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<b>Biomolecular Chemical Simulations toward Elucidation of the Enantioselectivity and Reactivity of Lipases in Organic Synthesis</b><b> </b>
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- Yagi Yoichiro
- Department of Electrical and Electronic Engineering, Okayama University of Science
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- Kimura Takatomo
- Konan Chemical Industry Co., Ltd.
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- Kamezawa Makoto
- Konan Chemical Industry Co., Ltd.
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- Naoshima Yoshinobu
- Research Institute of Natural Sciences, Okayama University of Science
Bibliographic Information
- Other Title
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- 有機合成における酵素リパーゼの鏡像体選択性と反応性の解明に向けた生体分子化学計算
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Description
<p>We are presently continuing to perform biomolecular chemical simulations for Burkholderia cepacia lipase (BCL) and Candida antarctica lipase typeB (CALB) to predict their enantioselectivity and reactivity toward various organic compounds. Here, we describe molecular dynamics (MD) and fragment molecular orbital (FMO) calculations on the complexes of CALB with primary and secondary alcohol esters. For esters with high enantioselectivity, the fast-reacting enantiomer of esters is located near the active site of CALB, whereas the slow-reacting enantiomer of esters moves away from the active site of CALB. On the other hand, for the esters with low enantioselectivity, we found that both (R)- and (S)-enantiomers of esters remain the active site of CALB. The FMO computations indicate that for the esters with high enantioselectivity, each fast-reacting enantiomer shows strong interactions with some particular amino acid residues, including Thr40, whereas for the esters with low enantioselectivity, both (R)- and (S)-enantiomers interact with identical amino acid residues including Thr40. It is predictable that Thr40 in CALB plays an important role in the chiral recognition of enantiomers through lipase-catalyzed biotransformations. </p>
Journal
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- Chem-Bio Informatics Journal
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Chem-Bio Informatics Journal 18 (0), 21-31, 2018
Chem-Bio Informatics Society
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Keywords
Details 詳細情報について
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- CRID
- 1390282680081750784
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- NII Article ID
- 130006339950
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- ISSN
- 13470442
- 13476297
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- Text Lang
- en
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- Data Source
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- JaLC
- Crossref
- CiNii Articles
- OpenAIRE
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- Abstract License Flag
- Disallowed