The 3D model of the lipase/acyltransferase from [i]Candida parapsilosis[/i], a tool for the elucidation of structural determinants in CAL-A lipase superfamily
Because lipids are hydrophobic, the development of efficient bioconversions in aqueous media free of organic solvents is particularly challenging for green oleochemistry. Within this aim, enzymes exhibiting various abilities to catalyze acyltransfer reaction in water/lipid systems have been identifi...
Published in: | Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics |
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Main Authors: | , , , , , |
Other Authors: | , , , , , , , , |
Format: | Article in Journal/Newspaper |
Language: | English |
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HAL CCSD
2015
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Subjects: | |
Online Access: | https://hal.science/hal-01269354 https://doi.org/10.1016/j.bbapap.2015.06.012 |
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fthalin2p3:oai:HAL:hal-01269354v1 |
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record_format |
openpolar |
institution |
Open Polar |
collection |
HAL-IN2P3 (Institut national de physique nucléaire et de physique des particules) |
op_collection_id |
fthalin2p3 |
language |
English |
topic |
Biocatalysis Protein engineering Lipase/acyltransferase CpLIP2 CAL-A Green chemistry [CHIM.CATA]Chemical Sciences/Catalysis [CHIM.GENI]Chemical Sciences/Chemical engineering |
spellingShingle |
Biocatalysis Protein engineering Lipase/acyltransferase CpLIP2 CAL-A Green chemistry [CHIM.CATA]Chemical Sciences/Catalysis [CHIM.GENI]Chemical Sciences/Chemical engineering Subileau, Maeva Jan, Anne Hélène Nozac'H, Hervé Pérez-Gordo, Marina Perrier, Véronique Dubreucq, Eric The 3D model of the lipase/acyltransferase from [i]Candida parapsilosis[/i], a tool for the elucidation of structural determinants in CAL-A lipase superfamily |
topic_facet |
Biocatalysis Protein engineering Lipase/acyltransferase CpLIP2 CAL-A Green chemistry [CHIM.CATA]Chemical Sciences/Catalysis [CHIM.GENI]Chemical Sciences/Chemical engineering |
description |
Because lipids are hydrophobic, the development of efficient bioconversions in aqueous media free of organic solvents is particularly challenging for green oleochemistry. Within this aim, enzymes exhibiting various abilities to catalyze acyltransfer reaction in water/lipid systems have been identified. Among these, CpLIP2 from Candida parapsilosis has been characterized as a lipase/acyltransferase, able to catalyze acyltransfer reactions preferentially to hydrolysis in the presence of particularly low acyl acceptor concentration and high thermodynamic activity of water (aw > 0.9). Lipase/acyltransferases are thus of great interest, being able to produce new esters at concentrations above the thermodynamic equilibrium of hydrolysis/esterification with limited to no release of free fatty acids. Here, we present a 3D model of CpLIP2 based on homologies with crystallographic structures of Pseudozyma antarctica lipase A. Indeed, the two enzymes have 31% of identity in their primary sequence, yielding a same general structure, but different catalytic properties. The quality of the calculated CpLIP2 model was confirmed by several methods. Limited proteolysis confirmed the location of some loops at the surface of the protein 3D model. Directed mutagenesis also supported the structural model constructed on CAL-A template: the functional properties of various mutants were consistent with their structure-based putative involvement in the oxyanion hole, substrate specificity, acyltransfer or hydrolysis catalysis and structural stability. The CpLIP2 3D model, in comparison with CAL-A 3D structure, brings insights for the elucidation and improvement of the structural determinants involved in the exceptional acyltransferase properties of this promising biocatalyst and of homologous enzymes of the same family. |
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) Service d'Ingénierie Moléculaire pour la Santé (ex SIMOPRO) (SIMoS) Médicaments et Technologies pour la Santé (MTS) Université Paris-Saclay-Direction de Recherche Fondamentale (CEA) (DRF (CEA)) Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Université Paris-Saclay-Direction de Recherche Fondamentale (CEA) (DRF (CEA)) Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE) IIS-Fundación Jiménez Díaz, Department of Allergy Avda Universidad Autónoma de Madrid (UAM) |
format |
Article in Journal/Newspaper |
author |
Subileau, Maeva Jan, Anne Hélène Nozac'H, Hervé Pérez-Gordo, Marina Perrier, Véronique Dubreucq, Eric |
author_facet |
Subileau, Maeva Jan, Anne Hélène Nozac'H, Hervé Pérez-Gordo, Marina Perrier, Véronique Dubreucq, Eric |
author_sort |
Subileau, Maeva |
title |
The 3D model of the lipase/acyltransferase from [i]Candida parapsilosis[/i], a tool for the elucidation of structural determinants in CAL-A lipase superfamily |
title_short |
The 3D model of the lipase/acyltransferase from [i]Candida parapsilosis[/i], a tool for the elucidation of structural determinants in CAL-A lipase superfamily |
title_full |
