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Structural origin and evolution of luciferase/oxigenase activity in AMP-CoA-ligases and beetle luciferases

Grant number: 12/04857-0
Support Opportunities:Regular Research Grants
Duration: August 01, 2012 - July 31, 2014
Field of knowledge:Biological Sciences - Biophysics - Radiology and Photobiology
Valor Concedido/Desembolsado (R$): 128,961.31 / 128,961.31
Principal Investigator:Vadim Viviani
Grantee:Vadim Viviani
Host Institution: Centro de Ciências e Tecnologias para a Sustentabilidade (CCTS). Universidade Federal de São Carlos (UFSCAR). Sorocaba , SP, Brazil
Associated researchers:Mário Tyago Murakami


Beetle luciferases arose from AMP-ligases. Because they display two catalytic functions, AMP/CoA-ligase and oxygenase, they constitute ideal models to investigate the structural and functional evolution of new catalytic functions in enzymes. Furthermore, because their biotechnological importance as bioanlaytical reagents and as reporter genes, such knowledge about structure, function and evolution are essential to develop new luciferases and even to develop luciferase activity in other enzymes, expanding the range of biotechnological and biomedical applications. However, the structural determinants of bioluminescence colors, and mainly of luciferase activity remain poorly understood. Previously our group cloned several new luciferases from bioluminescent beetles, among them the red emitting luciferase of Phrixotrix railroadworm, the luciferase of Pyrearinust termitilluminanas and some pH-sensitive luciferases from fireflies, and with them performed studies about the relationship between bioluminescence colors and structure, identifying important structural determinants. More recently we cloned the luciferase-like enzymes from Zophobas morio mealworm which constitute the first reasonable model of protoluciferase. This enzyme was partially characterized and an important structural determinant of luciferase activity was identified. However these studies are just at the beginning and new regions and residues involved with determination of luciferase activity remain to be identified. Furthermore, the natural substrate and enzymatic function of this new enzyme in the Malpighian tubules remains unknown. Therefore, with the aim to elucidate the structural determinants of luciferase activity, the following topics will be investigated: (1) the relationship between structure and luciferase activity in Zophobas morio protoluciferase and beetle luciferases, through site-directed and random mutagenesis; (2) thioesterase activity of this enzyme with distinct carboxylic substrates to identify the natural substrate of this enzyme; (3) the oxygenase activity of this protoluciferase and other beetle luciferases and (4) the structure of the active site of this enzyme and beetle luciferases from Phrixotrix hirtus e Pyrearinus termitilluminans, in the presence of CoA and luciferin analogs in order to identify the structural determinants of luciferase activity and the oxygen binding site. (AU)

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Scientific publications
(References retrieved automatically from Web of Science and SciELO through information on FAPESP grants and their corresponding numbers as mentioned in the publications by the authors)
VIVIANI, VADIM R.; RODRIGUES NEVES, DEIMISON; TRABUCO AMARAL, DANILO; PRADO, ROGILENE A.; MATSUHASHI, TAKUTO; HIRANO, TAKASHI. Bioluminescence of Beetle Luciferases with 6 `-Amino-D-luciferin Analogues Reveals Excited Keto-oxyluciferin as the Emitter and Phenolate/Luciferin Binding Site Interactions Modulate Bioluminescence Colors. BIOCHEMISTRY, v. 53, n. 32, p. 5208-5220, . (12/04857-0, 11/23961-0)
VIVIANI, V. R.; AMARAL, D. T.; NEVES, D. R.; SIMOES, A.; ARNOLDI, F. G. C.. The Luciferin Binding Site Residues C/T311 (S314) Influence the Bioluminescence Color of Beetle Luciferases through Main-Chain Interaction with Oxyluciferin Phenolate. BIOCHEMISTRY, v. 52, n. 1, p. 19-27, . (12/04857-0, 11/23961-0)

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