Revealing the Roles of Subdomains in the Catalytic Behavior of Lipases/Acyltransferases Homologous to CpLIP2 through Rational Design of Chimeric Enzymes
LiPolGreen platform (http://www.supagro.fr/plantlippolgreen/) UMR IATE fermentation platform The lipases/acyltransferases homologous to CpLIP2 of Candida parapsilosis efficiently catalyze acyltransfer reactions in lipid/water media with high water activity (a(W)>0.9). Two new enzymes of this fami...
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ftunimontpellier:oai:HAL:hal-01607598v1 2023-07-16T03:54:30+02:00 Revealing the Roles of Subdomains in the Catalytic Behavior of Lipases/Acyltransferases Homologous to CpLIP2 through Rational Design of Chimeric Enzymes Jan, Anne Hélène Dubreucq, Eric Subileau, Maeva Ingénierie des Agro-polymères et Technologies Émergentes (UMR IATE) Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-Institut National de la Recherche Agronomique (INRA)-Université Montpellier 2 - Sciences et Techniques (UM2)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Université de Montpellier (UM)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro) 2017 https://hal.science/hal-01607598 https://doi.org/10.1002/cbic.201600672 en eng HAL CCSD Wiley-VCH Verlag info:eu-repo/semantics/altIdentifier/doi/10.1002/cbic.201600672 info:eu-repo/semantics/altIdentifier/pmid/28258600 hal-01607598 https://hal.science/hal-01607598 doi:10.1002/cbic.201600672 PRODINRA: 395785 PUBMED: 28258600 WOS: 000401868700012 ISSN: 1439-4227 EISSN: 1439-7633 ChemBioChem https://hal.science/hal-01607598 ChemBioChem, 2017, 18 (10), pp.941 - 950. ⟨10.1002/cbic.201600672⟩ catalyst activity cap enzyme catalysis lipases acyltransferases protein engineering structure-activity relationships acyltransférase protéine chimere lipase activité catalytique [SDV.IDA]Life Sciences [q-bio]/Food engineering info:eu-repo/semantics/article Journal articles 2017 ftunimontpellier https://doi.org/10.1002/cbic.201600672 2023-06-27T22:55:33Z LiPolGreen platform (http://www.supagro.fr/plantlippolgreen/) UMR IATE fermentation platform The lipases/acyltransferases homologous to CpLIP2 of Candida parapsilosis efficiently catalyze acyltransfer reactions in lipid/water media with high water activity (a(W)>0.9). Two new enzymes of this family, CduLAc from Candida dubliniensis and CalLAc8 from Candida albicans, were characterized. Despite 82% sequence identity, the two enzymes have significant differences in their catalytic behaviors. In order to understand the roles played by the different subdomains of these proteins (main core, cap and C-terminal flap), chimeric enzymes were designed by rational exchange of cap and C-terminal flap, between CduLAc and CalLAc8. The results show that the cap region plays a significant role in substrate specificity; the main core was found to be the most important part of the protein for acyltransfer ability. Similar exchanges were made with CAL-A from Candida antarctica, but only the C-terminal exchange was successful. Yet, the role of this domain was not clearly elucidated, other than that it is essential for activity. Article in Journal/Newspaper Antarc* Antarctica Université de Montpellier: HAL ChemBioChem 18 10 941 950 |
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Université de Montpellier: HAL |
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ftunimontpellier |
language |
English |
topic |
catalyst activity cap enzyme catalysis lipases acyltransferases protein engineering structure-activity relationships acyltransférase protéine chimere lipase activité catalytique [SDV.IDA]Life Sciences [q-bio]/Food engineering |
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catalyst activity cap enzyme catalysis lipases acyltransferases protein engineering structure-activity relationships acyltransférase protéine chimere lipase activité catalytique [SDV.IDA]Life Sciences [q-bio]/Food engineering Jan, Anne Hélène Dubreucq, Eric Subileau, Maeva Revealing the Roles of Subdomains in the Catalytic Behavior of Lipases/Acyltransferases Homologous to CpLIP2 through Rational Design of Chimeric Enzymes |
