Luciferase

Function

Luciferase (Luc) is an oxidative enzyme used in bioluminescence. It catalyzes the oxidation of the pigment luciferin producing oxyluciferin and light^[1]. See detailed analysis in

See Colored & Bioluminescent Protein.

Relevance

Luc is used in biological research to assess gene transfection into cells where the Luc gene is added to the transfected gene and the light emission by Luc measured for indication of the transfection success^[2].

3D Structures of Luciferase

Updated on 01-June-2025

3iep, 1lci, 5dv9, 3ier – fLuc – firefly

5kyt, 5kyv – fLuc (mutant)
5dwv – fLuc+ substrate analog
1ba3 – fLuc+bromoform
3ies, 3rix, 4e5d – fLuc+inhibitor
4g36 – fLUc + dehydroluciferyl-sulfamoyl adenosine
4g37 – fLUc (mutant) + dehydroluciferyl-sulfamoyl adenosine
2d1q – LcLuc (mutant)+MgATP – Luciola cruciata
2d1r - LcLuc (mutant)+oxyluciferin+AMP
2d1s, 2d1t - LcLuc (mutant)+intermediate analog
3qya – LtLuc (mutant) – Lampyris turkestanicus
4m46 – LtLuc
3fgc – VhLuc α+β chain+FMN – Vibrio harveyi
1luc, 1brl - VhLuc α+β chain
1bsl, 1xkj - VhLuc β chain
2psd, 2psh, 2psj, 2pse, 2psf – Luc (mutant) – Renilla reniformis

Additional information

(2d1s)

Several organisms are bioluminescent, meaning that they produce light. Luciferase is one of the enzymes that catalyzes light emitting reactions in organisms.

Luciola cruciata luciferase (Japanese firefly), complexed with Oxyluciferin & AMP (2d1r) or with an high-energy analogue (2d1s)
3ies,3iep and 3ier Firefly luciferase (FLuc) bound to its natural substrate ATP and the inhibitor PTC124^[3]
1ba3 firefly luciferase enzyme from Photinus pyralis
2psd, 2pse, 2psf, 2psh, 2psj, and 2rh7 the luciferase from Renilla reniformis (RLuc)
1bsl 1.95Å heterodimer of bacterial luciferase from Vibrio harveyi
1brl 2.4Å heterodimer of bacterial luciferase from Vibrio harveyi
1xkj homodimer of bacterial luciferase from Vibrio harveyi
2d1q, 2d1r and 2d1s thermostable Japanese Firefly (Luciola cruciata) Luciferase complexed with High-energy intermediate analog
2d1t thermostable Japanese Firefly Luciferase red-color emission S286N mutant
1lci firefly luciferase enzyme from Photinus pyralis
Dinoflagellate luciferase
1luc The 1.5Å resolution crystal structure of bacterial luciferase from Vibrio harveyi
3fgc Bacterial luciferase from Vibrio harveyi^[4]
1vpr luciferase of Lingulodinium polyedrum, a marine bioluminescent dinoflagellate
Green Fluorescent Protein
For additional information, see: Colored & Bioluminescent Proteins

ReferencesReferences

↑ Meighen EA. Molecular biology of bacterial bioluminescence. Microbiol Rev. 1991 Mar;55(1):123-42. PMID:2030669
↑ Gould SJ, Subramani S. Firefly luciferase as a tool in molecular and cell biology. Anal Biochem. 1988 Nov 15;175(1):5-13. PMID:3072883
↑ Auld DS, Lovell S, Thorne N, Lea WA, Maloney DJ, Shen M, Rai G, Battaile KP, Thomas CJ, Simeonov A, Hanzlik RP, Inglese J. Molecular basis for the high-affinity binding and stabilization of firefly luciferase by PTC124. Proc Natl Acad Sci U S A. 2010 Mar 16;107(11):4878-83. Epub 2010 Mar 1. PMID:20194791
↑ Campbell ZT, Weichsel A, Montfort WR, Baldwin TO. Crystal Structure of the Bacterial Luciferase:Flavin Complex Provides Insight into the Function of the subunit. Biochemistry. 2009 May 12. PMID:19435287 doi:http://dx.doi.org/10.1021/bi900003t

Additional LiteratureAdditional Literature

^{[xtra 1]}^{[xtra 2]}

↑ Marques SM, Esteves da Silva JC. Firefly bioluminescence: a mechanistic approach of luciferase catalyzed reactions. IUBMB Life. 2009 Jan;61(1):6-17. PMID:18949818 doi:10.1002/iub.134
↑ Inouye S. Firefly luciferase: an adenylate-forming enzyme for multicatalytic functions. Cell Mol Life Sci. 2010 Feb;67(3):387-404. Epub 2009 Oct 27. PMID:19859663 doi:10.1007/s00018-009-0170-8

External ResourcesExternal Resources

Yahoo news coverage of luciferase studies funded research for military applications
Luciferase at Wikipedia
Luciferase: June 2006 Molecule of the Month as part of the series of tutorials that are at the RCSB Protein Data Bank and written by David S. Goodsell

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Wayne Decatur, David Canner, Loïc Gazquez, Alexander Berchansky, Michal Harel, Charlene Planchenault

[1] Meighen EA. Molecular biology of bacterial bioluminescence. Microbiol Rev. 1991 Mar;55(1):123-42. PMID:2030669

[2] Gould SJ, Subramani S. Firefly luciferase as a tool in molecular and cell biology. Anal Biochem. 1988 Nov 15;175(1):5-13. PMID:3072883

[3] Auld DS, Lovell S, Thorne N, Lea WA, Maloney DJ, Shen M, Rai G, Battaile KP, Thomas CJ, Simeonov A, Hanzlik RP, Inglese J. Molecular basis for the high-affinity binding and stabilization of firefly luciferase by PTC124. Proc Natl Acad Sci U S A. 2010 Mar 16;107(11):4878-83. Epub 2010 Mar 1. PMID:20194791

[4] Campbell ZT, Weichsel A, Montfort WR, Baldwin TO. Crystal Structure of the Bacterial Luciferase:Flavin Complex Provides Insight into the Function of the subunit. Biochemistry. 2009 May 12. PMID:19435287 doi:http://dx.doi.org/10.1021/bi900003t

[5] Marques SM, Esteves da Silva JC. Firefly bioluminescence: a mechanistic approach of luciferase catalyzed reactions. IUBMB Life. 2009 Jan;61(1):6-17. PMID:18949818 doi:10.1002/iub.134

[6] Inouye S. Firefly luciferase: an adenylate-forming enzyme for multicatalytic functions. Cell Mol Life Sci. 2010 Feb;67(3):387-404. Epub 2009 Oct 27. PMID:19859663 doi:10.1007/s00018-009-0170-8

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