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Volumn 19, Issue 1, 2004, Pages 8-20

Evolution of beetle bioluminescence: The origin of beetle luciferin

Author keywords

Bioluminescence; Coleoptera; Imaging; Luciferase; Luciferin

Indexed keywords

BIOCHEMISTRY; BIOSYNTHESIS; ENZYMES; GENE EXPRESSION; MEDICAL IMAGING; PHOSPHORESCENCE;

EID: 4844228022     PISSN: 15227235     EISSN: 10991271     Source Type: Journal    
DOI: 10.1002/bio.749     Document Type: Review
Times cited : (87)

References (101)
  • 1
    • 0002799431 scopus 로고
    • Functions and evolution of bioluminescence
    • Herring PJ (ed.). Academic Press: New York
    • Buck JB. Functions and evolution of bioluminescence. In Bioluminescence in Action, Herring PJ (ed.). Academic Press: New York, 1978.
    • (1978) Bioluminescence in Action
    • Buck, J.B.1
  • 2
    • 84973952530 scopus 로고
    • Communication in insects. 1. Flash communication in fireflies
    • Carlson AD, Copeland J. Communication in insects. 1. Flash communication in fireflies. Q. Rev. Biol. 1985; 60: 415-436.
    • (1985) Q. Rev. Biol. , vol.60 , pp. 415-436
    • Carlson, A.D.1    Copeland, J.2
  • 3
    • 0000711451 scopus 로고    scopus 로고
    • Firefly mating ecology, selection and evolution
    • Choe JC, Crespi BJ (eds). Cambridge University Press: Cambridge
    • Lloyd JE. Firefly mating ecology, selection and evolution. In The Evolution of Mating Systems in Insects and Arachnids, Choe JC, Crespi BJ (eds). Cambridge University Press: Cambridge, 1997; 184-192.
    • (1997) The Evolution of Mating Systems in Insects and Arachnids , pp. 184-192
    • Lloyd, J.E.1
  • 4
    • 0003320563 scopus 로고
    • The nature and possible functions of luminescence in Coleoptera larvae
    • Sivinski J. The nature and possible functions of luminescence in Coleoptera larvae. Coleopt. Bull. 1981; 35: 167-179.
    • (1981) Coleopt. Bull. , vol.35 , pp. 167-179
    • Sivinski, J.1
  • 5
    • 0036363666 scopus 로고    scopus 로고
    • Imaging of light emission from the expression of luciferases in living cells and organisms: A review
    • Greer LF III, Szalay AA. Imaging of light emission from the expression of luciferases in living cells and organisms: a review. Luminescence 2002; 17: 43-74.
    • (2002) Luminescence , vol.17 , pp. 43-74
    • Greer III, L.F.1    Szalay, A.A.2
  • 6
    • 0032117685 scopus 로고    scopus 로고
    • Prospects for chemiluminescent and bioluminescent immunossay and nucleic acid assay in food testing and the pharmaceutical industry
    • Kricka LJ. Prospects for chemiluminescent and bioluminescent immunossay and nucleic acid assay in food testing and the pharmaceutical industry. J. Biolumin. Chemilumin. 1998; 13: 185-188.
    • (1998) J. Biolumin. Chemilumin. , vol.13 , pp. 185-188
    • Kricka, L.J.1
  • 7
    • 0141976400 scopus 로고    scopus 로고
    • Bioluminescent molecular imaging of endogenous and exogenous p53-mediated transcription in vitro and in vivo using an HCT116 human colon carcinoma xenograft model
    • Wang W, El-Deiry WS. Bioluminescent molecular imaging of endogenous and exogenous p53-mediated transcription in vitro and in vivo using an HCT116 human colon carcinoma xenograft model. Cancer Biol. Ther. 2003; 2: 196-202.
    • (2003) Cancer Biol. Ther. , vol.2 , pp. 196-202
    • Wang, W.1    El-Deiry, W.S.2
  • 9
    • 0035055410 scopus 로고    scopus 로고
    • Visualizing pneumococcal infections in the lungs of live mice using bioluminescent Streptococcus pneumoniae transformed with a novel Gram-positive lux transposon
    • Francis KP, Yu J, Bellinger-Kawahara C et al. Visualizing pneumococcal infections in the lungs of live mice using bioluminescent Streptococcus pneumoniae transformed with a novel Gram-positive lux transposon. Infect. Immun. 2001; 69: 3350-3358.
    • (2001) Infect. Immun. , vol.69 , pp. 3350-3358
    • Francis, K.P.1    Yu, J.2    Bellinger-Kawahara, C.3
  • 10
    • 0021077237 scopus 로고
    • Biological diversity, chemical mechanisms, and the evolutionary origins of bioluminescent systems
    • Hastings JW. Biological diversity, chemical mechanisms, and the evolutionary origins of bioluminescent systems. J. Mol. Evol. 1983; 19: 309-321.
    • (1983) J. Mol. Evol. , vol.19 , pp. 309-321
    • Hastings, J.W.1
  • 11
    • 0031736101 scopus 로고    scopus 로고
    • Phototropism, bioluminenescence and the Diptera
    • Sivinski JM. Phototropism, bioluminenescence and the Diptera. Fla. Entomol. 1998; 81: 577-593.
    • (1998) Fla. Entomol. , vol.81 , pp. 577-593
    • Sivinski, J.M.1
  • 12
    • 0033278411 scopus 로고    scopus 로고
    • Aposematism and bioluminescence: Experimental evidence from glow-worm larvae (Coleoptera: Lampyridae)
    • De Cock R, Matthysen E. Aposematism and bioluminescence: experimental evidence from glow-worm larvae (Coleoptera: Lampyridae). Evol. Ecol. 1999; 13: 619-639.