topic_facet |
catalyst activity cap enzyme catalysis lipases acyltransferases protein engineering structure-activity relationships acyltransférase protéine chimere lipase activité catalytique [SDV.IDA]Life Sciences [q-bio]/Food engineering |
description |
LiPolGreen platform (http://www.supagro.fr/plantlippolgreen/) UMR IATE fermentation platform The lipases/acyltransferases homologous to CpLIP2 of Candida parapsilosis efficiently catalyze acyltransfer reactions in lipid/water media with high water activity (a(W)>0.9). Two new enzymes of this family, CduLAc from Candida dubliniensis and CalLAc8 from Candida albicans, were characterized. Despite 82% sequence identity, the two enzymes have significant differences in their catalytic behaviors. In order to understand the roles played by the different subdomains of these proteins (main core, cap and C-terminal flap), chimeric enzymes were designed by rational exchange of cap and C-terminal flap, between CduLAc and CalLAc8. The results show that the cap region plays a significant role in substrate specificity; the main core was found to be the most important part of the protein for acyltransfer ability. Similar exchanges were made with CAL-A from Candida antarctica, but only the C-terminal exchange was successful. Yet, the role of this domain was not clearly elucidated, other than that it is essential for activity. |
author2 |
Ingénierie des Agro-polymères et Technologies Émergentes (UMR IATE) Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-Institut National de la Recherche Agronomique (INRA)-Université Montpellier 2 - Sciences et Techniques (UM2)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Université de Montpellier (UM)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro) |
format |
Article in Journal/Newspaper |
author |
Jan, Anne Hélène Dubreucq, Eric Subileau, Maeva |
author_facet |
Jan, Anne Hélène Dubreucq, Eric Subileau, Maeva |
author_sort |
Jan, Anne Hélène |
title |
Revealing the Roles of Subdomains in the Catalytic Behavior of Lipases/Acyltransferases Homologous to CpLIP2 through Rational Design of Chimeric Enzymes |
title_short |
Revealing the Roles of Subdomains in the Catalytic Behavior of Lipases/Acyltransferases Homologous to CpLIP2 through Rational Design of Chimeric Enzymes |
title_full |
Revealing the Roles of Subdomains in the Catalytic Behavior of Lipases/Acyltransferases Homologous to CpLIP2 through Rational Design of Chimeric Enzymes |
title_fullStr |
Revealing the Roles of Subdomains in the Catalytic Behavior of Lipases/Acyltransferases Homologous to CpLIP2 through Rational Design of Chimeric Enzymes |
title_full_unstemmed |
Revealing the Roles of Subdomains in the Catalytic Behavior of Lipases/Acyltransferases Homologous to CpLIP2 through Rational Design of Chimeric Enzymes |
title_sort |
revealing the roles of subdomains in the catalytic behavior of lipases/acyltransferases homologous to cplip2 through rational design of chimeric enzymes |
publisher |
HAL CCSD |
publishDate |
2017 |
url |
https://hal.science/hal-01607598 https://doi.org/10.1002/cbic.201600672 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
ISSN: 1439-4227 EISSN: 1439-7633 ChemBioChem https://hal.science/hal-01607598 ChemBioChem, 2017, 18 (10), pp.941 - 950. ⟨10.1002/cbic.201600672⟩ |
op_relation |
info:eu-repo/semantics/altIdentifier/doi/10.1002/cbic.201600672 info:eu-repo/semantics/altIdentifier/pmid/28258600 hal-01607598 https://hal.science/hal-01607598 doi:10.1002/cbic.201600672 PRODINRA: 395785 PUBMED: 28258600 WOS: 000401868700012 |
op_doi |
https://doi.org/10.1002/cbic.201600672 |
container_title |
ChemBioChem |
container_volume |
18 |
container_issue |
10 |
container_start_page |
941 |
op_container_end_page |
950 |
_version_ |
1771551727722430464 |