Cloning and characterization of the cDNA for the Brazilian Cratomorphus distinctus larval firefly luciferase: similarities with European Lampyris noctiluca and Asiatic Pyrocoelia luciferases

Viviani, Vadim R.; Arnoldi, Frederico G. C.; Brochetto-Braga, Márcia Regina; Ohmiya, Yoshihiro

doi:10.1016/j.cbpc.2004.05.012

Cited by 57 publications

(40 citation statements)

References 22 publications

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“…B,C). Although the K m for d ‐luciferin was relatively high when compared with other luciferases reported, green‐light‐emitting luciferase of P. viviani has been reported to show similar K m for d ‐luciferin, which is 150 μ m . The emission spectrum of the recombinant protein measured at pH 8.0 showed a peak at 559 nm, which is in the range of green‐yellow light as seen in the luminous spot of the living Fijian click beetle (Fig.…”

Section: Resultsmentioning

confidence: 80%

Cloning and Characterization of Luciferase from a Fijian Luminous Click Beetle

Mitani

Futahashi

Niwa

et al. 2013

Photochem & Photobiology

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Luminous click beetle is distributed almost exclusively in Central and South America with a single genus in Melanesia. Among these click beetles, the description of Melanesian species has been fragmentary, and its luciferase gene and phylogenetic relation to other click beetles still remain uncertain. We collected a living luminous click beetle, Photophorus jansonii in Fiji. It emits green-yellow light from two spots on the pronotum and has no ventral luminous organ. Here, we cloned a luciferase gene from this insect by RT-PCR. The deduced amino acid sequence showed high identity of ~85% to the luciferases derived from other click beetle species. The luciferase of the Fijian click beetle was produced as a recombinant protein to characterize its biochemical properties. The Km for D-luciferin and ATP were 173 and 270 μm, respectively. The luciferase was pH-insensitive and the spectrum measured at pH 8.0 showed a peak at 559 nm, which was in the range of green-yellow light as seen in the luminous spot of the living Fijian click beetle. The Fijian click beetle luciferase was assigned to the Elateridae clade by a phylogenetic analysis, but it made a clearly different branch from Pyrophorus group examined in this study.

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Section: Resultsmentioning

confidence: 80%

Cloning and Characterization of Luciferase from a Fijian Luminous Click Beetle

Mitani

Futahashi

Niwa

et al. 2013

Photochem & Photobiology

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“…The luciferase-related genes including those for long-chain acyl-CoA synthetase, 4-coumarate-CoA ligases, and EntF nonribosomal peptide synthetases, have been cloned from species ranging from bacteria to mammals. A phylogenetic tree inferred from luciferase-related proteins supports the idea that the genera of luminous beetles represent the four families (Viviani et al, 2004), although mtDNAs or other proteins have not been used to confirm these relationships.…”

Section: Introductionmentioning

confidence: 64%

Mitochondrial genomes of two luminous beetles, Rhagophthalmus lufengensis and R. ohbai (Arthropoda, Insecta, Coleoptera)

Ogoh

Ohba

et al. 2007

Gene

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“…The substrate specificity of P. pyralis and L. cruciata luciferase with a series of carboxylic acids including amino acid, aromatic acid and monohydroxyl fatty acids was determined [131]. Very weak activities of adenylation were Luciola cruciata M26194 [139] Luciola lateralis X66919 [140] Luciola lateralis Z49891 [121] Luciola mingrelica S61961 [115] Photuris pennsylvanica D25415 [141] Photuris pennsylvanica U31240 [125] Pyrocoelia miyako L39928 [142] Pyrocoelia rufa AF328553 [143] Hotaria parvula L39929 [142] Hotaria unmunsana AF420006 [144] Lampyris noctiluca X89479 [145] Lampyris turkestanicus AY742225 [146] Cratomorphus distinctus AY633557 [147] Lampyroidea maculata DQ137139 [148] Pyrophorus plagiophthalamus - [ 149] Pyrearinus termitilluminans AF116843 [150] Pyrophorus plagiophthalamus AF543368 [151] Pyrophorus mellifluus AF545854 [151] Phrixothrix viviani AF139644 [152] Phrixothrix hirtus AF139645…”

Section: Multiple Functions Of Luciferase As An Adenylate-forming Enzymementioning

confidence: 99%

Firefly luciferase: an adenylate-forming enzyme for multicatalytic functions

Inouye

2009

Cell. Mol. Life Sci.

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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.

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Cloning and characterization of the cDNA for the Brazilian Cratomorphus distinctus larval firefly luciferase: similarities with European Lampyris noctiluca and Asiatic Pyrocoelia luciferases

Cited by 57 publications

References 22 publications

Cloning and Characterization of Luciferase from a Fijian Luminous Click Beetle

Cloning and Characterization of Luciferase from a Fijian Luminous Click Beetle

Mitochondrial genomes of two luminous beetles, Rhagophthalmus lufengensis and R. ohbai (Arthropoda, Insecta, Coleoptera)

Firefly luciferase: an adenylate-forming enzyme for multicatalytic functions

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