Solvent as a competitive inhibitor for Candida antarctica lipase B
International audience In enzyme-catalysed reactions, the choice of solvent often has a marked effect on the reaction outcome. In this paper, it is shown that solvent effects could be explained by the ability of the solvent to act as a competitive inhibitor to the substrate. Experimentally, the effe...
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ftccsdartic:oai:HAL:hal-00329734v1 2023-05-15T13:51:27+02:00 Solvent as a competitive inhibitor for Candida antarctica lipase B Graber, Marianne Irague, Romain Rosenfeld, Eric Lamare, Sylvain Franson, Linda Hult, Karl LIttoral ENvironnement et Sociétés - UMRi 7266 (LIENSs) Université de La Rochelle (ULR)-Centre National de la Recherche Scientifique (CNRS) Laboratoire de Biotechnologies et de Chimie Bio-organique (LBCBO) Department of Biochemistry- KTH Royal Institute of Technology Stockholm (KTH ) 2007-05-29 https://hal.archives-ouvertes.fr/hal-00329734 https://hal.archives-ouvertes.fr/hal-00329734/document https://hal.archives-ouvertes.fr/hal-00329734/file/Solvent_inhibitor070413_rev-1_unmarked.pdf en eng HAL CCSD Elsevier hal-00329734 https://hal.archives-ouvertes.fr/hal-00329734 https://hal.archives-ouvertes.fr/hal-00329734/document https://hal.archives-ouvertes.fr/hal-00329734/file/Solvent_inhibitor070413_rev-1_unmarked.pdf info:eu-repo/semantics/OpenAccess ISSN: 1570-9639 Biochimica et Biophysica Acta Proteins and Proteomics https://hal.archives-ouvertes.fr/hal-00329734 Biochimica et Biophysica Acta Proteins and Proteomics, Elsevier, 2007, 1774, pp.1052-1057 [SDV.BIO]Life Sciences [q-bio]/Biotechnology [INFO.INFO-BT]Computer Science [cs]/Biotechnology info:eu-repo/semantics/article Journal articles 2007 ftccsdartic 2021-10-24T20:41:54Z International audience In enzyme-catalysed reactions, the choice of solvent often has a marked effect on the reaction outcome. In this paper, it is shown that solvent effects could be explained by the ability of the solvent to act as a competitive inhibitor to the substrate. Experimentally, the effect of six solvents, 2-pentanone, 3-pentanone, 2-methyl-2-pentanol, 3-methyl-3-pentanol, 2-methylpentane and 3-methylpentane was studied in a solid/gas reactor. As a model reaction, the CALB- catalyzed transacylation between methyl propanoate and 1-propanol, was studied. It was shown that both ketones inhibited the enzyme activity whereas the tertiary alcohols and the hydrocarbons did not. Alcohol inhibition constants, Ki , determined in presence of 2-pentanone, 3-pentanone, and 3-methyl-3-pentanol, confirmed the marked inhibitory character of the ketones and an absence of inhibition of 3-methyl-3-pentanol. The molecular modeling study was performed on three solvents, 2-pentanone, 2-methyl-2-pentanol and 2-methyl pentane. It showed a clear inhibitory effect for the ketone and the tertiary alcohol, but no effect for the hydrocarbon. No change in enzyme conformation was seen during the simulations. The study led to the conclusion that the effect of added organic component on lipase catalyzed transacylation could be explained by the competitive inhibitory character of solvents towards the first binding substrate methyl propionate. Article in Journal/Newspaper Antarc* Antarctica Archive ouverte HAL (Hyper Article en Ligne, CCSD - Centre pour la Communication Scientifique Directe) |
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Archive ouverte HAL (Hyper Article en Ligne, CCSD - Centre pour la Communication Scientifique Directe) |
op_collection_id |
ftccsdartic |
language |
English |
topic |
[SDV.BIO]Life Sciences [q-bio]/Biotechnology [INFO.INFO-BT]Computer Science [cs]/Biotechnology |
