Biomolecular Chemical Simulations on Enantioselectivity and Reactivity of Lipase Enzymes to Azulene Derivatives ...

• Main Authors: Yagi, Yoichiro, Kimura, Takatomo, Kamezawa, Makoto
• Format: Article in Journal/Newspaper
• Language: unknown
• Published: SAGE Journals 2022
• Subjects: 111599 Pharmacology and Pharmaceutical Sciences not elsewhere classified; FOS: Clinical medicine; Antarc*; Antarctica
• Online Access: https://dx.doi.org/10.25384/sage.c.6060878.v1; https://sage.figshare.com/collections/Biomolecular_Chemical_Simulations_on_Enantioselectivity_and_Reactivity_of_Lipase_Enzymes_to_Azulene_Derivatives/6060878/1

Biomolecular chemical simulations have recently become a useful research method in the fields of organic chemistry and bioscience. In the last few years, we have been focusing on the biomolecular computational simulation on lipase enzyme and ligand complexes to predict the enantioselectivity and reactivity of lipases toward non-natural organic compounds. In this paper, we describe the molecular simulations including molecular dynamics (MD) and fragment molecular orbital (FMO) calculations for the complexes of Candida antarctica lipase type A (CALA) and trifluoromethylazulene alcohol derivatives. From the MD calculations, we found that the fast-reacting enantiomer of esters with high enantioselectivity stays in the vicinity of the active site of CALA, while the slow-reacting enantiomer leaves the active site of CALA. On the other hand, both ( R )- and ( S )-enantiomers of ester with low ensntioselectivity were found to keep near to near the active site of CALA. Further, for the esters that do not react with ...