The origin of luciferase activity in Zophobas mealworm AMP/CoA-ligase (protoluciferase): luciferin stereoselectivity as a switch for the oxygenase activity

Viviani, Vadim R.; Scorsato, Valéria; Prado, Rogilene A.; Pereira, José Gomes; Niwa, Kazuki; Ohmiya, Yoshihiro; Barbosa, J.A.R.G.

doi:10.1039/c0pp00080a

Cited by 9 publications

(30 citation statements)

References 32 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…1B) (10,11). The bathochromic luminescence of AncCanth fits the hypothesis that beetle "protoluciferases," having a less developed substrate-binding site environment, emitted red light (24,25). The present study provides experimental evidence that the first luciferase "prototype" emitted bathochromic yellow-orange color.…”

Section: Evolution Of Luminescence Colorsupporting

confidence: 83%

Resurrecting the ancient glow of the fireflies

et al. 2020

View full text Add to dashboard Cite

The color of firefly bioluminescence is determined by the structure of luciferase. Firefly luciferase genes have been isolated from more than 30 species, producing light ranging in color from green to orange-yellow. Here, we reconstructed seven ancestral firefly luciferase genes, characterized the enzymatic properties of the recombinant proteins, and determined the crystal structures of the gene from ancestral Lampyridae. Results showed that the synthetic luciferase for the last common firefly ancestor exhibited green light caused by a spatial constraint on the luciferin molecule in enzyme, while fatty acyl-CoA synthetic activity, an original function of firefly luciferase, was diminished in exchange. All known firefly species are bioluminescent in the larvae, with a common ancestor arising approximately 100 million years ago. Combined, our findings propose that, within the mid-Cretaceous forest, the common ancestor of fireflies evolved green light luciferase via trade-off of the original function, which was likely aposematic warning display against nocturnal predation.

show abstract

Section: Evolution Of Luminescence Colorsupporting

confidence: 83%

Resurrecting the ancient glow of the fireflies

et al. 2020

View full text Add to dashboard Cite

show abstract

“…[ 49 ] Furthermore, the protein–ligand interaction diagram was generated using Lig‐plot [ 50 ] and molecular graphics were modelled using the PyMOL program. [ 51 ]…”

Section: Methodsmentioning

confidence: 99%

Selective inhibition of Zophobas morio (Coleoptera: Tenebrionidae) luciferase‐like enzyme luminescence by diclofenac and potential suitability for light‐off biosensing

et al. 2020

Self Cite

View full text Add to dashboard Cite

The accumulation of toxic carboxylic compounds may cause severe effects on the environment and living organisms. A luciferase‐like enzyme, previously cloned from the Malpighian tubules of the non‐luminescent Zophobas morio mealworm, displays thioesterification activity with a wide range of carboxylic substrates, and produces weak red luminescence in the presence of ATP and firefly d‐luciferin, a xenobiotic for this organism. To better investigate the function of this enzyme in carboxylic xenobiotic detoxification, we analyzed the inhibitory effect of different xenobiotic carboxylic acids on the luminescence activity of this enzyme, including environmental pollutants and pharmaceutical compounds. Noteworthy, the anti‐inflammatory drug diclofenac severely inhibited this luciferase‐like enzyme luminescence activity, both in in vitro (IC50 20 μM) and in vivo in bacterial cells assays, when compared with other beetle luciferases. Similar results were obtained with its brighter I327S mutant. Kinetic analysis of diclofenac's effect on luminescence activity indicated mixed‐type inhibition for both ATP and d‐luciferin. Modelling studies showed five potential binding sites for diclofenac, including the coenzyme A binding site, which showed one of the highest binding constant. Taken together, these results raise the possibility of using this luciferase‐like enzyme for the development of novel whole‐cell luminescent biosensors for diclofenac and similar drugs.

show abstract

“…The cDNAs for Phrixotrix hirtus red-emitting (PxRE), Pyrearinus termitilluminans green-emitting (Pte) luciferases and Zophobas morio (Zop) luciferase-like enzyme were previously subcloned into pCold-vector (Takara) [19][20][21]. The cDNA for Phrixotrix vivianii green-emitting luciferase (PxGR) was previously subcloned in pCAN vector [14].…”

Section: Plasmids and Beetle Luciferases Cdnasmentioning

confidence: 99%

Influence of the C-terminal domain on the bioluminescence activity and color determination in green and red emitting beetle luciferases and luciferase-like enzyme

Bevilaqua

Carvalho

Pelentir

et al. 2021

Photochem Photobiol Sci

Self Cite

View full text Add to dashboard Cite

Beetle luciferases catalyze the bioluminescent oxidation of D-luciferin, producing bioluminescence colors ranging from green to red, using two catalytic steps: adenylation of D-luciferin to produce D-luciferyl-adenylate and PPi, and oxidation of D-luciferyl-adenylate, yielding AMP, CO 2 , and excited oxyluciferin, the emitter. Luciferases and CoA-ligases display a similar fold, with a large N-terminal domain, and a small C-terminal domain which undergoes rotation, closing the active site and promoting both adenylation and oxidative reactions. The effect of C-terminal domain deletion was already investigated for Photinus pyralis firefly luciferase, resulting in a red-emitting mutant with severely impacted luminescence activity. However, the contribution of C-terminal in the bioluminescence activities and colors of other beetle luciferases and related ancestral luciferases were not investigated yet. Here we compared the effects of the C-terminal domain deletion on green-emitting luciferases of Pyrearinus termitilluminans (Pte) click beetle and Phrixothrix vivianii railroadworm, and on the red-emitting luciferase of Phrixothrix hirtus railroadworm and luciferase-like enzyme of Zophobas morio. In all cases, the domain deletion severely impacted the overall bioluminescence activities and, slightly less, the oxidative activities, and usually red-shifted the bioluminescence colors. The results support the involvement of the C-terminal in shielding the active site from the solvent during the light emitting step. However, in Pte luciferase, the deletion caused only a 10 nm red-shift, indicating a distinctive active site which remains more shielded, independently of the C′-terminal. Altogether, the results confirm the main contribution of the C-terminal for the catalysis of the adenylation reaction and for active site shielding during the light emitting step.

show abstract

The origin of luciferase activity in Zophobas mealworm AMP/CoA-ligase (protoluciferase): luciferin stereoselectivity as a switch for the oxygenase activity

Cited by 9 publications

References 32 publications

Resurrecting the ancient glow of the fireflies

Resurrecting the ancient glow of the fireflies

Selective inhibition of Zophobas morio (Coleoptera: Tenebrionidae) luciferase‐like enzyme luminescence by diclofenac and potential suitability for light‐off biosensing

Influence of the C-terminal domain on the bioluminescence activity and color determination in green and red emitting beetle luciferases and luciferase-like enzyme

Contact Info

Product

Resources

About