Evolutionary divergence of Ure2pA glutathione transferases in wood degrading fungi.
Identifieur interne : 000265 ( Main/Exploration ); précédent : 000264; suivant : 000266Evolutionary divergence of Ure2pA glutathione transferases in wood degrading fungi.
Auteurs : Thomas Roret [France] ; Anne Thuillier [France] ; Frédérique Favier [France] ; Eric Gelhaye [France] ; Claude Didierjean [France] ; Mélanie Morel-Rouhier [France]Source :
- Fungal genetics and biology : FG & B [ 1096-0937 ] ; 2015.
Descripteurs français
- KwdFr :
- Alignement de séquences (MeSH), Analyse de séquence de protéine (MeSH), Biodiversité (MeSH), Bois (microbiologie), Cristallographie aux rayons X (MeSH), Domaine catalytique (MeSH), Données de séquences moléculaires (MeSH), Glutathion (composition chimique), Glutathion (métabolisme), Glutathione transferase (composition chimique), Glutathione transferase (génétique), Glutathione transferase (métabolisme), Isoenzymes (MeSH), Liaison aux protéines (MeSH), Phanerochaete (classification), Phanerochaete (enzymologie), Phylogenèse (MeSH), Protéines fongiques (composition chimique), Similitude de séquences d'acides aminés (MeSH), Structure secondaire des protéines (MeSH), Séquence d'acides aminés (MeSH), Évolution moléculaire (MeSH).
- MESH :
- composition chimique : Glutathion, Glutathione transferase, Phanerochaete, Protéines fongiques.
- enzymologie : Phanerochaete.
- génétique : Glutathione transferase.
- microbiologie : Bois.
- métabolisme : Glutathion, Glutathione transferase.
- Alignement de séquences, Analyse de séquence de protéine, Biodiversité, Cristallographie aux rayons X, Domaine catalytique, Données de séquences moléculaires, Isoenzymes, Liaison aux protéines, Phylogenèse, Similitude de séquences d'acides aminés, Structure secondaire des protéines, Séquence d'acides aminés, Évolution moléculaire.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Biodiversity (MeSH), Catalytic Domain (MeSH), Crystallography, X-Ray (MeSH), Evolution, Molecular (MeSH), Fungal Proteins (chemistry), Glutathione (chemistry), Glutathione (metabolism), Glutathione Transferase (chemistry), Glutathione Transferase (genetics), Glutathione Transferase (metabolism), Isoenzymes (MeSH), Molecular Sequence Data (MeSH), Phanerochaete (classification), Phanerochaete (enzymology), Phylogeny (MeSH), Protein Binding (MeSH), Protein Structure, Secondary (MeSH), Sequence Alignment (MeSH), Sequence Analysis, Protein (MeSH), Sequence Homology, Amino Acid (MeSH), Wood (microbiology).
- MESH :
- chemical , chemistry : Fungal Proteins, Glutathione, Glutathione Transferase.
- chemical , genetics : Glutathione Transferase.
- chemical , metabolism : Glutathione, Glutathione Transferase.
- classification : Phanerochaete.
- enzymology : Phanerochaete.
- microbiology : Wood.
- Amino Acid Sequence, Biodiversity, Catalytic Domain, Crystallography, X-Ray, Evolution, Molecular, Isoenzymes, Molecular Sequence Data, Phylogeny, Protein Binding, Protein Structure, Secondary, Sequence Alignment, Sequence Analysis, Protein, Sequence Homology, Amino Acid.
