Molecular modeling of the enantioselectivity in lipase-catalyzed transesterification reactions.
Two strategies based on the use of subsets for calculating the enantioselectivity in lipase-catalyzed transesterifications using the CHARMM force field were investigated. Molecular dynamics was used in our search for low energy conformations. Molecular mechanics was used for refining these low energ...
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ftpubmed:oai:pubmedcentral.nih.gov:1299473 2023-05-15T13:54:17+02:00 Molecular modeling of the enantioselectivity in lipase-catalyzed transesterification reactions. Haeffner, F Norin, T Hult, K 1998-03 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1299473 http://www.ncbi.nlm.nih.gov/pubmed/9512023 en eng http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1299473 http://www.ncbi.nlm.nih.gov/pubmed/9512023 Research Article Text 1998 ftpubmed 2013-08-30T17:52:15Z Two strategies based on the use of subsets for calculating the enantioselectivity in lipase-catalyzed transesterifications using the CHARMM force field were investigated. Molecular dynamics was used in our search for low energy conformations. Molecular mechanics was used for refining these low energy conformations. A tetrahedral intermediate with a rigid central part was used for mimicking the transition state. The energy differences between the transition states of the diastereomeric enzyme-substrate complexes were calculated. The way of defining the subsets was based on two fundamentally different strategies. The first strategy used predefined parts of the enzyme and the substrate as subsets. The second approach formed energy-based subsets, varying in size with the substrates studied. The selection of residues to be included in these energy-based subsets was based on the energy of the interaction between the specific residue or water molecule and the transition state. The reaction studied was the kinetic resolution of secondary alcohols in transesterifications using the Candida antarctica lipase B as chiral biocatalyst. The secondary alcohols used in the study were 2-butanol, 3-methyl-2-butanol, and 3,3-dimethyl-2-butanol. Text Antarc* Antarctica PubMed Central (PMC) |
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Research Article Haeffner, F Norin, T Hult, K Molecular modeling of the enantioselectivity in lipase-catalyzed transesterification reactions. |
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Research Article |
description |
Two strategies based on the use of subsets for calculating the enantioselectivity in lipase-catalyzed transesterifications using the CHARMM force field were investigated. Molecular dynamics was used in our search for low energy conformations. Molecular mechanics was used for refining these low energy conformations. A tetrahedral intermediate with a rigid central part was used for mimicking the transition state. The energy differences between the transition states of the diastereomeric enzyme-substrate complexes were calculated. The way of defining the subsets was based on two fundamentally different strategies. The first strategy used predefined parts of the enzyme and the substrate as subsets. The second approach formed energy-based subsets, varying in size with the substrates studied. The selection of residues to be included in these energy-based subsets was based on the energy of the interaction between the specific residue or water molecule and the transition state. The reaction studied was the kinetic resolution of secondary alcohols in transesterifications using the Candida antarctica lipase B as chiral biocatalyst. The secondary alcohols used in the study were 2-butanol, 3-methyl-2-butanol, and 3,3-dimethyl-2-butanol. |
format |
Text |
author |
Haeffner, F Norin, T Hult, K |
author_facet |
Haeffner, F Norin, T Hult, K |
author_sort |
Haeffner, F |
title |
Molecular modeling of the enantioselectivity in lipase-catalyzed transesterification reactions. |
title_short |
Molecular modeling of the enantioselectivity in lipase-catalyzed transesterification reactions. |
title_full |
Molecular modeling of the enantioselectivity in lipase-catalyzed transesterification reactions. |
title_fullStr |
Molecular modeling of the enantioselectivity in lipase-catalyzed transesterification reactions. |
title_full_unstemmed |
Molecular modeling of the enantioselectivity in lipase-catalyzed transesterification reactions. |
title_sort |
molecular modeling of the enantioselectivity in lipase-catalyzed transesterification reactions. |
publishDate |
1998 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1299473 http://www.ncbi.nlm.nih.gov/pubmed/9512023 |
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Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_relation |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1299473 http://www.ncbi.nlm.nih.gov/pubmed/9512023 |
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1766259977899474944 |