Enantiodifferentiation of ketoprofen by Japanese firefly luciferase from Luciola lateralis |
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| Affiliation: | 1. Department of Pharmacy, Chungbuk National University, Chungbuk 361-763, Republic of Korea;2. Korea Research Institute of Bioscience and Biotechnology, Ochang 363-883, Republic of Korea;3. College of Pharmacy, Dongguk University, Goyang 410-773, Republic of Korea;1. Department of Chemistry, Ankara University, 06100 Ankara, Turkey;2. Department of Biology, Gazi University, 06500 Ankara, Turkey;3. Department of Physics, Hacettepe University, 06800 Ankara, Turkey;1. School of Pharmacy and Biomedical Sciences, University of Central Lancashire, Maudland Building, Preston, Lancashire PR1 2HE, UK;2. Brain Tumour Research Centre, University of Wolverhampton, Wulfruna Street, Wolverhampton WV1 1LY, UK;1. Department of Biological Science and Technology, Tokyo University of Science, 6-3-1 Niijuku, Katsushika-ku, Tokyo 125-8585, Japan;2. Research Institute for Science and Technology, Tokyo University of Science, 2641 Yamazaki, Noda, Chiba 278-8510, Japan;1. Department of Chemistry, M. V. Lomonosov Moscow State University, 119991 Moscow, Russian Federation;2. Institute of Physiologically Active Compounds, Russian Academy of Sciences, 142432 Chernogolovka, Russian Federation |
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| Abstract: | Recently, we found that firefly luciferase exhibited (R)-enantioselective thioesterification activity toward 2-arylpropanoic acids. In the case of Japanese firefly luciferase from Luciola lateralis (LUC-H), the E-value for ketoprofen was approximately 20. In this study, we used a spectrophotometric method to measure the catalytic activity of LUC-H. Using this method allowed us to judge the reaction efficiency easily. Our results confirmed that LUC-H exhibits enantioselective thioesterification activity toward a series of 2-arylpropanoic acids. The highest activity was observed with ketoprofen. We also observed high enzymatic activity of LUC-H toward long-chain fatty acids. These results were reasonable because LUC-H is homologous with long-chain acyl-CoA synthetase. To obtain further information about the enantiodifferentiation mechanism of the LUC-H catalyzed thioesterification of ketoprofen, we determined the kinetic parameters of the reaction relative to each of its three substrates: ketoprofen, ATP, and coenzyme A (CoASH). We found that whereas the affinities of each compound are not affected by the chirality of ketoprofen, enantiodifferentiation is achieved by a chirality-dependent difference in the kcat parameter. |
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