Abstract
The intracellular systems of detoxification are crucial for the survival of wood degrading fungi. Within these systems, glutathione transferases could play a major role since this family of enzymes is specifically extended in lignolytic fungi. In particular the Ure2p class represents one third of the total GST number in Phanerochaete chrysosporium. These proteins have been phylogenetically split into two subclasses called Ure2pA and Ure2pB. Ure2pB can be classified as Nu GSTs because of shared structural and functional features with previously characterized bacterial isoforms. Ure2pA can rather be qualified as Nu-like GSTs since they exhibit a number of differences. Ure2pA possess a classical transferase activity, a more divergent catalytic site and a higher structural flexibility for some of them, compared to Nu GSTs. The characterization of four members of this Ure2pA subclass (PcUre2pA4, PcUre2pA5, PcUre2pA6 and PcUre2pA8) revealed specific functional and structural features, suggesting that these enzymes have rapidly evolved and differentiated, probably to adapt to the complex chemical environment associated with wood decomposition.
DOI: 10.1016/j.fgb.2015.09.002
PubMed: 26348000
Affiliations:
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Electronic address: Claude.Didierjean@univ-lorraine.fr.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Université de Lorraine, UMR 7036 CRM(2), F-54506 Vandoeuvre-lès-Nancy, France; CNRS, UMR 7036 CRM(2), F-54506 Vandoeuvre-lès-Nancy</wicri:regionArea><placeName><region type="region" nuts="2">Grand Est</region><region type="old region" nuts="2">Lorraine (région)</region><settlement type="city">Vandœuvre-lès-Nancy</settlement></placeName><orgName type="university">Université de Lorraine</orgName></affiliation></author><author><name sortKey="Morel Rouhier, Melanie" sort="Morel Rouhier, Melanie" uniqKey="Morel Rouhier M" first="Mélanie" last="Morel-Rouhier">Mélanie Morel-Rouhier</name><affiliation wicri:level="4"><nlm:affiliation>Université de Lorraine, UMR 1136 Interactions Arbres/Microorganismes, F-54506 Vandoeuvre-lès-Nancy, France; INRA, UMR 1136 Interactions Arbres/Microorganismes, F-54280 Champenoux, France. 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CNRS, UMR 7036 CRM(2), F-54506 Vandoeuvre-lès-Nancy, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Université de Lorraine, UMR 7036 CRM(2), F-54506 Vandoeuvre-lès-Nancy, France; CNRS, UMR 7036 CRM(2), F-54506 Vandoeuvre-lès-Nancy</wicri:regionArea><placeName><region type="region" nuts="2">Grand Est</region><region type="old region" nuts="2">Lorraine (région)</region><settlement type="city">Vandœuvre-lès-Nancy</settlement></placeName><orgName type="university">Université de Lorraine</orgName></affiliation></author><author><name sortKey="Thuillier, Anne" sort="Thuillier, Anne" uniqKey="Thuillier A" first="Anne" last="Thuillier">Anne Thuillier</name><affiliation wicri:level="4"><nlm:affiliation>Université de Lorraine, UMR 1136 Interactions Arbres/Microorganismes, F-54506 Vandoeuvre-lès-Nancy, France; INRA, UMR 1136 Interactions Arbres/Microorganismes, F-54280 Champenoux, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Université de Lorraine, UMR 1136 Interactions Arbres/Microorganismes, F-54506 Vandoeuvre-lès-Nancy, France; INRA, UMR 1136 Interactions Arbres/Microorganismes, F-54280 Champenoux</wicri:regionArea><placeName><region type="region" nuts="2">Grand Est</region><region type="old region" nuts="2">Lorraine (région)</region><settlement type="city">Champenoux</settlement></placeName><orgName type="university">Université de Lorraine</orgName></affiliation></author><author><name sortKey="Favier, Frederique" sort="Favier, Frederique" uniqKey="Favier F" first="Frédérique" last="Favier">Frédérique Favier</name><affiliation wicri:level="4"><nlm:affiliation>Université de Lorraine, UMR 7036 CRM(2), F-54506 Vandoeuvre-lès-Nancy, France; CNRS, UMR 7036 CRM(2), F-54506 Vandoeuvre-lès-Nancy, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Université de Lorraine, UMR 7036 CRM(2), F-54506 Vandoeuvre-lès-Nancy, France; CNRS, UMR 7036 