    • (1999) Evol. Ecol. , vol.13 , pp. 619-639
    • De Cock, R.1    Matthysen, E.2
  • 13
    • 0037287101 scopus 로고    scopus 로고
    • Glow-worm larvae bioluminescence (Coleoptera: Lampyridae) operates as an aposematic signal upon toads (Bufo bufo)
    • De Cock R, Matthysen E. Glow-worm larvae bioluminescence (Coleoptera: Lampyridae) operates as an aposematic signal upon toads (Bufo bufo). Behav. Ecol. 2003; 14: 103-108.
    • (2003) Behav. Ecol. , vol.14 , pp. 103-108
    • De Cock, R.1    Matthysen, E.2
  • 14
    • 0030800964 scopus 로고    scopus 로고
    • Bioluminescence in firefly larvae: A test of the aposematic display hypothesis (Coleoptera: Lampyridae)
    • Underwood TJ, Tallamy DW, Pesek JD. Bioluminescence in firefly larvae: a test of the aposematic display hypothesis (Coleoptera: Lampyridae). J. Insect Behav. 1997; 10: 365-370.
    • (1997) J. Insect Behav. , vol.10 , pp. 365-370
    • Underwood, T.J.1    Tallamy, D.W.2    Pesek, J.D.3
  • 15
    • 0008887606 scopus 로고
    • Function of bioluminescence in mesopelagic organisms
    • Clarke WD. Function of bioluminescence in mesopelagic organisms. Nature 1963; 198: 1244-1246.
    • (1963) Nature , vol.198 , pp. 1244-1246
    • Clarke, W.D.1
  • 16
  • 17
    • 0000503240 scopus 로고
    • Oceanic bioluminescence: An overview of general functions
    • Young RE. Oceanic bioluminescence: an overview of general functions. Bull. Mar. Sci. 1983; 33: 829-845.
    • (1983) Bull. Mar. Sci. , vol.33 , pp. 829-845
    • Young, R.E.1
  • 18
    • 0033404342 scopus 로고    scopus 로고
    • Spectral sensitivity of vision and bioluminescence in the midwater shrimp Sergestes similis
    • Lindsay SM, Frank TM, Kent J, Partridge JC, Latz MI. Spectral sensitivity of vision and bioluminescence in the midwater shrimp Sergestes similis. Biol. Bull. 1999; 197: 348-360.
    • (1999) Biol. Bull. , vol.197 , pp. 348-360
    • Lindsay, S.M.1    Frank, T.M.2    Kent, J.3    Partridge, J.C.4    Latz, M.I.5
  • 19
    • 0016838374 scopus 로고
    • The origin of bioluminescence
    • Seliger HH. The origin of bioluminescence. Photochem. Photobiol. 1975; 21: 355-361.
    • (1975) Photochem. Photobiol. , vol.21 , pp. 355-361
    • Seliger, H.H.1
  • 21
    • 0032521119 scopus 로고    scopus 로고
    • Bioluminescence as a possible auxiliary oxygen detoxifying mechanism in elaterid larvae
    • Barros MP, Bechara EJ. Bioluminescence as a possible auxiliary oxygen detoxifying mechanism in elaterid larvae. Free Radic. Biol. Med. 1998; 24: 767-777.
    • (1998) Free Radic. Biol. Med. , vol.24 , pp. 767-777
    • Barros, M.P.1    Bechara, E.J.2
  • 22
    • 0034191815 scopus 로고    scopus 로고
    • Luciferase and urate may act as anti-oxidant defenses in larval Pyrearinus termitilluminans (Elateridae: Coleoptera) during natural development and upon 20-hydroxyecdysone treatment
    • Barros MP, Bechara EJ. Luciferase and urate may act as anti-oxidant defenses in larval Pyrearinus termitilluminans (Elateridae: Coleoptera) during natural development and upon 20-hydroxyecdysone treatment. Photochem. Photobiol. 2000; 71: 648-654.
    • (2000) Photochem. Photobiol. , vol.71 , pp. 648-654
    • Barros, M.P.1    Bechara, E.J.2
  • 23
    • 0035100489 scopus 로고    scopus 로고
    • Daily variations of antioxidant enzyme and luciferase activities in the luminescent click-beetle Pyrearinus termitilluminans: Cooperation against oxygen toxicity
    • Barros MP, Bechara EJ. Daily variations of antioxidant enzyme and luciferase activities in the luminescent click-beetle Pyrearinus termitilluminans: cooperation against oxygen toxicity. Insect Biochem. Mol. Biol. 2001; 31: 393-400.
    • (2001) Insect Biochem. Mol. Biol. , vol.31 , pp. 393-400
    • Barros, M.P.1    Bechara, E.J.2
  • 25
    • 10644240820 scopus 로고
    • The chemical mechanism and evolutionary development of beetle bioluminescence
    • Wood KV. The chemical mechanism and evolutionary development of beetle bioluminescence. Photochem. Photobiol. 1995; 62: 662-673.
    • (1995) Photochem. Photobiol. , vol.62 , pp. 662-673
    • Wood, K.V.1
  • 27
    • 33845185678 scopus 로고
    • Structure of dinoflagellate luciferin and its enzymic and nonenzymic air-oxidation products
    • Nakamura H, Kishi Y, Shimomura O, Morse D, Hastings JW. Structure of dinoflagellate luciferin and its enzymic and nonenzymic air-oxidation products. J. Am. Chem. Soc. 1989; 111: 7607-7611.
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 7607-7611
    • Nakamura, H.1    Kishi, Y.2    Shimomura, O.3    Morse, D.4    Hastings, J.W.5
  • 28
    • 0024659554 scopus 로고
    • Lux C, D and E genes of the Vibrio fischeri luminescence operon code for the reductase, transferase, and synthetase enzymes involved in aldehyde biosynthesis
    • Boylan M, Miyamoto C, Wall L, Graham A, Meighen E. Lux C, D and E genes of the Vibrio fischeri luminescence operon code for the reductase, transferase, and synthetase enzymes involved in aldehyde biosynthesis. Photochem. Photobiol. 1989; 49: 681-688.
