J. R., Wood, K. V., DeLuca, M., Helinski, D. R., & Subramani, S. (1987). Firefly luciferase gene: structure and expression in mammalian cells. Molecular and cellular biology, 7(2), 725–737. https://doi.org/10.1128/mcb.7.2.725</ref><ref name="Escherichia">de Wet, J. R., Wood, K. V., Helinski, D. R., & DeLuca, M. (1985). Cloning of firefly luciferase cDNA and the expression of active luciferase in Escherichia coli. Proceedings of the National Academy of Sciences of the United States of America, 82(23), 7870–7873. https://doi.org/10.1073/pnas.82.23.7870</ref><ref name="Throne">Thorne, N., Shen, M., Lea, W. A., Simeonov, A., Lovell, S., Auld, D. S., & Inglese, J. (2012). Firefly luciferase in chemical biology: a compendium of inhibitors, mechanistic evaluation of chemotypes, and suggested use as a reporter. Chemistry & biology, 19(8), 1060–1072. https://doi.org/10.1016/j.chembiol.2012.07.015</ref>, amongst other things.

Revision as of 20:03, 27 April 2021

Firefly Luciferase

apple juice! B~)

Luciferin-4-monooxygenase. The wild-type luciferase in the adenylate-forming conformation with DLSA (PDB 4G36) and the cross-linked luciferase in the second catalytic conformation with DLSA (PDB 4G37)

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References

  1. ↑ Branchini, B. R., Magyar, R. A., Murtiashaw, M. H., Anderson, S. M., Helgerson, L. C., & Zimmer, M. (1999). Site-directed mutagenesis of firefly luciferase active site amino acids: a proposed model for bioluminescence color. Biochemistry 38(40), 13223–13230. https://doi.org/10.1021/bi991181o
  2. ↑ 2.0 2.1 2.2 2.3 2.4 2.5 2.6 Sundlov, J. A., Fontaine, D. M., Southworth, T. L., Branchini, B. R., Gulick, A. M. (2012). Crystal Structure of Firefly Luciferase in a Second Catalytic Conformation Supports a Domain Alternation Mechanism. Biochemistry 51(33), 6493-6495. https://doi.org/10.1021/bi300934s
  3. ↑ Marahiel, M. A., Stachelhaus, T., Mootz, H. D. (1997). Modular Peptide Synthetases Involved in Nonribosmal Peptide Synthesis. Chemical Reviews 97(7), 2651-2674. https://doi.org/10.1021/cr960029e
  4. ↑ 4.0 4.1 Branchini, B. R., Southworth, T. L., Murtiahsaw, M. H., Wilkinson, S. R., Khattak, N. F., Rosenberg, J. C., & Zimmer, M. (2005). Mutagenesis Evidence that the Partial Reactions of Firefly Bioluminescence are Catalyzed by Different Conformations of the Luciferase C-Terminal Domain. “Biochemistry 44”(5), 1385-1393. https://doi.org/10.1021/bi047903f
  5. ↑ Oba, Y., Ojika, M., Inouye, S. (2003). Firefly luciferase is a bifunctional enzyme: ATP-dependent monoxygenase and a long chain fatty acyl-CoA synthetase. “FEBS Letters 540”(1-3), 251-254. https://doi.org/10.1016/S0014-5793(03)00272-2
  6. ↑ Nakamura, M., Maki, S., Amano, Y., Ohkita, Y., Niwa, K., Hirano, T., Ohmiya, Y., & Niwa, H. (2005). Firefly luciferase exhibits bimodal action depending on the luciferin chirality. “Biochemical and Biophysical Research Communications, 331”(2), 471–475. https://doi.org/10.1016/j.bbrc.2005.03.202
  7. ↑ Branchini, B. R., Murtiashaw, M. H., Magyar, R. A., Anderson, S. M. (2000). The Role of Lysine 529, a Conserved Residue of the Acyl-Adenylate-Forming Enzyme Superfamily, in Firefly Luciferase. Biochemistry 39(18), 5433-5440. https://doi.org/10.1021/bi9928804
  8. ↑ Sala-Newby, G. B., & Campbell, A. K. (1991). Engineering a bioluminescent indicator for cyclic AMP-dependent protein kinase. “The Biochemical Journal”, 279 (Pt 3), 727–732. https://doi.org/10.1042/bj2790727
  9. ↑ de Wet, J. R., Wood, K. V., DeLuca, M., Helinski, D. R., & Subramani, S. (1987). Firefly luciferase gene: structure and expression in mammalian cells. Molecular and cellular biology, 7(2), 725–737. https://doi.org/10.1128/mcb.7.2.725
  10. ↑ de Wet, J. R., Wood, K. V., Helinski, D. R., & DeLuca, M. (1985). Cloning of firefly luciferase cDNA and the expression of active luciferase in Escherichia coli. Proceedings of the National Academy of Sciences of the United States of America, 82(23), 7870–7873. https://doi.org/10.1073/pnas.82.23.7870
  11. ↑ Thorne, N., Shen, M., Lea, W. A., Simeonov, A., Lovell, S., Auld, D. S., & Inglese, J. (2012). Firefly luciferase in chemical biology: a compendium of inhibitors, mechanistic evaluation of chemotypes, and suggested use as a reporter. Chemistry & biology, 19(8), 1060–1072. https://doi.org/10.1016/j.chembiol.2012.07.015
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