Specificity in lipases: A computational study of transesterification of sucrose
Computational conformational searches of putative transition states of the reaction of sucrose with vinyl laurate catalyzed by lipases from Candida antarctica B and Thermomyces lanuginosus have been carried out. The dielectric of the media have been varied to understand the role of protein plasticit...
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ftpubmed:oai:pubmedcentral.nih.gov:2287317 2023-05-15T13:45:14+02:00 Specificity in lipases: A computational study of transesterification of sucrose Fuentes, Gloria Ballesteros, Anthonio Verma, Chandra S. 2004-12 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2287317 http://www.ncbi.nlm.nih.gov/pubmed/15557256 https://doi.org/10.1110/ps.04724504 en eng Cold Spring Harbor Laboratory Press http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2287317 http://www.ncbi.nlm.nih.gov/pubmed/15557256 http://dx.doi.org/10.1110/ps.04724504 Copyright © Copyright 2004 The Protein Society Article Text 2004 ftpubmed https://doi.org/10.1110/ps.04724504 2013-09-01T17:30:30Z Computational conformational searches of putative transition states of the reaction of sucrose with vinyl laurate catalyzed by lipases from Candida antarctica B and Thermomyces lanuginosus have been carried out. The dielectric of the media have been varied to understand the role of protein plasticity in modulating the observed regioselective transesterification. The binding pocket of lipase from Candida adapts to the conformational variability of the various substates of the substrates by small, local adjustments within the binding pocket. In contrast, the more constrained pocket of the lipase from Thermomyces adapts by adjusting through concerted global motions between subdomains. This leads to the identification of one large pocket in Candida that accommodates both the sucrose and the lauroyl moieties of the transition state, whereas in Thermomyces the binding pocket is smaller, leading to the localization of the two moieties in two distinct pockets; this partly rationalizes the broader specificity of the former relative to the latter. Mutations have been suggested to exploit the differences towards changing the observed selectivities. Text Antarc* Antarctica PubMed Central (PMC) Protein Science 13 12 3092 3103 |
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Article Fuentes, Gloria Ballesteros, Anthonio Verma, Chandra S. Specificity in lipases: A computational study of transesterification of sucrose |
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Article |
description |
Computational conformational searches of putative transition states of the reaction of sucrose with vinyl laurate catalyzed by lipases from Candida antarctica B and Thermomyces lanuginosus have been carried out. The dielectric of the media have been varied to understand the role of protein plasticity in modulating the observed regioselective transesterification. The binding pocket of lipase from Candida adapts to the conformational variability of the various substates of the substrates by small, local adjustments within the binding pocket. In contrast, the more constrained pocket of the lipase from Thermomyces adapts by adjusting through concerted global motions between subdomains. This leads to the identification of one large pocket in Candida that accommodates both the sucrose and the lauroyl moieties of the transition state, whereas in Thermomyces the binding pocket is smaller, leading to the localization of the two moieties in two distinct pockets; this partly rationalizes the broader specificity of the former relative to the latter. Mutations have been suggested to exploit the differences towards changing the observed selectivities. |
format |
Text |
author |
Fuentes, Gloria Ballesteros, Anthonio Verma, Chandra S. |
author_facet |
Fuentes, Gloria Ballesteros, Anthonio Verma, Chandra S. |
author_sort |
Fuentes, Gloria |
title |
Specificity in lipases: A computational study of transesterification of sucrose |
title_short |
Specificity in lipases: A computational study of transesterification of sucrose |
title_full |
Specificity in lipases: A computational study of transesterification of sucrose |
title_fullStr |
Specificity in lipases: A computational study of transesterification of sucrose |
title_full_unstemmed |
Specificity in lipases: A computational study of transesterification of sucrose |
title_sort |
specificity in lipases: a computational study of transesterification of sucrose |
publisher |
Cold Spring Harbor Laboratory Press |
publishDate |
2004 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2287317 http://www.ncbi.nlm.nih.gov/pubmed/15557256 https://doi.org/10.1110/ps.04724504 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_relation |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2287317 http://www.ncbi.nlm.nih.gov/pubmed/15557256 http://dx.doi.org/10.1110/ps.04724504 |
op_rights |
Copyright © Copyright 2004 The Protein Society |
op_doi |
https://doi.org/10.1110/ps.04724504 |
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Protein Science |
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13 |
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12 |
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3092 |
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3103 |
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1766217738618929152 |