    • (1989) Photochem. Photobiol. , vol.49 , pp. 681-688
    • Boylan, M.1    Miyamoto, C.2    Wall, L.3    Graham, A.4    Meighen, E.5
  • 29
    • 0035949480 scopus 로고    scopus 로고
    • Can coelenterates make coelenterazine? Dietary requirement for luciferin in cnidarian bioluminescence
    • Haddock SH, Rivers TJ, Robison BH. Can coelenterates make coelenterazine? Dietary requirement for luciferin in cnidarian bioluminescence. Proc. Natl Acad. Sci. USA 2001; 98: 11148-11151.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 11148-11151
    • Haddock, S.H.1    Rivers, T.J.2    Robison, B.H.3
  • 30
    • 0000372063 scopus 로고
    • Spectral emission and quantum yield of firefly bioluminescence
    • McElroy WD, Seliger HH. Spectral emission and quantum yield of firefly bioluminescence. Arch. Biochem. Biophys. 1960; 88: 136.
    • (1960) Arch. Biochem. Biophys. , vol.88 , pp. 136
    • McElroy, W.D.1    Seliger, H.H.2
  • 31
    • 0029939559 scopus 로고    scopus 로고
    • Chemistries and colors of bioluminescent reactions: A review
    • Hastings JW. Chemistries and colors of bioluminescent reactions: a review. Gene 1996; 173: 5-11.
    • (1996) Gene , vol.173 , pp. 5-11
    • Hastings, J.W.1
  • 33
    • 0002468820 scopus 로고
    • The colors of firefly bioluminescence: Enzyme configuration and species specificity
    • Seliger HH, McElroy WD. The colors of firefly bioluminescence: enzyme configuration and species specificity. Proc. Natl Acad. Sci. USA 1964; 52: 75-81.
    • (1964) Proc. Natl Acad. Sci. USA , vol.52 , pp. 75-81
    • Seliger, H.H.1    McElroy, W.D.2
  • 35
    • 0023548002 scopus 로고
    • Identification of a peroxisomal targeting signal at the carboxy-terminus of firefly luciferase
    • Gould SJ, Keller GA, Subramani S. Identification of a peroxisomal targeting signal at the carboxy-terminus of firefly luciferase. J. Cell Biol. 1987; 105: 2923-2931.
    • (1987) J. Cell Biol. , vol.105 , pp. 2923-2931
    • Gould, S.J.1    Keller, G.A.2    Subramani, S.3
  • 36
    • 0024230406 scopus 로고
    • Firefly luciferase as a tool in molecular and cell biology
    • Gould SJ, Subramani S. Firefly luciferase as a tool in molecular and cell biology. Anal. Biochem. 1988; 175: 5-13.
    • (1988) Anal. Biochem. , vol.175 , pp. 5-13
    • Gould, S.J.1    Subramani, S.2
  • 38
    • 0030584662 scopus 로고    scopus 로고
    • Crystal structure of firefly luciferase throws light on a superfamily of adenylate-forming enzymes
    • Conti E, Franks NP, Brick P. Crystal structure of firefly luciferase throws light on a superfamily of adenylate-forming enzymes. Structure 1996; 4: 287-298.
    • (1996) Structure , vol.4 , pp. 287-298
    • Conti, E.1    Franks, N.P.2    Brick, P.3
  • 39
    • 0032480765 scopus 로고    scopus 로고
    • Site-directed mutagenesis of histidine 245 in firefly luciferase: A proposed model of the active site
    • Branchini BR, Magyar RA, Murtiashaw MH, Anderson SM, Zimmer M. Site-directed mutagenesis of histidine 245 in firefly luciferase: a proposed model of the active site. Biochemistry 1998; 37: 15311-15319.
    • (1998) Biochemistry , vol.37 , pp. 15311-15319
    • Branchini, B.R.1    Magyar, R.A.2    Murtiashaw, M.H.3    Anderson, S.M.4    Zimmer, M.5
  • 40
    • 0033173841 scopus 로고    scopus 로고
    • Model of the active site of firefly luciferase
    • Sandalova TP, Ugarova NN. Model of the active site of firefly luciferase. Biochemistry (Mosc.) 1999; 64: 962-967.
    • (1999) Biochemistry (Mosc.) , vol.64 , pp. 962-967
    • Sandalova, T.P.1    Ugarova, N.N.2
  • 41
    • 0037126024 scopus 로고    scopus 로고
    • Crystal structure of DhbE, an archetype for aryl acid activating domains of modular nonribosomal peptide synthetases
    • May JJ, Kessler N, Marahiel MA, Stubbs MT. Crystal structure of DhbE, an archetype for aryl acid activating domains of modular nonribosomal peptide synthetases. Proc. Natl Acad. Sci. USA 2002; 99: 12120-12125.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 12120-12125
    • May, J.J.1    Kessler, N.2    Marahiel, M.A.3    Stubbs, M.T.4
  • 42
    • 0037452897 scopus 로고    scopus 로고
    • The 1.75 Å crystal structure of acetyl-CoA synthetase bound to adenosine-5′-propylphosphate and coenzyme A
    • Gulick AM, Starai VJ, Horswill AR, Homick KM, Escalante-Semerena JC. The 1.75 Å crystal structure of acetyl-CoA synthetase bound to adenosine-5′-propylphosphate and coenzyme A. Biochemistry 2003; 42: 2866-2873.
