Biomolecular Simulations on the Complexes of ACA (1’-acetoxychavicol acetate) and Lipases

Yoichiro Yagi, Soya Nakagawa, Takatomo Kimura, Makoto Kamezawa

In this work, we described the molecular simulations including molecular dynamics (MD) and fragment molecular orbital (FMO) calculations for the complexes of Burkholderia cepacia lipase (BCL) and both enantiomers of ACA (1’-acetoxychavicol acetate). The MD calculations show that the fast-reacting (R)-enantiomer of ACA stays in the vicinity of the active site of BCL, while the slow-reacting (S)-enantiomer leaves the active site of BCL. The FMO computations provide us useful information on particular amino acid residues such as Leu17, Thr18, and Tyr29 in BCL that can play an important role in the chiral recognition of substrate enantiomers

The 66th Symposium on the Chemistry of Terpenes, Essential Oils and Aromatics

Symposium on the Chemistry of Terpenes, Essential Oils and Aromatics

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