CRM(2), F-54506 Vandoeuvre-lès-Nancy</wicri:regionArea><placeName><region type="region" nuts="2">Grand Est</region><region type="old region" nuts="2">Lorraine (région)</region><settlement type="city">Vandœuvre-lès-Nancy</settlement></placeName><orgName type="university">Université de Lorraine</orgName></affiliation></author><author><name sortKey="Gelhaye, Eric" sort="Gelhaye, Eric" uniqKey="Gelhaye E" first="Eric" last="Gelhaye">Eric Gelhaye</name><affiliation wicri:level="4"><nlm:affiliation>Université de Lorraine, UMR 1136 Interactions Arbres/Microorganismes, F-54506 Vandoeuvre-lès-Nancy, France; INRA, UMR 1136 Interactions Arbres/Microorganismes, F-54280 Champenoux, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Université de Lorraine, UMR 1136 Interactions Arbres/Microorganismes, F-54506 Vandoeuvre-lès-Nancy, France; INRA, UMR 1136 Interactions Arbres/Microorganismes, F-54280 Champenoux</wicri:regionArea><placeName><region type="region" nuts="2">Grand Est</region><region type="old region" nuts="2">Lorraine (région)</region><settlement type="city">Champenoux</settlement></placeName><orgName type="university">Université de Lorraine</orgName></affiliation></author><author><name sortKey="Didierjean, Claude" sort="Didierjean, Claude" uniqKey="Didierjean C" first="Claude" last="Didierjean">Claude Didierjean</name><affiliation wicri:level="4"><nlm:affiliation>Université de Lorraine, UMR 7036 CRM(2), F-54506 Vandoeuvre-lès-Nancy, France; CNRS, UMR 7036 CRM(2), F-54506 Vandoeuvre-lès-Nancy, France. Electronic address: Claude.Didierjean@univ-lorraine.fr.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Université de Lorraine, UMR 7036 CRM(2), F-54506 Vandoeuvre-lès-Nancy, France; CNRS, UMR 7036 CRM(2), F-54506 Vandoeuvre-lès-Nancy</wicri:regionArea><placeName><region type="region" nuts="2">Grand Est</region><region type="old region" nuts="2">Lorraine (région)</region><settlement type="city">Vandœuvre-lès-Nancy</settlement></placeName><orgName type="university">Université de Lorraine</orgName></affiliation></author><author><name sortKey="Morel Rouhier, Melanie" sort="Morel Rouhier, Melanie" uniqKey="Morel Rouhier M" first="Mélanie" last="Morel-Rouhier">Mélanie Morel-Rouhier</name><affiliation wicri:level="4"><nlm:affiliation>Université de Lorraine, UMR 1136 Interactions Arbres/Microorganismes, F-54506 Vandoeuvre-lès-Nancy, France; INRA, UMR 1136 Interactions Arbres/Microorganismes, F-54280 Champenoux, France. Electronic address: Melanie.Morel@univ-lorraine.fr.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Université de Lorraine, UMR 1136 Interactions Arbres/Microorganismes, F-54506 Vandoeuvre-lès-Nancy, France; INRA, UMR 1136 Interactions Arbres/Microorganismes, F-54280 Champenoux</wicri:regionArea><placeName><region type="region" nuts="2">Grand Est</region><region type="old region" nuts="2">Lorraine (région)</region><settlement type="city">Champenoux</settlement></placeName><orgName type="university">Université de Lorraine</orgName></affiliation></author></analytic><series><title level="j">Fungal genetics and biology : FG & B</title><idno type="eISSN">1096-0937</idno><imprint><date when="2015" type="published">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Biodiversity (MeSH)</term><term>Catalytic Domain (MeSH)</term><term>Crystallography, X-Ray (MeSH)</term><term>Evolution, Molecular (MeSH)</term><term>Fungal Proteins (chemistry)</term><term>Glutathione (chemistry)</term><term>Glutathione (metabolism)</term><term>Glutathione Transferase (chemistry)</term><term>Glutathione Transferase (genetics)</term><term>Glutathione Transferase (metabolism)</term><term>Isoenzymes (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Phanerochaete (classification)</term><term>Phanerochaete (enzymology)</term><term>Phylogeny (MeSH)</term><term>Protein Binding (MeSH)</term><term>Protein Structure, Secondary (MeSH)</term><term>Sequence Alignment (MeSH)</term><term>Sequence Analysis, Protein (MeSH)</term><term>Sequence Homology, Amino Acid (MeSH)</term><term>Wood (microbiology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Alignement de séquences (MeSH)</term><term>Analyse de séquence de protéine (MeSH)</term><term>Biodiversité (MeSH)</term><term>Bois (microbiologie)</term><term>Cristallographie aux rayons X (MeSH)</term><term>Domaine catalytique (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Glutathion (composition chimique)</term><term>Glutathion (métabolisme)</term><term>Glutathione transferase (composition chimique)</term><term>Glutathione transferase (génétique)</term><term>Glutathione transferase (métabolisme)</term><term>Isoenzymes (MeSH)</term><term>Liaison aux protéines (MeSH)</term><term>Phanerochaete (classification)</term><term>Phanerochaete (enzymologie)</term><term>Phylogenèse (MeSH)</term><term>Protéines fongiques (composition chimique)</term><term>Similitude de séquences d'acides aminés (MeSH)</term><term>Structure secondaire des protéines (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Évolution moléculaire (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Fungal Proteins</term><term>Glutathione</term><term>Glutathione Transferase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Glutathione Transferase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutathione</term><term>Glutathione Transferase</term></keywords><keywords scheme="MESH" qualifier="classification" xml:lang="en"><term>Phanerochaete</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Glutathion</term><term>Glutathione transferase</term><term>Phanerochaete</term><term>Protéines fongiques</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Phanerochaete</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Phanerochaete</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Glutathione transferase</term></keywords><keywords scheme="MESH" qualifier="microbiologie" xml:lang="fr"><term>Bois</term></keywords><keywords scheme="MESH" qualifier="microbiology" xml:lang="en"><term>Wood</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glutathion</term><term>Glutathione transferase</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Biodiversity</term><term>Catalytic Domain</term><term>Crystallography, X-Ray</term><term>Evolution, Molecular</term><term>Isoenzymes</term><term>Molecular Sequence Data</term><term>Phylogeny</term><term>Protein Binding</term><term>Protein Structure, Secondary</term><term>Sequence Alignment</term><term>Sequence Analysis, Protein</term><term>Sequence Homology, Amino Acid</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Alignement de séquences</term><term>Analyse de séquence de protéine</term><term>Biodiversité</term><term>Cristallographie aux rayons X</term><term>Domaine catalytique</term><term>Données de séquences moléculaires</term><term>Isoenzymes</term><term>Liaison aux protéines</term><term>Phylogenèse</term><term>Similitude de séquences d'acides aminés</term><term>Structure secondaire des protéines</term><term>Séquence d'acides aminés</term><term>Évolution moléculaire</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The intracellular systems of detoxification are crucial for the survival of wood degrading fungi. Within these systems, glutathione transferases could play a major role since this family of enzymes is specifically extended in lignolytic fungi. In particular the Ure2p class represents one third of the total GST number in Phanerochaete chrysosporium. These proteins have been phylogenetically split into two subclasses called Ure2pA and Ure2pB. Ure2pB can be classified as Nu GSTs because of shared structural and functional features with previously characterized bacterial isoforms. Ure2pA can rather be qualified as Nu-like GSTs since they exhibit a number of differences. Ure2pA possess a classical transferase activity, a more divergent catalytic site and a higher structural flexibility for some of them, compared to Nu GSTs. The characterization of four members of this Ure2pA subclass (PcUre2pA4, PcUre2pA5, PcUre2pA6 and PcUre2pA8) revealed specific functional and structural features, suggesting that these enzymes have rapidly evolved and differentiated, probably to adapt to the complex chemical environment associated with wood decomposition. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">26348000</PMID><DateCompleted><Year>2016</Year><Month>07</Month><Day>27</Day></DateCompleted><DateRevised><Year>2017</Year><Month>11</Month><Day>07</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1096-0937</ISSN><JournalIssue CitedMedium="Internet"><Volume>83</Volume><PubDate><Year>2015</Year><Month>Oct</Month></PubDate></JournalIssue><Title>Fungal genetics and biology : FG & B</Title><ISOAbbreviation>Fungal Genet Biol</ISOAbbreviation></Journal><ArticleTitle>Evolutionary divergence of Ure2pA glutathione transferases in wood degrading fungi.</ArticleTitle><Pagination><MedlinePgn>103-112</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S1087-1845(15)30026-8</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.fgb.2015.09.002</ELocationID><Abstract><AbstractText>The intracellular systems of detoxification are crucial for the survival of wood degrading fungi. Within these systems, glutathione transferases could play a major role since this family of enzymes is specifically extended in lignolytic fungi. In particular the Ure2p class represents one third of the total GST number in Phanerochaete chrysosporium. These proteins have been phylogenetically split into two subclasses called Ure2pA and Ure2pB. Ure2pB can be classified as Nu GSTs because of shared structural and functional features with previously characterized bacterial isoforms. Ure2pA can rather be qualified as Nu-like GSTs since they exhibit a number of differences. Ure2pA possess a classical transferase activity, a more divergent catalytic site and a higher structural flexibility for some of them, compared to Nu GSTs. The characterization of four members of this Ure2pA subclass (PcUre2pA4, PcUre2pA5, PcUre2pA6 and PcUre2pA8) revealed specific functional and structural features, suggesting that these enzymes have rapidly evolved and differentiated, probably to adapt to the complex chemical environment associated with wood decomposition. </AbstractText><CopyrightInformation>Copyright © 2015 Elsevier Inc. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Roret</LastName><ForeName>Thomas</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Université de Lorraine, UMR 7036 CRM(2), F-54506 Vandoeuvre-lès-Nancy, France; CNRS, UMR 7036 CRM(2), F-54506 Vandoeuvre-lès-Nancy, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Thuillier</LastName><ForeName>Anne</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Université de Lorraine, UMR 1136 Interactions Arbres/Microorganismes, F-54506 Vandoeuvre-lès-Nancy, France; INRA, UMR 1136 Interactions Arbres/Microorganismes, F-54280 Champenoux, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Favier</LastName><ForeName>Frédérique</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>Université de Lorraine, UMR 7036 CRM(2), F-54506 Vandoeuvre-lès-Nancy, France; CNRS, UMR 7036 CRM(2), F-54506 Vandoeuvre-lès-Nancy, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Gelhaye</LastName><ForeName>Eric</ForeName><Initials>E</Initials><AffiliationInfo><Affiliation>Université de Lorraine, UMR 1136 Interactions Arbres/Microorganismes, F-54506 Vandoeuvre-lès-Nancy, France; INRA, UMR 1136 Interactions Arbres/Microorganismes, F-54280 Champenoux, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Didierjean</LastName><ForeName>Claude</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Université de Lorraine, UMR 7036 CRM(2), F-54506 Vandoeuvre-lès-Nancy, France; CNRS, UMR 7036 CRM(2), F-54506 Vandoeuvre-lès-Nancy, France. Electronic address: Claude.Didierjean@univ-lorraine.fr.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Morel-Rouhier</LastName><ForeName>Mélanie</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Université de Lorraine, UMR 1136 Interactions Arbres/Microorganismes, F-54506 Vandoeuvre-lès-Nancy, France; INRA, UMR 1136 Interactions Arbres/Microorganismes, F-54280 Champenoux, France. Electronic address: Melanie.Morel@univ-lorraine.fr.