Structural insights into the binding mode of d-sorbitol with sorbitol dehydrogenase using QM-polarized ligand docking and molecular dynamics simulations
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- 作者：Chandrabose Selvaraja ; 1 ; Gopinath Krishnasamya ; 1 ; Sujit Sadashiv Jagtapa ; 1 ; Sanjay K.S. Patela ; Saurabh Sudha Dhimana ; Tae-Su Kima ; Sanjeev Kumar Singhb ; Jung-Kul Leea ; jkrhee@konkuk.ac.kr" class="auth_mail" title="E-mail the corresponding author
- 关键词：SDH ; sorbitol dehydrogenase ; MDH ; mannitol dehydrogenase ; MD ; molecular dynamics ; QPLD ; quantum polarized ligand docking ; XP ; extra precision ; SP ; standard precision ; QM ; quantum mechanics ; MM ; molecular mechanics
- 刊名：Biochemical Engineering Journal
- 出版年：2016
- 出版时间：15 October 2016
- 年：2016
- 卷：114
- 期：Complete
- 页码：244-256
- 全文大小：5237 K
文摘
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Computational approaches were applied to gain an insight into the binding of d-sorbitol to sorbitol dehydrogenase.
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QM/MM-based interaction studies suggested amino acids actively involved in d-sorbitol binding.
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Replacement of Met366 and Asp368 will be helpful to increase l-sorbose production.