NDLI: The origin of luciferase activity in Zophobas mealworm AMP/CoA-ligase (protoluciferase): luciferin stereoselectivity as a switch for the oxygenase activity

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The origin of luciferase activity in Zophobas mealworm AMP/CoA-ligase (protoluciferase): luciferin stereoselectivity as a switch for the oxygenase activity

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Photochemical & Photobiological Sciences Vol - 9 Issue - 7

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The origin of luciferase activity in Zophobas mealworm AMP/CoA-ligase (protoluciferase): luciferin stereoselectivity as a switch for the oxygenase activity

Content Provider	Royal Society of Chemistry (RSC)
Author	Barbosa, João A. R. G. Scorsato, Valeria Viviani, Vadim R. Ohmiya, Yoshihiro Prado, Rogilene A. Pereira, Jose G. C. Niwa, Kazuki
Copyright Year	2010
Abstract	Beetle luciferases evolved from AMP/CoA-ligases. However, it is unclear how the new luciferase activity evolved. In order to clarify this question, we compared the luminescence and catalytic properties of a recently cloned luciferase-like enzyme from Zophobas mealworm, an AMP/CoA-ligase displaying weak luminescence activity, with those of cloned luciferases from the three main families of luminescent beetles: Phrixthrix hirtus railroad worm; Pyrearinus termitilluminans click beetle and Photinus pyralis firefly. The catalytic constant of the mealworm enzyme was 2–4 orders of magnitude lower than that of beetle luciferases, but 3 orders of magnitude above the non-catalyzed chemiluminescence of luciferyl-adenylate in buffer. Studies with D- and L-luciferin and their adenylates show that the luminescence reaction of the luciferase-like enzyme and beetle luciferases are stereoselective for D-luciferin and its adenylate, and that the selectivity is determined mainly at the adenylation step. Modelling studies showed that the luciferin binding site cavity of this enzyme is smaller and more hydrophobic than that of beetle luciferases. Therefore Zophobas mealworm enzyme displays true luciferase activity, keeping the attributes of an ancient protoluciferase. These results suggest that stereoselectivity for D-luciferin may have been a key event for the origin of oxygenase/luciferase activity in AMP/CoA-ligases, and that efficient luciferase activity may have further evolved mainly by increasing the catalytic constant of the oxidative reaction and the quantum yield of bioluminescence.
Starting Page	1111
Ending Page	1119
Page Count	9
File Format	HTM / HTML PDF
ISSN	1474905X
Volume Number	9
Issue Number	8
Journal	Photochemical & Photobiological Sciences
DOI	10.1039/c0pp00080a
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Bioluminescence Adenosine monophosphate Enzyme Luciferase Luminescence Mealworm Railroad worm Chemiluminescence Firefly Click beetle Stereoselectivity Quantum Amino acid Luciferin Beetle Zophobas Photinus pyralis
Content Type	Text
Resource Type	Article
Subject	Physical and Theoretical Chemistry

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The origin of luciferase activity in Zophobas mealworm AMP/CoA-ligase (protoluciferase): luciferin stereoselectivity as a switch for the oxygenase activity

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The origin of luciferase activity in Zophobas mealworm AMP/CoA-ligase (protoluciferase): luciferin stereoselectivity as a switch for the oxygenase activity