    • (2003) Biochemistry , vol.42 , pp. 2866-2873
    • Gulick, A.M.1    Starai, V.J.2    Horswill, A.R.3    Homick, K.M.4    Escalante-Semerena, J.C.5
  • 43
    • 0008380298 scopus 로고
    • Cloning of firefly luciferase cDNA and the expression of active luciferase in Escherichia coli
    • de Wet JR, Wood KV, Helinski DR, DeLuca M. Cloning of firefly luciferase cDNA and the expression of active luciferase in Escherichia coli. Proc. Natl Acad. Sci. USA 1985; 82: 7870-7873.
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 7870-7873
    • De Wet, J.R.1    Wood, K.V.2    Helinski, D.R.3    DeLuca, M.4
  • 44
    • 0036288916 scopus 로고    scopus 로고
    • Molecular cloning and expression of a cDNA encoding the luciferase from the firefly, Hotaria unmunsana
    • Choi YS, Lee KS, Bae JS et al. Molecular cloning and expression of a cDNA encoding the luciferase from the firefly, Hotaria unmunsana. Comp. Biochem. Physiol. Biochem. Mol. Biol. 2002; 132: 661-670.
    • (2002) Comp. Biochem. Physiol. Biochem. Mol. Biol. , vol.132 , pp. 661-670
    • Choi, Y.S.1    Lee, K.S.2    Bae, J.S.3
  • 45
    • 0027325309 scopus 로고
    • Luciferase from the east European firefly Luciola mingrelica: Cloning and nucleotide sequence of the cDNA, overexpression in Escherichia coli and purification of the enzyme
    • Devine JH, Kutuzova GD, Green VA, Ugarova NN, Baldwin TO. Luciferase from the east European firefly Luciola mingrelica: cloning and nucleotide sequence of the cDNA, overexpression in Escherichia coli and purification of the enzyme. Biochim. Biophys. Acta 1993; 1173: 121-132.
    • (1993) Biochim. Biophys. Acta , vol.1173 , pp. 121-132
    • Devine, J.H.1    Kutuzova, G.D.2    Green, V.A.3    Ugarova, N.N.4    Baldwin, T.O.5
  • 46
    • 0024560864 scopus 로고
    • Cloning and sequence analysis of cDNA for luciferase of a Japanese firefly, Luciola cruciata
    • Masuda T, Tatsumi H, Nakano E. Cloning and sequence analysis of cDNA for luciferase of a Japanese firefly, Luciola cruciata. Gene 1989; 77: 265-270.
    • (1989) Gene , vol.77 , pp. 265-270
    • Masuda, T.1    Tatsumi, H.2    Nakano, E.3
  • 47
    • 0029347142 scopus 로고
    • Cloning, expression and sequence analysis of cDNA for the luciferases from the Japanese fireflies, Pyrocoelia miyako and Hotaria parvula
    • Ohmiya Y, Ohba N, Toh H, Tsuji F. Cloning, expression and sequence analysis of cDNA for the luciferases from the Japanese fireflies, Pyrocoelia miyako and Hotaria parvula. Photochem. Photobiol. 1995; 62: 309-313.
    • (1995) Photochem. Photobiol. , vol.62 , pp. 309-313
    • Ohmiya, Y.1    Ohba, N.2    Toh, H.3    Tsuji, F.4
  • 48
    • 0030034869 scopus 로고    scopus 로고
    • Sequence and biochemical similarities between the luciferases of the glow-worm Lampyris noctiluca and the firefly Photinus pyralis
    • Sala-Newby GB, Thomson CM, Campbell AK. Sequence and biochemical similarities between the luciferases of the glow-worm Lampyris noctiluca and the firefly Photinus pyralis. Biochem. J. 1996; 313: 761-767.
    • (1996) Biochem. J. , vol.313 , pp. 761-767
    • Sala-Newby, G.B.1    Thomson, C.M.2    Campbell, A.K.3
  • 49
    • 0024653997 scopus 로고
    • Luciferase cDNA from Japanese firefly, Luciola cruciata: Cloning, structure and expression in Escherichia coli
    • Tatsumi H, Masuda T, Kajiyama N, Nakano E. Luciferase cDNA from Japanese firefly, Luciola cruciata: cloning, structure and expression in Escherichia coli. J. Biolumin. Chemilumin. 1989; 3: 75-78.
    • (1989) J. Biolumin. Chemilumin. , vol.3 , pp. 75-78
    • Tatsumi, H.1    Masuda, T.2    Kajiyama, N.3    Nakano, E.4
  • 50
    • 0026717564 scopus 로고
    • Molecular cloning and expression in Escherichia coli of a cDNA clone encoding luciferase of a firefly, Luciola lateralis
    • Tatsumi H, Kajiyama N, Nakano E. Molecular cloning and expression in Escherichia coli of a cDNA clone encoding luciferase of a firefly, Luciola lateralis. Biochim. Biophys. Acta 1992; 1131: 161-165.
    • (1992) Biochim. Biophys. Acta , vol.1131 , pp. 161-165
    • Tatsumi, H.1    Kajiyama, N.2    Nakano, E.3
  • 51
    • 0033614782 scopus 로고    scopus 로고
    • Cloning, sequence analysis, and expression of active Phrixothrix railroad-worm luciferases: Relationship between bioluminescence spectra and primary structures
    • Viviani VR, Bechara EJ, Ohmiya Y. Cloning, sequence analysis, and expression of active Phrixothrix railroad-worm luciferases: relationship between bioluminescence spectra and primary structures. Biochemistry 1999; 38: 8271-8279.
    • (1999) Biochemistry , vol.38 , pp. 8271-8279
    • Viviani, V.R.1    Bechara, E.J.2    Ohmiya, Y.3
  • 52
    • 0033174499 scopus 로고    scopus 로고
    • Cloning and molecular characterization of the cDNA for the Brazilian larval click-beetle Pyrearinus termitilluminans luciferase
    • Viviani VR, Silva AC, Perez GL et al. Cloning and molecular characterization of the cDNA for the Brazilian larval click-beetle Pyrearinus termitilluminans luciferase. Photochem. Photobiol. 1999; 70: 254-260.