The 3D model of the lipase/acyltransferase from [i]Candida parapsilosis[/i], a tool for the elucidation of structural determinants in CAL-A lipase superfamily |
title_fullStr |
The 3D model of the lipase/acyltransferase from [i]Candida parapsilosis[/i], a tool for the elucidation of structural determinants in CAL-A lipase superfamily |
title_full_unstemmed |
The 3D model of the lipase/acyltransferase from [i]Candida parapsilosis[/i], a tool for the elucidation of structural determinants in CAL-A lipase superfamily |
title_sort |
3d model of the lipase/acyltransferase from [i]candida parapsilosis[/i], a tool for the elucidation of structural determinants in cal-a lipase superfamily |
publisher |
HAL CCSD |
publishDate |
2015 |
url |
https://hal.science/hal-01269354 https://doi.org/10.1016/j.bbapap.2015.06.012 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
ISSN: 1570-9639 Biochimica et Biophysica Acta Proteins and Proteomics https://hal.science/hal-01269354 Biochimica et Biophysica Acta Proteins and Proteomics, 2015, 1854 (10), pp.1400-1411. ⟨10.1016/j.bbapap.2015.06.012⟩ |
op_relation |
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbapap.2015.06.012 hal-01269354 https://hal.science/hal-01269354 doi:10.1016/j.bbapap.2015.06.012 PRODINRA: 332149 WOS: 000362307500018 |
op_doi |
https://doi.org/10.1016/j.bbapap.2015.06.012 |
container_title |
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics |
container_volume |
1854 |
container_issue |
10 |
container_start_page |
1400 |
op_container_end_page |
1411 |
_version_ |
1766280748891897856 |
spelling |
fthalin2p3:oai:HAL:hal-01269354v1 2023-05-15T14:08:44+02:00 The 3D model of the lipase/acyltransferase from [i]Candida parapsilosis[/i], a tool for the elucidation of structural determinants in CAL-A lipase superfamily Subileau, Maeva Jan, Anne Hélène Nozac'H, Hervé Pérez-Gordo, Marina 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) Service d'Ingénierie Moléculaire pour la Santé (ex SIMOPRO) (SIMoS) Médicaments et Technologies pour la Santé (MTS) Université Paris-Saclay-Direction de Recherche Fondamentale (CEA) (DRF (CEA)) Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Université Paris-Saclay-Direction de Recherche Fondamentale (CEA) (DRF (CEA)) Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE) IIS-Fundación Jiménez Díaz, Department of Allergy Avda Universidad Autónoma de Madrid (UAM) 2015 https://hal.science/hal-01269354 https://doi.org/10.1016/j.bbapap.2015.06.012 en eng HAL CCSD Elsevier info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbapap.2015.06.012 hal-01269354 https://hal.science/hal-01269354 doi:10.1016/j.bbapap.2015.06.012 PRODINRA: 332149 WOS: 000362307500018 ISSN: 1570-9639 Biochimica et Biophysica Acta Proteins and Proteomics https://hal.science/hal-01269354 Biochimica et Biophysica Acta Proteins and Proteomics, 2015, 1854 (10), pp.1400-1411. ⟨10.1016/j.bbapap.2015.06.012⟩ Biocatalysis Protein engineering Lipase/acyltransferase CpLIP2 CAL-A Green chemistry [CHIM.CATA]Chemical Sciences/Catalysis [CHIM.GENI]Chemical Sciences/Chemical engineering info:eu-repo/semantics/article Journal articles 2015 fthalin2p3 https://doi.org/10.1016/j.bbapap.2015.06.012 2023-04-05T16:33:55Z Because lipids are hydrophobic, the development of efficient bioconversions in aqueous media free of organic solvents is particularly challenging for green oleochemistry. Within this aim, enzymes exhibiting various abilities to catalyze acyltransfer reaction in water/lipid systems have been identified. Among these, CpLIP2 from Candida parapsilosis has been characterized as a lipase/acyltransferase, able to catalyze acyltransfer reactions preferentially to hydrolysis in the presence of particularly low acyl acceptor concentration and high thermodynamic activity of water (aw > 0.9). Lipase/acyltransferases are thus of great interest, being able to produce new esters at concentrations above the thermodynamic equilibrium of hydrolysis/esterification with limited to no release of free fatty acids. Here, we present a 3D model of CpLIP2 based on homologies with crystallographic structures of Pseudozyma antarctica lipase A. Indeed, the two enzymes have 31% of identity in their primary sequence, yielding a same general structure, but different catalytic properties. The quality of the calculated CpLIP2 model was confirmed by several methods. Limited proteolysis confirmed the location of some loops at the surface of the protein 3D model. Directed mutagenesis also supported the structural model constructed on CAL-A template: the functional properties of various mutants were consistent with their structure-based putative involvement in the oxyanion hole, substrate specificity, acyltransfer or hydrolysis catalysis and structural stability. The CpLIP2 3D model, in comparison with CAL-A 3D structure, brings insights for the elucidation and improvement of the structural determinants involved in the exceptional acyltransferase properties of this promising biocatalyst and of homologous enzymes of the same family. Article in Journal/Newspaper Antarc* Antarctica HAL-IN2P3 (Institut national de physique nucléaire et de physique des particules) Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1854 10 1400 1411 |