PhytophthoraV1, Main, Exploration, bibRecord, 000D87

Probing the Functions of Carbohydrate Binding Modules in the CBEL Protein from the Oomycete Phytophthora parasitica.

Identifieur interne : 000D87 ( Main/Exploration ); précédent : 000D86; suivant : 000D88

Probing the Functions of Carbohydrate Binding Modules in the CBEL Protein from the Oomycete Phytophthora parasitica.

Auteurs : Thomas Martinez [France] ; Hélène Texier [France] ; Virginie Nahoum [France] ; Claude Lafitte [France] ; Gianluca Cioci [France] ; Laurent Heux [France] ; Bernard Dumas [France] ; Michael O'Donohue [France] ; Elodie Gaulin [France] ; Claire Dumon [France]

Source :

PloS one [ 1932-6203 ] ; 2015.

RBID : pubmed:26390127

Descripteurs français

KwdFr :
- Cellulose (métabolisme), Endo-1,4-beta xylanases (composition chimique), Endo-1,4-beta xylanases (métabolisme), Glycoprotéines (composition chimique), Glycoprotéines (métabolisme), Hydrolyse (MeSH), Lectines (composition chimique), Lectines (métabolisme), Liaison aux protéines (MeSH), Phytophthora (composition chimique), Phytophthora (métabolisme), Sites de fixation (MeSH), Structure tertiaire des protéines (MeSH), Talaromyces (enzymologie), Triticum (métabolisme).
MESH :
- composition chimique : Endo-1,4-beta xylanases, Glycoprotéines, Lectines, Phytophthora.
- enzymologie : Talaromyces.
- métabolisme : Cellulose, Endo-1,4-beta xylanases, Glycoprotéines, Lectines, Phytophthora, Triticum.
- Hydrolyse, Liaison aux protéines, Sites de fixation, Structure tertiaire des protéines.

English descriptors

KwdEn :
- Binding Sites (MeSH), Cellulose (metabolism), Endo-1,4-beta Xylanases (chemistry), Endo-1,4-beta Xylanases (metabolism), Glycoproteins (chemistry), Glycoproteins (metabolism), Hydrolysis (MeSH), Lectins (chemistry), Lectins (metabolism), Phytophthora (chemistry), Phytophthora (metabolism), Protein Binding (MeSH), Protein Structure, Tertiary (MeSH), Talaromyces (enzymology), Triticum (metabolism).
MESH :
- chemical , chemistry : Endo-1,4-beta Xylanases, Glycoproteins, Lectins.
- chemical , metabolism : Cellulose, Endo-1,4-beta Xylanases, Glycoproteins, Lectins.
- chemistry : Phytophthora.
- enzymology : Talaromyces.
- metabolism : Phytophthora, Triticum.
- Binding Sites, Hydrolysis, Protein Binding, Protein Structure, Tertiary.

Abstract

Oomycetes are microorganisms that are distantly related to true fungi and many members of this phylum are major plant pathogens. Oomycetes express proteins that are able to interact with plant cell wall polysaccharides, such as cellulose. This interaction is thought to be mediated by carbohydrate-binding modules that are classified into CBM family 1 in the CAZy database. In this study, the two CBMs (1-1 and 1-2) that form part of the cell wall glycoprotein, CBEL, from Phytophthora parasitica have been submitted to detailed characterization, first to better quantify their interaction with cellulose and second to determine whether these CBMs can be useful for biotechnological applications, such as biomass hydrolysis. A variety of biophysical techniques were used to study the interaction of the CBMs with various substrates and the data obtained indicate that CBEL's CBM1-1 exhibits much greater cellulose binding ability than CBM1-2. Engineering of the family 11 xylanase from Talaromyces versatilis (TvXynB), an enzyme that naturally bears a fungal family 1 CBM, has produced two variants. The first one lacks its native CBM, whereas the second contains the CBEL CBM1-1. The study of these enzymes has revealed that wild type TvXynB binds to cellulose, via its CBM1, and that the substitution of its CBM by oomycetal CBM1-1 does not affect its activity on wheat straw. However, intriguingly the addition of CBEL during the hydrolysis of wheat straw actually potentiates the action of TvXynB variant lacking a CBM1. This suggests that the potentiating effect of CBM1-1 might not require the formation of a covalent linkage to TvXynB.

