Is Promiscuous CALB a Good Scaffold for Designing New Epoxidases?
Candida Antarctica lipase B (CALB) is a well-known enzyme, especially because of its promiscuous activity. Due to its properties, CALB was widely used as a benchmark for designing new catalysts for important organic reactions. The active site of CALB is very similar to that of soluble epoxide hydrol...
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ftpubmed:oai:pubmedcentral.nih.gov:6331936 2023-05-15T13:36:39+02:00 Is Promiscuous CALB a Good Scaffold for Designing New Epoxidases? Bordes, Isabel Recatalá, José Świderek, Katarzyna Moliner, Vicent 2015-09-25 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6331936/ http://www.ncbi.nlm.nih.gov/pubmed/26404218 https://doi.org/10.3390/molecules201017789 en eng MDPI http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6331936/ http://www.ncbi.nlm.nih.gov/pubmed/26404218 http://dx.doi.org/10.3390/molecules201017789 © 2015 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/4.0/). CC-BY Article Text 2015 ftpubmed https://doi.org/10.3390/molecules201017789 2019-01-27T01:30:45Z Candida Antarctica lipase B (CALB) is a well-known enzyme, especially because of its promiscuous activity. Due to its properties, CALB was widely used as a benchmark for designing new catalysts for important organic reactions. The active site of CALB is very similar to that of soluble epoxide hydrolase (sEH) formed by a nucleophile-histidine-acid catalytic triad and an oxyanion hole typical for molecular structures derived from processes of α/β hydrolases. In this work we are exploring these similarities and proposing a Ser105Asp variant of CALB as a new catalyst for epoxide hydrolysis. In particular, the hydrolysis of the trans-diphenylpropene oxide (t-DPPO) is studied by means of quantum cluster models mimicking the active site of both enzymes. Our results, based on semi-empirical and DFT calculations, suggest that mutant Ser105Asp CALB is a good protein scaffold to be used for the bio-synthesis of chiral compounds. Text Antarc* Antarctica PubMed Central (PMC) Molecules 20 10 17789 17806 |
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Article Bordes, Isabel Recatalá, José Świderek, Katarzyna Moliner, Vicent Is Promiscuous CALB a Good Scaffold for Designing New Epoxidases? |
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Candida Antarctica lipase B (CALB) is a well-known enzyme, especially because of its promiscuous activity. Due to its properties, CALB was widely used as a benchmark for designing new catalysts for important organic reactions. The active site of CALB is very similar to that of soluble epoxide hydrolase (sEH) formed by a nucleophile-histidine-acid catalytic triad and an oxyanion hole typical for molecular structures derived from processes of α/β hydrolases. In this work we are exploring these similarities and proposing a Ser105Asp variant of CALB as a new catalyst for epoxide hydrolysis. In particular, the hydrolysis of the trans-diphenylpropene oxide (t-DPPO) is studied by means of quantum cluster models mimicking the active site of both enzymes. Our results, based on semi-empirical and DFT calculations, suggest that mutant Ser105Asp CALB is a good protein scaffold to be used for the bio-synthesis of chiral compounds. |
format |
Text |
author |
Bordes, Isabel Recatalá, José Świderek, Katarzyna Moliner, Vicent |
author_facet |
Bordes, Isabel Recatalá, José Świderek, Katarzyna Moliner, Vicent |
author_sort |
Bordes, Isabel |
title |
Is Promiscuous CALB a Good Scaffold for Designing New Epoxidases? |
title_short |
Is Promiscuous CALB a Good Scaffold for Designing New Epoxidases? |
title_full |
Is Promiscuous CALB a Good Scaffold for Designing New Epoxidases? |
title_fullStr |
Is Promiscuous CALB a Good Scaffold for Designing New Epoxidases? |
title_full_unstemmed |
Is Promiscuous CALB a Good Scaffold for Designing New Epoxidases? |
title_sort |
is promiscuous calb a good scaffold for designing new epoxidases? |
publisher |
MDPI |
publishDate |
2015 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6331936/ http://www.ncbi.nlm.nih.gov/pubmed/26404218 https://doi.org/10.3390/molecules201017789 |
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Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_relation |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6331936/ http://www.ncbi.nlm.nih.gov/pubmed/26404218 http://dx.doi.org/10.3390/molecules201017789 |
op_rights |
© 2015 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/4.0/). |
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CC-BY |
op_doi |
https://doi.org/10.3390/molecules201017789 |
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Molecules |
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20 |
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10 |
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17789 |
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17806 |
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1766082171650441216 |