    • (1999) Photochem. Photobiol. , vol.70 , pp. 254-260
    • Viviani, V.R.1    Silva, A.C.2    Perez, G.L.3
  • 53
    • 0024967767 scopus 로고
    • Complementary DNA coding click beetle luciferases can elicit bioluminescence of different colors
    • Wood KV, Lam YA, Seliger HH, McElroy WD. Complementary DNA coding click beetle luciferases can elicit bioluminescence of different colors. Science 1989; 244: 700-702.
    • (1989) Science , vol.244 , pp. 700-702
    • Wood, K.V.1    Lam, Y.A.2    Seliger, H.H.3    McElroy, W.D.4
  • 54
    • 0030895027 scopus 로고    scopus 로고
    • Cloning and sequencing of a cDNA for firefly luciferase from Photuris pennsylvanica
    • Ye L, Buck LM, Schaeffer HJ, Leach FR. Cloning and sequencing of a cDNA for firefly luciferase from Photuris pennsylvanica. Biochim. Biophys. Acta 1997; 1339: 39-52.
    • (1997) Biochim. Biophys. Acta , vol.1339 , pp. 39-52
    • Ye, L.1    Buck, L.M.2    Schaeffer, H.J.3    Leach, F.R.4
  • 55
    • 0002552327 scopus 로고
    • The chemi-and bioluminescence of firefly luciferin: An efficient chemical production of electronlically excited states
    • White EH, Rapaport E, Seliger HH, Hopkins TA. The chemi-and bioluminescence of firefly luciferin: an efficient chemical production of electronlically excited states. Bioorg. Chem. 1971; 1: 92-122.
    • (1971) Bioorg. Chem. , vol.1 , pp. 92-122
    • White, E.H.1    Rapaport, E.2    Seliger, H.H.3    Hopkins, T.A.4
  • 56
    • 0031577478 scopus 로고    scopus 로고
    • Synthesis of dehydroluciferin by firefly luciferase: Effect of dehydroluciferin, coenzyme A and nucleoside triphosphates on the luminescent reaction
    • Fontes R, Dukhovich A, Sillero A, Sillero MAG. Synthesis of dehydroluciferin by firefly luciferase: effect of dehydroluciferin, coenzyme A and nucleoside triphosphates on the luminescent reaction. Biochem. Biophys. Res. Commun. 1997; 237: 445-450.
    • (1997) Biochem. Biophys. Res. Commun. , vol.237 , pp. 445-450
    • Fontes, R.1    Dukhovich, A.2    Sillero, A.3    Sillero, M.A.G.4
  • 57
    • 0037431017 scopus 로고    scopus 로고
    • Firefly luciferase is a bifunctional enzyme: ATP-dependent monooxygenase and a long chain fatty acyl-CoA synthetase
    • Oba Y, Ojika M, Inouye S. Firefly luciferase is a bifunctional enzyme: ATP-dependent monooxygenase and a long chain fatty acyl-CoA synthetase. FEBS Lett. 2003; 540: 251-254.
    • (2003) FEBS Lett. , vol.540 , pp. 251-254
    • Oba, Y.1    Ojika, M.2    Inouye, S.3
  • 58
    • 0035115792 scopus 로고    scopus 로고
    • Arachidonic and eicosapentaenoic acids in tissues of the firefly, Photinus pyralis (Insecta: Coleoptera)
    • Nor Aliza AR, Bedick JC, Rana RL et al. Arachidonic and eicosapentaenoic acids in tissues of the firefly, Photinus pyralis (Insecta: Coleoptera). Comp. Biochem. Physiol. A Mol. Integr. Physiol. 2001; 128: 251-257.
    • (2001) Comp. Biochem. Physiol. A Mol. Integr. Physiol. , vol.128 , pp. 251-257
    • Nor Aliza, A.R.1    Bedick, J.C.2    Rana, R.L.3
  • 59
    • 0001238772 scopus 로고    scopus 로고
    • Larval Tenebrio molitor (Coleoptera: Tenebrionidae) fat body extracts catalyze firefly D-luciferin- and ATP-dependent chemiluminescence: A luciferase-like enzyme
    • Viviani VR, Bechara EJV. Larval Tenebrio molitor (Coleoptera: Tenebrionidae) fat body extracts catalyze firefly D-luciferin- and ATP-dependent chemiluminescence: a luciferase-like enzyme. Photochem. Photobiol. 1996; 63: 713-718.
    • (1996) Photochem. Photobiol. , vol.63 , pp. 713-718
    • Viviani, V.R.1    Bechara, E.J.V.2
  • 60
    • 0004121193 scopus 로고
    • Cormier MJ, Hercules DM, Lee J (eds). Plenum: New York
    • Seliger HH. In Chemiluminescence and Bioluminescence, Cormier MJ, Hercules DM, Lee J (eds). Plenum: New York, 1973; 461-478.
    • (1973) Chemiluminescence and Bioluminescence , pp. 461-478
    • Seliger, H.H.1
  • 62
    • 0015211209 scopus 로고
    • The molecular structure of firefly D-(-)-luciferin: A single crystal X-ray analysis
    • Blank GE, Pletcher J, Sax M. The molecular structure of firefly D-(-)-luciferin: a single crystal X-ray analysis. Biochem. Biophys. Res. Commun. 1971; 42: 583-588.
    • (1971) Biochem. Biophys. Res. Commun. , vol.42 , pp. 583-588
    • Blank, G.E.1    Pletcher, J.2    Sax, M.3
  • 63
    • 0342714502 scopus 로고
    • Brazilian species of luminescent Elateridae: Luciferin identification and bioluminescence spectra
    • Colepicolo-Neto P, Costa C, Bechara EJH. Brazilian species of luminescent Elateridae: luciferin identification and bioluminescence spectra. Insect Biochem. 1986; 16: 803-810.