DOI: 10.1371/journal.pone.0137481
PubMed: 26390127
PubMed Central: PMC4577117

Affiliations:

Links toward previous steps (curation, corpus...)

to stream Main, to step Corpus: 000D64
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Le document en format XML

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<sourceDesc><biblStruct><analytic><title xml:lang="en">Probing the Functions of Carbohydrate Binding Modules in the CBEL Protein from the Oomycete Phytophthora parasitica.</title>
<author><name sortKey="Martinez, Thomas" sort="Martinez, Thomas" uniqKey="Martinez T" first="Thomas" last="Martinez">Thomas Martinez</name>
<affiliation wicri:level="4"><nlm:affiliation>Université Toulouse 3, UPS, Laboratoire de Recherche en Sciences Végétales, 24 chemin de Borde Rouge, BP42617, Auzeville, F-31326, Castanet-Tolosan, France; CNRS, Laboratoire de Recherche en Sciences Végétales, 24 chemin de Borde Rouge, BP42617, Auzeville, F-31326, Castanet-Tolosan, France; Université de Toulouse; INSA, UPS, INP, LISBP, 135 Avenue de Rangueil, F-31077 Toulouse, France; CNRS, UMR5504, F-31400 Toulouse, France; INRA, UMR792 Ingénierie des Systèmes Biologiques et des Procédés, F-31400 Toulouse, France.</nlm:affiliation>
<country xml:lang="fr">France</country>
<wicri:regionArea>Université Toulouse 3, UPS, Laboratoire de Recherche en Sciences Végétales, 24 chemin de Borde Rouge, BP42617, Auzeville, F-31326, Castanet-Tolosan, France; CNRS, Laboratoire de Recherche en Sciences Végétales, 24 chemin de Borde Rouge, BP42617, Auzeville, F-31326, Castanet-Tolosan, France; Université de Toulouse; INSA, UPS, INP, LISBP, 135 Avenue de Rangueil, F-31077 Toulouse, France; CNRS, UMR5504, F-31400 Toulouse, France; INRA, UMR792 Ingénierie des Systèmes Biologiques et des Procédés, F-31400 Toulouse</wicri:regionArea>
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<author><name sortKey="Texier, Helene" sort="Texier, Helene" uniqKey="Texier H" first="Hélène" last="Texier">Hélène Texier</name>
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<author><name sortKey="Cioci, Gianluca" sort="Cioci, Gianluca" uniqKey="Cioci G" first="Gianluca" last="Cioci">Gianluca Cioci</name>
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<author><name sortKey="Heux, Laurent" sort="Heux, Laurent" uniqKey="Heux L" first="Laurent" last="Heux">Laurent Heux</name>
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<author><name sortKey="Dumas, Bernard" sort="Dumas, Bernard" uniqKey="Dumas B" first="Bernard" last="Dumas">Bernard Dumas</name>
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<country xml:lang="fr">France</country>
<wicri:regionArea>Université Toulouse 3, UPS, Laboratoire de Recherche en Sciences Végétales, 24 chemin de Borde Rouge, BP42617, Auzeville, F-31326, Castanet-Tolosan, France; CNRS, Laboratoire de Recherche en Sciences Végétales, 24 chemin de Borde Rouge, BP42617, Auzeville, F-31326, Castanet-Tolosan</wicri:regionArea>
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<author><name sortKey="O Donohue, Michael" sort="O Donohue, Michael" uniqKey="O Donohue M" first="Michael" last="O'Donohue">Michael O'Donohue</name>
<affiliation wicri:level="3"><nlm:affiliation>Université de Toulouse; INSA, UPS, INP, LISBP, 135 Avenue de Rangueil, F-31077 Toulouse, France; CNRS, UMR5504, F-31400 Toulouse, France; INRA, UMR792 Ingénierie des Systèmes Biologiques et des Procédés, F-31400 Toulouse, France.</nlm:affiliation>
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<author><name sortKey="Gaulin, Elodie" sort="Gaulin, Elodie" uniqKey="Gaulin E" first="Elodie" last="Gaulin">Elodie Gaulin</name>
<affiliation wicri:level="4"><nlm:affiliation>Université Toulouse 3, UPS, Laboratoire de Recherche en Sciences Végétales, 24 chemin de Borde Rouge, BP42617, Auzeville, F-31326, Castanet-Tolosan, France; CNRS, Laboratoire de Recherche en Sciences Végétales, 24 chemin de Borde Rouge, BP42617, Auzeville, F-31326, Castanet-Tolosan, France.</nlm:affiliation>
<country xml:lang="fr">France</country>
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</placeName>
<orgName type="university">Université Toulouse III - Paul Sabatier</orgName>
</affiliation>
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<author><name sortKey="Dumon, Claire" sort="Dumon, Claire" uniqKey="Dumon C" first="Claire" last="Dumon">Claire Dumon</name>