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[SDV.BIO]Life Sciences [q-bio]/Biotechnology [INFO.INFO-BT]Computer Science [cs]/Biotechnology Graber, Marianne Irague, Romain Rosenfeld, Eric Lamare, Sylvain Franson, Linda Hult, Karl Solvent as a competitive inhibitor for Candida antarctica lipase B |
topic_facet |
[SDV.BIO]Life Sciences [q-bio]/Biotechnology [INFO.INFO-BT]Computer Science [cs]/Biotechnology |
description |
International audience In enzyme-catalysed reactions, the choice of solvent often has a marked effect on the reaction outcome. In this paper, it is shown that solvent effects could be explained by the ability of the solvent to act as a competitive inhibitor to the substrate. Experimentally, the effect of six solvents, 2-pentanone, 3-pentanone, 2-methyl-2-pentanol, 3-methyl-3-pentanol, 2-methylpentane and 3-methylpentane was studied in a solid/gas reactor. As a model reaction, the CALB- catalyzed transacylation between methyl propanoate and 1-propanol, was studied. It was shown that both ketones inhibited the enzyme activity whereas the tertiary alcohols and the hydrocarbons did not. Alcohol inhibition constants, Ki , determined in presence of 2-pentanone, 3-pentanone, and 3-methyl-3-pentanol, confirmed the marked inhibitory character of the ketones and an absence of inhibition of 3-methyl-3-pentanol. The molecular modeling study was performed on three solvents, 2-pentanone, 2-methyl-2-pentanol and 2-methyl pentane. It showed a clear inhibitory effect for the ketone and the tertiary alcohol, but no effect for the hydrocarbon. No change in enzyme conformation was seen during the simulations. The study led to the conclusion that the effect of added organic component on lipase catalyzed transacylation could be explained by the competitive inhibitory character of solvents towards the first binding substrate methyl propionate. |
author2 |
LIttoral ENvironnement et Sociétés - UMRi 7266 (LIENSs) Université de La Rochelle (ULR)-Centre National de la Recherche Scientifique (CNRS) Laboratoire de Biotechnologies et de Chimie Bio-organique (LBCBO) Department of Biochemistry- KTH Royal Institute of Technology Stockholm (KTH ) |
format |
Article in Journal/Newspaper |
author |
Graber, Marianne Irague, Romain Rosenfeld, Eric Lamare, Sylvain Franson, Linda Hult, Karl |
author_facet |
Graber, Marianne Irague, Romain Rosenfeld, Eric Lamare, Sylvain Franson, Linda Hult, Karl |
author_sort |
Graber, Marianne |
title |
Solvent as a competitive inhibitor for Candida antarctica lipase B |
title_short |
Solvent as a competitive inhibitor for Candida antarctica lipase B |
title_full |
Solvent as a competitive inhibitor for Candida antarctica lipase B |
title_fullStr |
Solvent as a competitive inhibitor for Candida antarctica lipase B |
title_full_unstemmed |
Solvent as a competitive inhibitor for Candida antarctica lipase B |
title_sort |
solvent as a competitive inhibitor for candida antarctica lipase b |
publisher |
HAL CCSD |
publishDate |
2007 |
url |
https://hal.archives-ouvertes.fr/hal-00329734 https://hal.archives-ouvertes.fr/hal-00329734/document https://hal.archives-ouvertes.fr/hal-00329734/file/Solvent_inhibitor070413_rev-1_unmarked.pdf |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
ISSN: 1570-9639 Biochimica et Biophysica Acta Proteins and Proteomics https://hal.archives-ouvertes.fr/hal-00329734 Biochimica et Biophysica Acta Proteins and Proteomics, Elsevier, 2007, 1774, pp.1052-1057 |
op_relation |
hal-00329734 https://hal.archives-ouvertes.fr/hal-00329734 https://hal.archives-ouvertes.fr/hal-00329734/document https://hal.archives-ouvertes.fr/hal-00329734/file/Solvent_inhibitor070413_rev-1_unmarked.pdf |
op_rights |
info:eu-repo/semantics/OpenAccess |
_version_ |
1766255326357618688 |