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Firefly luciferase exhibits bimodal action depending on the luciferin chirality.

Research paper by Mitsuhiro M Nakamura, Shojiro S Maki, Yoshiharu Y Amano, Yutaka Y Ohkita, Kazuki K Niwa, Takashi T Hirano, Yoshihiro Y Ohmiya, Haruki H Niwa

Indexed on: 27 Apr '05Published on: 27 Apr '05Published in: Biochemical and Biophysical Research Communications



Abstract

Firefly luciferase is able to convert L-luciferin into luciferyl-CoA even under ordinary aerobic luciferin-luciferase reaction conditions. The luciferase is able to recognize strictly the chirality of the luciferin structure, serving as the acyl-CoA synthetase for L-luciferin, whereas d-luciferin is used for the bioluminescence reaction. D-Luciferin inhibits the luciferyl-CoA synthetase activity of L-luciferin, whereas L-luciferin retards the bioluminescence reaction of D-luciferin, meaning that both enzyme activities are prevented by the enantiomer of its own substrate.