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2015</Year><Month>09</Month><Day>05</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Fungal Genet Biol</MedlineTA><NlmUniqueID>9607601</NlmUniqueID><ISSNLinking>1087-1845</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005656">Fungal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007527">Isoenzymes</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.5.1.18</RegistryNumber><NameOfSubstance UI="D005982">Glutathione Transferase</NameOfSubstance></Chemical><Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber><NameOfSubstance UI="D005978">Glutathione</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D044822" MajorTopicYN="N">Biodiversity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020134" MajorTopicYN="N">Catalytic Domain</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018360" MajorTopicYN="N">Crystallography, X-Ray</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019143" MajorTopicYN="N">Evolution, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005982" MajorTopicYN="N">Glutathione Transferase</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007527" MajorTopicYN="N">Isoenzymes</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020075" MajorTopicYN="N">Phanerochaete</DescriptorName><QualifierName UI="Q000145" MajorTopicYN="N">classification</QualifierName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010802" MajorTopicYN="N">Phylogeny</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017433" MajorTopicYN="N">Protein Structure, Secondary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016415" MajorTopicYN="N">Sequence Alignment</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020539" MajorTopicYN="N">Sequence Analysis, Protein</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017386" MajorTopicYN="N">Sequence Homology, Amino Acid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014934" MajorTopicYN="N">Wood</DescriptorName><QualifierName UI="Q000382" MajorTopicYN="N">microbiology</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Activity</Keyword><Keyword MajorTopicYN="N">Diversity</Keyword><Keyword MajorTopicYN="N">Glutathione transferase</Keyword><Keyword MajorTopicYN="N">Lignolytic fungi</Keyword><Keyword MajorTopicYN="N">Nu</Keyword><Keyword MajorTopicYN="N">Structure</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2015</Year><Month>05</Month><Day>28</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2015</Year><Month>09</Month><Day>01</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2015</Year><Month>09</Month><Day>04</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2015</Year><Month>9</Month><Day>9</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2015</Year><Month>9</Month><Day>9</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2016</Year><Month>7</Month><Day>28</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">26348000</ArticleId><ArticleId IdType="pii">S1087-1845(15)30026-8</ArticleId><ArticleId IdType="doi">10.1016/j.fgb.2015.09.002</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>France</li></country><region><li>Grand Est</li><li>Lorraine (région)</li></region><settlement><li>Champenoux</li><li>Vandœuvre-lès-Nancy</li></settlement><orgName><li>Université de Lorraine</li></orgName></list><tree><country name="France"><region name="Grand Est"><name sortKey="Roret, Thomas" sort="Roret, Thomas" uniqKey="Roret T" first="Thomas" last="Roret">Thomas Roret</name></region><name sortKey="Didierjean, Claude" sort="Didierjean, Claude" uniqKey="Didierjean C" first="Claude" last="Didierjean">Claude Didierjean</name><name sortKey="Favier, Frederique" sort="Favier, Frederique" uniqKey="Favier F" first="Frédérique" last="Favier">Frédérique Favier</name><name sortKey="Gelhaye, Eric" sort="Gelhaye, Eric" uniqKey="Gelhaye E" first="Eric" last="Gelhaye">Eric Gelhaye</name><name sortKey="Morel Rouhier, Melanie" sort="Morel Rouhier, Melanie" uniqKey="Morel Rouhier M" first="Mélanie" last="Morel-Rouhier">Mélanie Morel-Rouhier</name><name sortKey="Thuillier, Anne" sort="Thuillier, Anne" uniqKey="Thuillier A" first="Anne" last="Thuillier">Anne Thuillier</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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