    • (1986) Insect Biochem. , vol.16 , pp. 803-810
    • Colepicolo-Neto, P.1    Costa, C.2    Bechara, E.J.H.3
  • 64
    • 0030293927 scopus 로고    scopus 로고
    • Separation, identification and determination of luciferin in the Iranian firefly, Lampyris turkestanicus, by HPLC and spectroscopic methods
    • Hadj-Mohammadi MR, Chaichi MJ. Separation, identification and determination of luciferin in the Iranian firefly, Lampyris turkestanicus, by HPLC and spectroscopic methods. Photochem. Photobiol. 1996; 64: 821-822.
    • (1996) Photochem. Photobiol. , vol.64 , pp. 821-822
    • Hadj-Mohammadi, M.R.1    Chaichi, M.J.2
  • 66
    • 0030987671 scopus 로고    scopus 로고
    • Firefly 'femmes fatales' acquire defensive steroids (lucibufagins) from their firefly prey
    • Eisner T, Goetz MA, Hill DE, Smedley SR, Meinwald J. Firefly 'femmes fatales' acquire defensive steroids (lucibufagins) from their firefly prey. Proc. Natl Acad. Sci. USA 1997; 94: 9723-9728.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 9723-9728
    • Eisner, T.1    Goetz, M.A.2    Hill, D.E.3    Smedley, S.R.4    Meinwald, J.5
  • 67
    • 0036369283 scopus 로고    scopus 로고
    • Two bioluminescent diptera: The North American Orfelia fultoni and the Australian Arachnocampa flava. Similar niche, different bioluminescence systems
    • Viviani VR, Hastings JW, Wilson T. Two bioluminescent diptera: the North American Orfelia fultoni and the Australian Arachnocampa flava. Similar niche, different bioluminescence systems. Photochem. Photobiol. 2002; 75: 22-27.
    • (2002) Photochem. Photobiol. , vol.75 , pp. 22-27
    • Viviani, V.R.1    Hastings, J.W.2    Wilson, T.3
  • 69
    • 37049133635 scopus 로고
    • A model for firefly luciferin biosynthesis
    • McCapra F, Razavi Z. A model for firefly luciferin biosynthesis. J.C.S. Chem. Commun. 1975; 2: 42-43.
    • (1975) J.C.S. Chem. Commun. , vol.2 , pp. 42-43
    • McCapra, F.1    Razavi, Z.2
  • 70
    • 49549155001 scopus 로고
    • Firefly bioluminescence III. Conversion of oxyluciferin to luciferin in firefly
    • Okada K, Iio H, Kubota L, Goto T. Firefly bioluminescence III. Conversion of oxyluciferin to luciferin in firefly. Tetrahedron Lett. 1974; 15: 2771-2774.
    • (1974) Tetrahedron Lett. , vol.15 , pp. 2771-2774
    • Okada, K.1    Iio, H.2    Kubota, L.3    Goto, T.4
  • 71
    • 0016839347 scopus 로고
    • The production of oxyluciferin during the firefly luciferase light reaction
    • Gates BJ, DeLuca M. The production of oxyluciferin during the firefly luciferase light reaction. Arch. Biochem. Biophys. 1975; 169: 616-621.
    • (1975) Arch. Biochem. Biophys. , vol.169 , pp. 616-621
    • Gates, B.J.1    DeLuca, M.2
  • 72
    • 37049107520 scopus 로고
    • Biosynthesis of luciferin in Pyrophorus pellucens
    • McCapra FM, Razavi Z. Biosynthesis of luciferin in Pyrophorus pellucens. J. Chem. Soc. Chem. Commun. 1976; 5: 153-154.
    • (1976) J. Chem. Soc. Chem. Commun. , vol.5 , pp. 153-154
    • McCapra, F.M.1    Razavi, Z.2
  • 73
    • 0035965211 scopus 로고    scopus 로고
    • Oxyluciferin, a luminescence product of firefly luciferase, is enzymatically regenerated into luciferin
    • Gomi K, Kajiyama N. Oxyluciferin, a luminescence product of firefly luciferase, is enzymatically regenerated into luciferin. J. Biol. Chem. 2001; 276: 36508-36513.
    • (2001) J. Biol. Chem. , vol.276 , pp. 36508-36513
    • Gomi, K.1    Kajiyama, N.2
  • 74
    • 77956995475 scopus 로고
    • Synthesis of firefly luciferin and structural analogs
    • Bowie LJ. Synthesis of firefly luciferin and structural analogs. Methods Enzymol. 1978; 57: 15-28.
    • (1978) Methods Enzymol. , vol.57 , pp. 15-28
    • Bowie, L.J.1
  • 75
    • 0033944664 scopus 로고    scopus 로고
    • Chemical synthesis of firefly luciferin analogs and inhibitors
    • Branchini BR. Chemical synthesis of firefly luciferin analogs and inhibitors. Methods Enzymol. 2000; 305: 188-195.
    • (2000) Methods Enzymol. , vol.305 , pp. 188-195
    • Branchini, B.R.1
  • 76
    • 0035694055 scopus 로고    scopus 로고
    • The evolution of bioluminescence in cantharoids (Coleoptera: Elateroidea)
    • Branham MA, Wenzel JW. The evolution of bioluminescence in cantharoids (Coleoptera: Elateroidea). Fla. Entomol. 2001; 84: 565-586.
    • (2001) Fla. Entomol. , vol.84 , pp. 565-586
    • Branham, M.A.1    Wenzel, J.W.2
  • 77
    • 0043166468 scopus 로고    scopus 로고
    • Structure and evolution of the luciferin-regenerating enzyme (LRE) gene from the firefly Photinus pyralis
    • Day JC, Bailey MJ. Structure and evolution of the luciferin-regenerating enzyme (LRE) gene from the firefly Photinus pyralis. Insect Mol. Biol. 2003; 12: 365-372.
