Peculiar features of four enzymes of the CaLA superfamily in aqueous media: Differences in substrate specificities and abilities to catalyze alcoholysis
With 31% of identity with the Lipase A of Candida antarctica (CaLA), the promising lipase/acyltransferase from Candida parapsilosis (CpLIP2) can be classified in the original CaLA-like superfamily. Contrary to CaLA, CpLIP2 has the exceptional property to catalyze acyltransfer reactions preferentiall...
Published in: | Journal of Molecular Catalysis B: Enzymatic |
---|---|
Main Authors: | , , , |
Other Authors: | , |
Format: | Article in Journal/Newspaper |
Language: | English |
Published: |
HAL CCSD
2013
|
Subjects: | |
Online Access: | https://hal.science/hal-01506519 https://doi.org/10.1016/j.molcatb.2013.05.002 |
id |
ftunivnantes:oai:HAL:hal-01506519v1 |
---|---|
record_format |
openpolar |
spelling |
ftunivnantes:oai:HAL:hal-01506519v1 2023-05-15T13:56:02+02:00 Peculiar features of four enzymes of the CaLA superfamily in aqueous media: Differences in substrate specificities and abilities to catalyze alcoholysis Neang, Pisey Subileau, Maeva Perrier, Véronique Dubreucq, Eric 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) 2013 https://hal.science/hal-01506519 https://doi.org/10.1016/j.molcatb.2013.05.002 en eng HAL CCSD Elsevier info:eu-repo/semantics/altIdentifier/doi/10.1016/j.molcatb.2013.05.002 hal-01506519 https://hal.science/hal-01506519 doi:10.1016/j.molcatb.2013.05.002 PRODINRA: 375339 WOS: 000322349300006 ISSN: 1381-1177 Journal of Molecular Catalysis B: Enzymatic https://hal.science/hal-01506519 Journal of Molecular Catalysis B: Enzymatic, 2013, 94, pp.36-46. ⟨10.1016/j.molcatb.2013.05.002⟩ Enzyme catalysis Lipids Lipase/acyltransferase Aqueous medium CaLA like superfamily enzymatic catalysis structure function relationship lipase catalyse enzymatique relation structure fonction acétyltransférase [SDV.IDA]Life Sciences [q-bio]/Food engineering info:eu-repo/semantics/article Journal articles 2013 ftunivnantes https://doi.org/10.1016/j.molcatb.2013.05.002 2023-03-01T05:53:00Z With 31% of identity with the Lipase A of Candida antarctica (CaLA), the promising lipase/acyltransferase from Candida parapsilosis (CpLIP2) can be classified in the original CaLA-like superfamily. Contrary to CaLA, CpLIP2 has the exceptional property to catalyze acyltransfer reactions preferentially to hydrolysis even in aqueous media with high thermodynamic activity of water (aw > 0.9). Two new enzymes, CtroL4 from Candida tropicalis and AflaL0 from Aspergillus flavus, homologous to the CaLA-like superfamily proteins were obtained by heterologous production and used for comparative functional characterization in aqueous media. The ability of the lipases to catalyze acyltransfer reaction in water was correlated with their degree of homology with CpLIP2, indicating a global sequence/function relationship that could be very useful for the selection of new biocatalysts of high industrial interest. The four enzymes exhibited different substrate specificity profiles, considering the length and the carbon chain unsaturation degree of the acyl group in the donor ester, and the class and the position of the hydroxyl group of the acyl accepting alcohol. Within the lipases sequences, peculiar variability in the (putative) substrate binding site was observed and will be further investigated for the elucidation of structure/function relationships. Article in Journal/Newspaper Antarc* Antarctica Université de Nantes: HAL-UNIV-NANTES Journal of Molecular Catalysis B: Enzymatic 94 36 46 |
institution |
Open Polar |
collection |
Université de Nantes: HAL-UNIV-NANTES |
op_collection_id |
ftunivnantes |
language |
English |
topic |
Enzyme catalysis Lipids Lipase/acyltransferase Aqueous medium CaLA like superfamily enzymatic catalysis structure function relationship lipase catalyse enzymatique relation structure fonction acétyltransférase [SDV.IDA]Life Sciences [q-bio]/Food engineering |
spellingShingle |
