Luciferin and luciopterin isolated from the japanese firefly,

Kishi, Yoshito; Matsu-Ura, Shinya; Inoue, Shoji; Shimomura, Osamu; Goto, Terutaka

doi:10.1016/s0040-4039(00)75644-9

Cited by 28 publications

(19 citation statements)

References 6 publications

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“…From the Japanese firefly, Luciola cruciata, approximately 5.5 mg of luciferin was crystallized from 12,000 adult abdomens (233 g of acetone powder) [19]. The structure of firefly luciferin, D(-)-Luciferin, (S)-2-(6 0 -hydroxy-2 0 -benzothiazolyl)-2-thiazoline-4-carboxylic acid, was determined by chemical synthesis [20,21].…”

Section: Firefly Luciferin = D(-)-luciferin (D-lh 2 )mentioning

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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Section: Firefly Luciferin = D(-)-luciferin (D-lh 2 )mentioning

confidence: 99%

Firefly luciferase: an adenylate-forming enzyme for multicatalytic functions

Inouye

2009

Cell. Mol. Life Sci.

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“…These amounts of luciferin are approximately equal to the values previously reported: L. lateralis by HPLC with a fluorescence detector; 12) P. pyralis and L. cruciata by purification. 8,9) The amount of luciferin in an adult of L. parvula is approximately three times higher than that in L. lateralis, although they have roughly same body size. The amount of luciferin in larval L. cruciata determined by the L-L reaction was higher than that by HPLC (Student's t-test, P < 0:05).…”

Section: )mentioning

confidence: 99%

Determination of the Luciferin Contents in Luminous and Non-Luminous Beetles

Oba

Shintani

Nakamura

et al. 2008

Bioscience, Biotechnology, and Biochemistry

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“…Luminescence activity was determined by transferring 20 JJ. 1 of an ATP solution (10 pmol) to a well of a 96-well culture plate and injecting 200 (il of 25 mM glycylglycine buffer (pH 7.8) containing 10 ng of enzyme, 1.7xl0~5 M firefly luciferin and 15 mM MgS0 4 . Modification of PpC216V luciferase with TPCK and assay for luminescence activity were carried out as mentioned above.…”

Section: Site-specific Mutagenesis Of Cysteine Residues and Assay Of mentioning

confidence: 99%

“…In the presence of adenosine 5'-triphosphate (ATP) and Mg 2+ , the substrate, luciferin (LH 2 ), is activated to form luciferyl adenylate, which is then oxidized by molecular oxygen to yield light, oxyluciferin, C0 2 and adenosine 5'-monophosphate (AMP). LH 2 is a benzothiazole compound which serves as a common substrate in the firefly luminescence reaction [3,4]. E + LH 2 + Mg-ATP E-LH 2 -AMP + PP; E-LH 2 -AMP + 0 2 Light + Oxyluciferin + C0 2 + AMP Employing sulfhydryl-modifying reagents, earlier investigators have found that the luciferase from the North American firefly, Photinus pyralis (Pp), possesses 2 sulfhydryl groups, located at or near the luciferin binding site, that are essential for catalytic activity [5][6][7][8].…”

Section: Introductionmentioning

confidence: 99%

Mutagenesis of firefly luciferase shows that cysteine residues are not required for bioluminescence activity

Ohmiya

Tsuji

1997

FEBS Letters

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Conflicting reports exist in the literature as to whether sulfhydryl groups are essential for firefly luciferase activity. Inactivation of Photinus pyralis luciferase with ./V-tosyl-L-phenylalanine chloromethyl ketone (TPCK) and site-directed mutagenesis demonstrate that the cysteine residues are not absolutely required for activity. However, loss of P. pyralis luciferase activity is observed when any of the 4 cysteine residues is replaced with serine.© 1997 Federation of European Biochemical Societies.Key words: Photinus pyralis; Oxygenase; Active site; Protein modification; Amino acid sequence homology of the essentiality of sulfhydryl groups in firefly luciferase has been reexamined using a combination of iV-tosyl-L-phenylalanine chloromethyl ketone (TPCK) and site-specific mutagenesis to modify the cysteine residues in Pp luciferase [10] and in the luciferases of the Japanese fireflies, Hotaria parvula (Hp) [11] and Pyrocoelia miyako (Pm) [11]. The results show that, even though modification of the cysteine residues can cause significant changes in activity, sulfhydryl groups are not absolutely required for activity.

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Luciferin and luciopterin isolated from the japanese firefly,

Cited by 28 publications

References 6 publications

Firefly luciferase: an adenylate-forming enzyme for multicatalytic functions

Firefly luciferase: an adenylate-forming enzyme for multicatalytic functions

Determination of the Luciferin Contents in Luminous and Non-Luminous Beetles

Mutagenesis of firefly luciferase shows that cysteine residues are not required for bioluminescence activity

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