    • (2003) Insect Mol. Biol. , vol.12 , pp. 365-372
    • Day, J.C.1    Bailey, M.J.2
  • 78
    • 0037055277 scopus 로고    scopus 로고
    • Molecular cloning and expression of the cDNAs encoding luciferin-regenerating enzyme from Luciola cruciata and Luciola lateralis
    • Gomi K, Hirokawa K, Kajiyama N. Molecular cloning and expression of the cDNAs encoding luciferin-regenerating enzyme from Luciola cruciata and Luciola lateralis. Gene 2002; 294: 157-166.
    • (2002) Gene , vol.294 , pp. 157-166
    • Gomi, K.1    Hirokawa, K.2    Kajiyama, N.3
  • 79
    • 0029948484 scopus 로고    scopus 로고
    • Firefly luciferase can use L-luciferin to produce light
    • Lembert N. Firefly luciferase can use L-luciferin to produce light. Biochem J. 1996; 317: 273-277.
    • (1996) Biochem J. , vol.317 , pp. 273-277
    • Lembert, N.1
  • 80
    • 0036280341 scopus 로고    scopus 로고
    • Genetics and assembly line enzymology of siderophore biosynthesis in bacteria
    • Crosa JH, Walsh CT. Genetics and assembly line enzymology of siderophore biosynthesis in bacteria. Microbiol. Mol. Biol. Rev. 2002; 66: 223-249.
    • (2002) Microbiol. Mol. Biol. Rev. , vol.66 , pp. 223-249
    • Crosa, J.H.1    Walsh, C.T.2
  • 81
    • 0024420904 scopus 로고
    • Subcloning, expression, and purification of the enterobactin biosynthetic enzyme 2,3-dihydroxybenzoate-AMP ligase: Demonstration of enzyme-bound (2,3-dihydroxybenzoyl)adenylate product
    • Rusnak F, Faraci WS, Walsh CT. Subcloning, expression, and purification of the enterobactin biosynthetic enzyme 2,3-dihydroxybenzoate-AMP ligase: demonstration of enzyme-bound (2,3-dihydroxybenzoyl)adenylate product. Biochemistry 1989; 28: 6827-6835.
    • (1989) Biochemistry , vol.28 , pp. 6827-6835
    • Rusnak, F.1    Faraci, W.S.2    Walsh, C.T.3
  • 82
    • 0025863049 scopus 로고
    • Biosynthesis of the Escherichia coli siderophore enterobactin: Sequence of the entF gene, expression and purification of EntF, and analysis of covalent phosphopantetheine
    • Rusnak F, Sakaitani M, Drueckhammer D, Reichert J, Walsh CT. Biosynthesis of the Escherichia coli siderophore enterobactin: sequence of the entF gene, expression and purification of EntF, and analysis of covalent phosphopantetheine. Biochemistry 1991; 30: 2916-2927.
    • (1991) Biochemistry , vol.30 , pp. 2916-2927
    • Rusnak, F.1    Sakaitani, M.2    Drueckhammer, D.3    Reichert, J.4    Walsh, C.T.5
  • 83
    • 0033539471 scopus 로고    scopus 로고
    • Assembly of the Pseudomonas aeruginosa non-ribosomal peptide siderophore pyochelin: In vitro reconstitution of aryl-4,2-bisthiazoline synthetase activity from PchD, PchE, and PchF
    • Quadri LE, Keating TA, Patel HM, Walsh CT. Assembly of the Pseudomonas aeruginosa non-ribosomal peptide siderophore pyochelin: in vitro reconstitution of aryl-4,2-bisthiazoline synthetase activity from PchD, PchE, and PchF. Biochemistry 1999; 38: 14941-14954.
    • (1999) Biochemistry , vol.38 , pp. 14941-14954
    • Quadri, L.E.1    Keating, T.A.2    Patel, H.M.3    Walsh, C.T.4
  • 85
    • 0030577007 scopus 로고    scopus 로고
    • A new benzothiazole derivative by degradation of pheomelanins with alkaline hydrogen peroxide
    • Napolitano A, Vincensi M, d'Ischia M, Prota G. A new benzothiazole derivative by degradation of pheomelanins with alkaline hydrogen peroxide. Tetrahedron Lett. 1996; 37: 6799-6802.
    • (1996) Tetrahedron Lett. , vol.37 , pp. 6799-6802
    • Napolitano, A.1    Vincensi, M.2    D'Ischia, M.3    Prota, G.4
  • 87
    • 0033747010 scopus 로고    scopus 로고
    • Local and systemic induction of two defense-related subtilisin-like protease promoters in transgenic Arabidopsis plants. Luciferin induction of PR gene expression
    • Jorda L, Vera P. Local and systemic induction of two defense-related subtilisin-like protease promoters in transgenic Arabidopsis plants. Luciferin induction of PR gene expression. Plant Physiol. 2000; 124: 1049-1058.
    • (2000) Plant Physiol. , vol.124 , pp. 1049-1058
    • Jorda, L.1    Vera, P.2
  • 88
    • 0035902526 scopus 로고    scopus 로고
    • Biosynthesis of the thiazole moiety of thiamine in Escherichia coli: Identification of an acyldisulphide linked protein-protein conjugate that is functionally analogous to the ubiquitin-E1 complex
    • Jun X, Kinsland C, McLafferty FW, Begley TP. Biosynthesis of the thiazole moiety of thiamine in Escherichia coli: identification of an acyldisulphide linked protein-protein conjugate that is functionally analogous to the ubiquitin-E1 complex. Proc. Natl Acad. Sci. USA 2001; 98: 8513-8518.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 8513-8518
    • Jun, X.1    Kinsland, C.2    McLafferty, F.W.3    Begley, T.P.4
  • 90
    • 85153263107 scopus 로고    scopus 로고
    • On the evolution and synthesis of beetle luciferin: Clues from the similarity of bacterial siderophores to beetle luciferin
    • Stanley PE, Kricka LJ (eds). World Scientific Publishing: Singapore
    • Tisi LC, Murray JAH. On the evolution and synthesis of beetle luciferin: clues from the similarity of bacterial siderophores to beetle luciferin. In Bioluminescence and Chemiluminescence: Progress and Current Applications, Stanley PE, Kricka LJ (eds). World Scientific Publishing: Singapore, 2002; 53-56.
