Biosynthesis of luciferin in Pyrophorus pellucens

McCapra, Frank; Razavi, Zia

doi:10.1039/c39760000153

Cited by 18 publications

(7 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This step is reported to occur without enzymes ( Okada et al, 1974 ; Gomi & Kajiyama, 2001 ; Day, Tisi & Bailey, 2004 ). Incorporation experiments demonstrate incorporations of 2-cyano-6-hydrobenzothiazole (CHBT), and D- and L- cysteine into D-luciferin in fireflies ( McCapra & Razavi, 1976 ; Okada, Iio & Goto, 1976 ; Day, Tisi & Bailey, 2004 ; Niwa, Nakamura & Ohmiya, 2006 ). Both D- and L- forms of luciferin are found in the firefly at a different ratio at different stages of development ( Lembert, 1996 ; Niwa, Nakamura & Ohmiya, 2006 ).…”

Section: Resultsmentioning

confidence: 99%

“…The bioluminescence systems used in these applications rely solely on commercially synthesized luciferin. Many attempts to resolve the luciferin biosynthetic pathway have been performed ( Okada et al, 1974 ; Okada, Iio & Goto, 1976 ; McCapra & Razavi, 1975 ; McCapra & Razavi, 1976 ; Colepicolo, Pagni & Bechara, 1988 ; Niwa, Nakamura & Ohmiya, 2006 ). Recently, Oba et al (2013) analyzed the luciferin biosynthetic pathway by injection of isotope-labeled compounds L-cysteine, hydroquinone, and benzoquinone into an adult lantern of firefly L. lateralis .…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Transcriptome analysis reveals candidate genes involved in luciferin metabolism inLuciola aquatilis(Coleoptera: Lampyridae)

Vongsangnak

Chumnanpuen

Sriboonlert

2016

PeerJ

View full text Add to dashboard Cite

Bioluminescence, which living organisms such as fireflies emit light, has been studied extensively for over half a century. This intriguing reaction, having its origins in nature where glowing insects can signal things such as attraction or defense, is now widely used in biotechnology with applications of bioluminescence and chemiluminescence. Luciferase, a key enzyme in this reaction, has been well characterized; however, the enzymes involved in the biosynthetic pathway of its substrate, luciferin, remains unsolved at present. To elucidate the luciferin metabolism, we performed a de novo transcriptome analysis using larvae of the firefly species, Luciola aquatilis. Here, a comparative analysis is performed with the model coleopteran insect Tribolium casteneum to elucidate the metabolic pathways in L. aquatilis. Based on a template luciferin biosynthetic pathway, combined with a range of protein and pathway databases, and various prediction tools for functional annotation, the candidate genes, enzymes, and biochemical reactions involved in luciferin metabolism are proposed for L. aquatilis. The candidate gene expression is validated in the adult L. aquatilis using reverse transcription PCR (RT-PCR). This study provides useful information on the bio-production of luciferin in the firefly and will benefit to future applications of the valuable firefly bioluminescence system.

show abstract

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Transcriptome analysis reveals candidate genes involved in luciferin metabolism inLuciola aquatilis(Coleoptera: Lampyridae)

Vongsangnak

Chumnanpuen

Sriboonlert

2016

PeerJ

View full text Add to dashboard Cite

show abstract

“…Biosynthetic pathways have been proposed, but based on insufficient information with inadequate experiments In the presence and absence of CoA (250 lM), the reaction was started by the addition of recombinant P. pyralis luciferase (1 pmol: Promega) and the light intensity of luminescence was measured at 22-23°C [63][64][65][66]. The only clear evidence is that cysteine is a synthetic unit of firefly luciferin [63,66]. In 2001, a luciferin-regeneration enzyme of firefly luciferin from oxyluciferin was reported [67,68].…”

Section: Biosynthesis Of Firefly Luciferin In Vivomentioning

confidence: 99%

Firefly luciferase: an adenylate-forming enzyme for multicatalytic functions

Inouye

2009

Cell. Mol. Life Sci.

View full text Add to dashboard Cite

Firefly luciferase is a member of the acyl-adenylate/thioester-forming superfamily of enzymes and catalyzes the oxidation of firefly luciferin with molecular oxygen to emit light. Knowledge of the luminescence mechanism catalyzed by firefly luciferase has been gathered, leading to the discovery of a novel catalytic function of luciferase. Recently, we demonstrated that firefly luciferase has a catalytic function of fatty acyl-CoA synthesis from fatty acids in the presence of ATP, Mg(2+) and coenzyme A. Based on identification of fatty acyl-CoA genes in firefly, Drosophila, and non-luminous click beetles, we then proposed that the evolutionary origin of firefly luciferase is a fatty acyl-CoA synthetase in insects. Further, we succeeded in converting the fatty acyl-CoA synthetase of non-luminous insects into functional luciferase showing luminescence activity by site-directed mutagenesis.

show abstract

“…Okada et al also identified that the addition of cysteine improved the yield of luciferin. As a result, in Phyrophorus pellucens it was found that radiolabelled cysteine was incorporated into newly synthesized luciferin (72). These results have been explained in the following two-step reaction: (a) transformation of oxyluciferin to 2-cyano-6-hydroxybenzothiazole; and (b) condensation of 2C6HB with D-cysteine to yield luciferin [ Fig.…”

Section: Structure and Biosynthesis Of Beetle Luciferinmentioning

confidence: 95%

Evolution of beetle bioluminescence: the origin of beetle luciferin

2004

View full text Add to dashboard Cite

Bioluminescence, the conversion of chemical energy into light in living organisms, is dependent on two principal components, an enzyme luciferase and the substrate luciferin. In beetles, the enzyme luciferase has been extensively studied, with significant enzymological, sequence and structural data now available. Furthermore, the enzyme has been employed in a remarkable number of important applications, from microbial detection and medical imaging to GM gene expression studies. However, there is little information regarding the biosynthesis of beetle luciferin, and here we review the literature and speculate as to its evolutionary origins. Luciferin consists of a benzothiazole moiety attached to a thiazole carboxylic acid moiety, the former being rarely observed in nature but the latter being observed in a broad range of biologically derived molecules. Benzothiazoles are, however, observed in melanogenesis and we speculate as to whether this may be relevant to the understanding of luciferin biosynthesis in beetles. This review examines recent novel insights into beetle luciferin recycling and we assess a range of possible biosynthetic mechanisms.

show abstract

Biosynthesis of luciferin in Pyrophorus pellucens

Abstract: The luminescent click beetle, P. pellucens, incorporates DL-cystine into the substrate in the light reaction, showing that luciferin is synthesised in adult beetles.

Cited by 18 publications

References 0 publications

Transcriptome analysis reveals candidate genes involved in luciferin metabolism inLuciola aquatilis(Coleoptera: Lampyridae)

Transcriptome analysis reveals candidate genes involved in luciferin metabolism inLuciola aquatilis(Coleoptera: Lampyridae)

Firefly luciferase: an adenylate-forming enzyme for multicatalytic functions

Evolution of beetle bioluminescence: the origin of beetle luciferin

Contact Info

Product

Resources

About