<affiliation wicri:level="3"><nlm:affiliation>Université de Toulouse; INSA, UPS, INP, LISBP, 135 Avenue de Rangueil, F-31077 Toulouse, France; CNRS, UMR5504, F-31400 Toulouse, France; INRA, UMR792 Ingénierie des Systèmes Biologiques et des Procédés, F-31400 Toulouse, France.</nlm:affiliation>
<country xml:lang="fr">France</country>
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<series><title level="j">PloS one</title>
<idno type="eISSN">1932-6203</idno>
<imprint><date when="2015" type="published">2015</date>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Binding Sites (MeSH)</term>
<term>Cellulose (metabolism)</term>
<term>Endo-1,4-beta Xylanases (chemistry)</term>
<term>Endo-1,4-beta Xylanases (metabolism)</term>
<term>Glycoproteins (chemistry)</term>
<term>Glycoproteins (metabolism)</term>
<term>Hydrolysis (MeSH)</term>
<term>Lectins (chemistry)</term>
<term>Lectins (metabolism)</term>
<term>Phytophthora (chemistry)</term>
<term>Phytophthora (metabolism)</term>
<term>Protein Binding (MeSH)</term>
<term>Protein Structure, Tertiary (MeSH)</term>
<term>Talaromyces (enzymology)</term>
<term>Triticum (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Cellulose (métabolisme)</term>
<term>Endo-1,4-beta xylanases (composition chimique)</term>
<term>Endo-1,4-beta xylanases (métabolisme)</term>
<term>Glycoprotéines (composition chimique)</term>
<term>Glycoprotéines (métabolisme)</term>
<term>Hydrolyse (MeSH)</term>
<term>Lectines (composition chimique)</term>
<term>Lectines (métabolisme)</term>
<term>Liaison aux protéines (MeSH)</term>
<term>Phytophthora (composition chimique)</term>
<term>Phytophthora (métabolisme)</term>
<term>Sites de fixation (MeSH)</term>
<term>Structure tertiaire des protéines (MeSH)</term>
<term>Talaromyces (enzymologie)</term>
<term>Triticum (métabolisme)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Endo-1,4-beta Xylanases</term>
<term>Glycoproteins</term>
<term>Lectins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cellulose</term>
<term>Endo-1,4-beta Xylanases</term>
<term>Glycoproteins</term>
<term>Lectins</term>
</keywords>
<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Phytophthora</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Endo-1,4-beta xylanases</term>
<term>Glycoprotéines</term>
<term>Lectines</term>
<term>Phytophthora</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Talaromyces</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Talaromyces</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Phytophthora</term>
<term>Triticum</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cellulose</term>
<term>Endo-1,4-beta xylanases</term>
<term>Glycoprotéines</term>
<term>Lectines</term>
<term>Phytophthora</term>
<term>Triticum</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Binding Sites</term>
<term>Hydrolysis</term>
<term>Protein Binding</term>
<term>Protein Structure, Tertiary</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Hydrolyse</term>
<term>Liaison aux protéines</term>
<term>Sites de fixation</term>
<term>Structure tertiaire des protéines</term>
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<front><div type="abstract" xml:lang="en">Oomycetes are microorganisms that are distantly related to true fungi and many members of this phylum are major plant pathogens. Oomycetes express proteins that are able to interact with plant cell wall polysaccharides, such as cellulose. This interaction is thought to be mediated by carbohydrate-binding modules that are classified into CBM family 1 in the CAZy database. In this study, the two CBMs (1-1 and 1-2) that form part of the cell wall glycoprotein, CBEL, from Phytophthora parasitica have been submitted to detailed characterization, first to better quantify their interaction with cellulose and second to determine whether these CBMs can be useful for biotechnological applications, such as biomass hydrolysis. A variety of biophysical techniques were used to study the interaction of the CBMs with various substrates and the data obtained indicate that CBEL's CBM1-1 exhibits much greater cellulose binding ability than CBM1-2. Engineering of the family 11 xylanase from Talaromyces versatilis (TvXynB), an enzyme that naturally bears a fungal family 1 CBM, has produced two variants. The first one lacks its native CBM, whereas the second contains the CBEL CBM1-1. The study of these enzymes has revealed that wild type TvXynB binds to cellulose, via its CBM1, and that the substitution of its CBM by oomycetal CBM1-1 does not affect its activity on wheat straw. However, intriguingly the addition of CBEL during the hydrolysis of wheat straw actually potentiates the action of TvXynB variant lacking a CBM1. This suggests that the potentiating effect of CBM1-1 might not require the formation of a covalent linkage to TvXynB. </div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">26390127</PMID>