    • (2002) Bioluminescence and Chemiluminescence: Progress and Current Applications , pp. 53-56
    • Tisi, L.C.1    Murray, J.A.H.2
  • 92
    • 0001142406 scopus 로고
    • Nutrition and cultivation of spiroplasmas
    • Whitcomb RF, Tully JG (eds). Academic Press: San Diego
    • Chang C-J. Nutrition and cultivation of spiroplasmas. In The Mycoplasmas, Whitcomb RF, Tully JG (eds). Academic Press: San Diego, 1989; 113-200.
    • (1989) The Mycoplasmas , pp. 113-200
    • Chang, C.-J.1
  • 93
    • 0023351464 scopus 로고
    • Characterization of some new insect-derived acholeplasmas
    • Tully JG, Rose DL, Whitcomb RF et al. Characterization of some new insect-derived acholeplasmas. Isr. J. Med. Sci. 1987; 23: 699-703.
    • (1987) Isr. J. Med. Sci. , vol.23 , pp. 699-703
    • Tully, J.G.1    Rose, D.L.2    Whitcomb, R.F.3
  • 94
    • 51249167811 scopus 로고
    • Lampyridae (Coleoptera): A plethora of mollicute associations
    • Hackett KJ, Whitcomb RF, Tully JG et al. Lampyridae (Coleoptera): a plethora of mollicute associations. Microb. Ecol. 1992; 23: 181-193.
    • (1992) Microb. Ecol. , vol.23 , pp. 181-193
    • Hackett, K.J.1    Whitcomb, R.F.2    Tully, J.G.3
  • 95
    • 0024312502 scopus 로고
    • Mycoplasma ellychniae sp. nov., a sterol-requiring mollicute from the firefly beetle Ellychnia corrusca
    • Tully JG, Rose DL, Hackett KJ et al. Mycoplasma ellychniae sp. nov., a sterol-requiring mollicute from the firefly beetle Ellychnia corrusca. Int. J. Syst. Bacteriol. 1989; 39: 284-289.
    • (1989) Int. J. Syst. Bacteriol. , vol.39 , pp. 284-289
    • Tully, J.G.1    Rose, D.L.2    Hackett, K.J.3
  • 96
    • 0025306259 scopus 로고
    • Mycoplasma somnilux sp. nov., Mycoplasma luminosum, sp. nov., and Mycoplasma lucivorax, sp. nov., new sterol-requiring mollicutes from firefly beetles (Coleoptera: Lampyridae)
    • Williamson DL, Tully JG, Rose DL et al. Mycoplasma somnilux sp. nov., Mycoplasma luminosum, sp. nov., and Mycoplasma lucivorax, sp. nov., new sterol-requiring mollicutes from firefly beetles (Coleoptera: Lampyridae). Int. J. Syst. Bacteriol. 1990; 40: 160-164.
    • (1990) Int. J. Syst. Bacteriol. , vol.40 , pp. 160-164
    • Williamson, D.L.1    Tully, J.G.2    Rose, D.L.3
  • 97
    • 2342460369 scopus 로고    scopus 로고
    • Stadium-specific transmission of endosymbionts needed for pederin biosynthesis in three species of Paederus rove beetles
    • Kellner RLL, Stadium-specific transmission of endosymbionts needed for pederin biosynthesis in three species of Paederus rove beetles. Entomol. Exp. Appl. 2003; 107: 115-124.
    • (2003) Entomol. Exp. Appl. , vol.107 , pp. 115-124
    • Kellner, R.L.L.1
  • 98
    • 0035107234 scopus 로고    scopus 로고
    • Suppression of pederin biosynthesis through antibiotic elimination of endosymbionts in Paederus sabaeus
    • Kellner RLL. Suppression of pederin biosynthesis through antibiotic elimination of endosymbionts in Paederus sabaeus. J. Insect Physiol. 2001; 47: 475-483.
    • (2001) J. Insect Physiol. , vol.47 , pp. 475-483
    • Kellner, R.L.L.1
  • 99
    • 0036009127 scopus 로고    scopus 로고
    • Molecular identification of an endosymbiotic bacterium associated with pederin biosynthesis in Paederus sabaeus (Coleoptera: Staphylinidae)
    • Kellner RLL. Molecular identification of an endosymbiotic bacterium associated with pederin biosynthesis in Paederus sabaeus (Coleoptera: Staphylinidae). Insect Biochem. Mol. Biol. 2002; 32: 389-395.
    • (2002) Insect Biochem. Mol. Biol. , vol.32 , pp. 389-395
    • Kellner, R.L.L.1
  • 100
    • 0002190278 scopus 로고
    • Firefly parasites and predators
    • Lloyd JE. Firefly parasites and predators. Coleopt. Bull. 1973; 27: 91-106.
    • (1973) Coleopt. Bull. , vol.27 , pp. 91-106
    • Lloyd, J.E.1
  • 101
    • 85153316506 scopus 로고
    • Aposematism and bioluminescence
    • Guilford T, Cuthill I. Aposematism and bioluminescence. Anim. Behav. 1989; 34: 286-288.
    • (1989) Anim. Behav. , vol.34 , pp. 286-288
    • Guilford, T.1    Cuthill, I.2


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