Enzyme catalysis Lipids Lipase/acyltransferase Aqueous medium CaLA like superfamily enzymatic catalysis structure function relationship lipase catalyse enzymatique relation structure fonction acétyltransférase [SDV.IDA]Life Sciences [q-bio]/Food engineering Neang, Pisey Subileau, Maeva Perrier, Véronique Dubreucq, Eric Peculiar features of four enzymes of the CaLA superfamily in aqueous media: Differences in substrate specificities and abilities to catalyze alcoholysis |
topic_facet |
Enzyme catalysis Lipids Lipase/acyltransferase Aqueous medium CaLA like superfamily enzymatic catalysis structure function relationship lipase catalyse enzymatique relation structure fonction acétyltransférase [SDV.IDA]Life Sciences [q-bio]/Food engineering |
description |
With 31% of identity with the Lipase A of Candida antarctica (CaLA), the promising lipase/acyltransferase from Candida parapsilosis (CpLIP2) can be classified in the original CaLA-like superfamily. Contrary to CaLA, CpLIP2 has the exceptional property to catalyze acyltransfer reactions preferentially to hydrolysis even in aqueous media with high thermodynamic activity of water (aw > 0.9). Two new enzymes, CtroL4 from Candida tropicalis and AflaL0 from Aspergillus flavus, homologous to the CaLA-like superfamily proteins were obtained by heterologous production and used for comparative functional characterization in aqueous media. The ability of the lipases to catalyze acyltransfer reaction in water was correlated with their degree of homology with CpLIP2, indicating a global sequence/function relationship that could be very useful for the selection of new biocatalysts of high industrial interest. The four enzymes exhibited different substrate specificity profiles, considering the length and the carbon chain unsaturation degree of the acyl group in the donor ester, and the class and the position of the hydroxyl group of the acyl accepting alcohol. Within the lipases sequences, peculiar variability in the (putative) substrate binding site was observed and will be further investigated for the elucidation of structure/function relationships. |
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 |
Neang, Pisey Subileau, Maeva Perrier, Véronique Dubreucq, Eric |
author_facet |
Neang, Pisey Subileau, Maeva Perrier, Véronique Dubreucq, Eric |
author_sort |
Neang, Pisey |
title |
Peculiar features of four enzymes of the CaLA superfamily in aqueous media: Differences in substrate specificities and abilities to catalyze alcoholysis |
title_short |
Peculiar features of four enzymes of the CaLA superfamily in aqueous media: Differences in substrate specificities and abilities to catalyze alcoholysis |
title_full |
Peculiar features of four enzymes of the CaLA superfamily in aqueous media: Differences in substrate specificities and abilities to catalyze alcoholysis |
title_fullStr |
Peculiar features of four enzymes of the CaLA superfamily in aqueous media: Differences in substrate specificities and abilities to catalyze alcoholysis |
title_full_unstemmed |
Peculiar features of four enzymes of the CaLA superfamily in aqueous media: Differences in substrate specificities and abilities to catalyze alcoholysis |
title_sort |
peculiar features of four enzymes of the cala superfamily in aqueous media: differences in substrate specificities and abilities to catalyze alcoholysis |
publisher |
HAL CCSD |
publishDate |
2013 |
url |
https://hal.science/hal-01506519 https://doi.org/10.1016/j.molcatb.2013.05.002 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
ISSN: 1381-1177 Journal of Molecular Catalysis B: Enzymatic https://hal.science/hal-01506519 Journal of Molecular Catalysis B: Enzymatic, 2013, 94, pp.36-46. ⟨10.1016/j.molcatb.2013.05.002⟩ |
op_relation |
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.molcatb.2013.05.002 hal-01506519 https://hal.science/hal-01506519 doi:10.1016/j.molcatb.2013.05.002 PRODINRA: 375339 WOS: 000322349300006 |
op_doi |
https://doi.org/10.1016/j.molcatb.2013.05.002 |
container_title |
Journal of Molecular Catalysis B: Enzymatic |
container_volume |
94 |
container_start_page |
36 |
op_container_end_page |
46 |
_version_ |
1766263243819450368 |