<DateCompleted><Year>2016</Year>
<Month>05</Month>
<Day>31</Day>
</DateCompleted>
<DateRevised><Year>2018</Year>
<Month>11</Month>
<Day>13</Day>
</DateRevised>
<Article PubModel="Electronic-eCollection"><Journal><ISSN IssnType="Electronic">1932-6203</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>10</Volume>
<Issue>9</Issue>
<PubDate><Year>2015</Year>
</PubDate>
</JournalIssue>
<Title>PloS one</Title>
<ISOAbbreviation>PLoS One</ISOAbbreviation>
</Journal>
<ArticleTitle>Probing the Functions of Carbohydrate Binding Modules in the CBEL Protein from the Oomycete Phytophthora parasitica.</ArticleTitle>
<Pagination><MedlinePgn>e0137481</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1371/journal.pone.0137481</ELocationID>
<Abstract><AbstractText>Oomycetes are microorganisms that are distantly related to true fungi and many members of this phylum are major plant pathogens. Oomycetes express proteins that are able to interact with plant cell wall polysaccharides, such as cellulose. This interaction is thought to be mediated by carbohydrate-binding modules that are classified into CBM family 1 in the CAZy database. In this study, the two CBMs (1-1 and 1-2) that form part of the cell wall glycoprotein, CBEL, from Phytophthora parasitica have been submitted to detailed characterization, first to better quantify their interaction with cellulose and second to determine whether these CBMs can be useful for biotechnological applications, such as biomass hydrolysis. A variety of biophysical techniques were used to study the interaction of the CBMs with various substrates and the data obtained indicate that CBEL's CBM1-1 exhibits much greater cellulose binding ability than CBM1-2. Engineering of the family 11 xylanase from Talaromyces versatilis (TvXynB), an enzyme that naturally bears a fungal family 1 CBM, has produced two variants. The first one lacks its native CBM, whereas the second contains the CBEL CBM1-1. The study of these enzymes has revealed that wild type TvXynB binds to cellulose, via its CBM1, and that the substitution of its CBM by oomycetal CBM1-1 does not affect its activity on wheat straw. However, intriguingly the addition of CBEL during the hydrolysis of wheat straw actually potentiates the action of TvXynB variant lacking a CBM1. This suggests that the potentiating effect of CBM1-1 might not require the formation of a covalent linkage to TvXynB. </AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Martinez</LastName>
<ForeName>Thomas</ForeName>
<Initials>T</Initials>
<AffiliationInfo><Affiliation>Université Toulouse 3, UPS, Laboratoire de Recherche en Sciences Végétales, 24 chemin de Borde Rouge, BP42617, Auzeville, F-31326, Castanet-Tolosan, France; CNRS, Laboratoire de Recherche en Sciences Végétales, 24 chemin de Borde Rouge, BP42617, Auzeville, F-31326, Castanet-Tolosan, France; Université de Toulouse; INSA, UPS, INP, LISBP, 135 Avenue de Rangueil, F-31077 Toulouse, France; CNRS, UMR5504, F-31400 Toulouse, France; INRA, UMR792 Ingénierie des Systèmes Biologiques et des Procédés, F-31400 Toulouse, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Texier</LastName>
<ForeName>Hélène</ForeName>
<Initials>H</Initials>
<AffiliationInfo><Affiliation>Université de Toulouse; INSA, UPS, INP, LISBP, 135 Avenue de Rangueil, F-31077 Toulouse, France; CNRS, UMR5504, F-31400 Toulouse, France; INRA, UMR792 Ingénierie des Systèmes Biologiques et des Procédés, F-31400 Toulouse, France; Cinabio ADISSEO France SAS, Hall Gilbert Durand 3, 135 avenue de Rangueil, 31077 Toulouse, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Nahoum</LastName>
<ForeName>Virginie</ForeName>
<Initials>V</Initials>
<AffiliationInfo><Affiliation>Université de Toulouse, UPS, IPBS, Toulouse, F-31077, France; Institut de Pharmacologie et de Biologie Structurale (IPBS), Centre National de la Recherche Scientifique (CNRS), Toulouse, F-31077, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Lafitte</LastName>
<ForeName>Claude</ForeName>
<Initials>C</Initials>
