Reaction mechanism and free energy profile for acylation of Candida Antarctica lipase B with methylcaprylate and acetylcholine: Density functional theory calculations |
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| Affiliation: | 1. Biophysical chemistry laboratory, Department of Chemistry, Faculty of Science, Ferdowsi University of Mashhad, Mashhad, Iran;2. Research and Technology Center of Biomolecules, Faculty of Science, Ferdowsi University of Mashhad, Mashhad, Iran;3. Department of Chemistry, University of Isfahan, Isfahan, Iran;1. Higher Medical and Business-technological School of Applied Studies, Hajduk Veljkova 10, 15000 ?abac, Serbia;2. Faculty of Pharmacy, University of Belgrade, Vojvode Stepe 450, 11000 Belgrade, Serbia;1. Institute of Informatics, Silesian University of Technology, ul. Akademicka 2A, 44-100, Gliwice, Poland;2. Faculty of Mechanical Engineering and Computer Science, University of Bielsko - Biala, ul. Willowa 2, 43-309, Bielsko-Biala, Poland;3. Institute of Electronics, Silesian University of Technology, ul. Akademicka 2A, 44-100, Gliwice, Poland;1. State Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences, Beijing 100190, China;2. University of Chinese Academy of Sciences, Beijing, 100049, China;3. Department of Bioproducts and Biosystems Engineering and Biotechnology Institute, University of Minnesota, St. Paul, MN 55108, USA;1. State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, 200237, Shanghai, People’s Republic of China;2. Wuhan Kernel Bio-tech Co. Ltd., People’s Republic of China;3. Hubei Provincial Institute for Food Supervision and Test, Wuhan, 430071, People’s Republic of China;1. State Key Laboratory of Advanced Electromagnetic Engineering and Technology, Huazhong University of Science and Technology, Wuhan, China;2. Hubei Electric Power Company, Wuhan, China;1. Moscow State University of Fine Chemical Technologies, Vernadskogo Pr. 86, 119571 Moscow, Russian Federation;2. Centro de Química Estrutural, Instituto Superior Técnico, University of Lisbon, Av. Rovisco Pais, 1049–001 Lisbon, Portugal;3. Universidade Lusófona de Humanidades e Tecnologias, ULHT Lisbon, Av. Campo Grande 376, 1749-024 Lisbon, Portugal;4. Department of Chemistry, Saint Petersburg State University, Universitetsky pr. 26, 198504 Saint Petersburg, Russian Federation;5. Department of Chemistry, University of Jyväskylä, P.O. Box 35, FI-40014, Finland |
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| Abstract: | Candida Antarctica lipase B (CALB), a specific enzyme to catalyze the hydrolysis of esters, can be a good candidate for acetylcholine (ACh) hydrolysis instead of acetylcholinesterase. The catalytic mechanism of the CALB acylation, as the first stage in the hydrolysis reaction, with ACh and methylcaprylate (MEC) has been examined by using density functional theory technique. The significant emphasis of this article is on the free energy barriers for the acylation step of hydrolysis reactions. Computed free energy barriers of the first step are 9.2 and 15.9 kcal mol?1, but for the second step are 7.9 and 11.6 kcal mol?1 for MEC and ACh respectively. Activation free energies are in the comparable and acceptable range and imply both of two reactions are theoretically possible. The stability role of the adjacent amino acids was examined by using two applied tools. It is exposed that the oxyanion hole residues decrease energy barriers by stabilizing the transition state structures. |
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| Keywords: | Enzyme-substrate interaction MD simulation QM investigation Catalytic hydrolysis Activation energy |
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