<AffiliationInfo><Affiliation>Université Toulouse 3, UPS, Laboratoire de Recherche en Sciences Végétales, 24 chemin de Borde Rouge, BP42617, Auzeville, F-31326, Castanet-Tolosan, France; CNRS, Laboratoire de Recherche en Sciences Végétales, 24 chemin de Borde Rouge, BP42617, Auzeville, F-31326, Castanet-Tolosan, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Cioci</LastName>
<ForeName>Gianluca</ForeName>
<Initials>G</Initials>
<AffiliationInfo><Affiliation>Université de Toulouse; INSA, UPS, INP, LISBP, 135 Avenue de Rangueil, F-31077 Toulouse, France; CNRS, UMR5504, F-31400 Toulouse, France; INRA, UMR792 Ingénierie des Systèmes Biologiques et des Procédés, F-31400 Toulouse, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Heux</LastName>
<ForeName>Laurent</ForeName>
<Initials>L</Initials>
<AffiliationInfo><Affiliation>CERMAV, CNRS, Grenoble, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Dumas</LastName>
<ForeName>Bernard</ForeName>
<Initials>B</Initials>
<AffiliationInfo><Affiliation>Université Toulouse 3, UPS, Laboratoire de Recherche en Sciences Végétales, 24 chemin de Borde Rouge, BP42617, Auzeville, F-31326, Castanet-Tolosan, France; CNRS, Laboratoire de Recherche en Sciences Végétales, 24 chemin de Borde Rouge, BP42617, Auzeville, F-31326, Castanet-Tolosan, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>O'Donohue</LastName>
<ForeName>Michael</ForeName>
<Initials>M</Initials>
<AffiliationInfo><Affiliation>Université de Toulouse; INSA, UPS, INP, LISBP, 135 Avenue de Rangueil, F-31077 Toulouse, France; CNRS, UMR5504, F-31400 Toulouse, France; INRA, UMR792 Ingénierie des Systèmes Biologiques et des Procédés, F-31400 Toulouse, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Gaulin</LastName>
<ForeName>Elodie</ForeName>
<Initials>E</Initials>
<AffiliationInfo><Affiliation>Université Toulouse 3, UPS, Laboratoire de Recherche en Sciences Végétales, 24 chemin de Borde Rouge, BP42617, Auzeville, F-31326, Castanet-Tolosan, France; CNRS, Laboratoire de Recherche en Sciences Végétales, 24 chemin de Borde Rouge, BP42617, Auzeville, F-31326, Castanet-Tolosan, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Dumon</LastName>
<ForeName>Claire</ForeName>
<Initials>C</Initials>
<AffiliationInfo><Affiliation>Université de Toulouse; INSA, UPS, INP, LISBP, 135 Avenue de Rangueil, F-31077 Toulouse, France; CNRS, UMR5504, F-31400 Toulouse, France; INRA, UMR792 Ingénierie des Systèmes Biologiques et des Procédés, F-31400 Toulouse, France.</Affiliation>
</AffiliationInfo>
</Author>
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<Language>eng</Language>
<PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2015</Year>
<Month>09</Month>
<Day>21</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>United States</Country>
<MedlineTA>PLoS One</MedlineTA>
<NlmUniqueID>101285081</NlmUniqueID>
<ISSNLinking>1932-6203</ISSNLinking>
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<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D006023">Glycoproteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D037102">Lectins</NameOfSubstance>
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<Chemical><RegistryNumber>9004-34-6</RegistryNumber>
<NameOfSubstance UI="D002482">Cellulose</NameOfSubstance>
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<Chemical><RegistryNumber>EC 3.2.1.8</RegistryNumber>
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<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
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<MeshHeading><DescriptorName UI="D043364" MajorTopicYN="N">Endo-1,4-beta Xylanases</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006023" MajorTopicYN="N">Glycoproteins</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006868" MajorTopicYN="N">Hydrolysis</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D037102" MajorTopicYN="N">Lectins</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010838" MajorTopicYN="N">Phytophthora</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D017434" MajorTopicYN="N">Protein Structure, Tertiary</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D032901" MajorTopicYN="N">Talaromyces</DescriptorName>
<QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D014908" MajorTopicYN="N">Triticum</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
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Probing the Functions of Carbohydrate Binding Modules in the CBEL Protein from the Oomycete Phytophthora parasitica.

Probing the Functions of Carbohydrate Binding Modules in the CBEL Protein from the Oomycete Phytophthora parasitica.

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