Substrate specificity of plant and fungi pectin methylesterases: Identification of novel inhibitors of PMEs.
Identifieur interne : 000115 ( PubMed/Corpus ); précédent : 000114; suivant : 000116Substrate specificity of plant and fungi pectin methylesterases: Identification of novel inhibitors of PMEs.
Auteurs : Mélanie L'Enfant ; Jean-Marc Domon ; Catherine Rayon ; Thierry Desnos ; Marie-Christine Ralet ; Estelle Bonnin ; Jérôme Pelloux ; Corinne Pau-RoblotSource :
- International journal of biological macromolecules [ 1879-0003 ] ; 2015.
English descriptors
- KwdEn :
- Amino Acid Sequence, Carboxylic Ester Hydrolases (antagonists & inhibitors), Carboxylic Ester Hydrolases (chemistry), Carboxylic Ester Hydrolases (isolation & purification), Carboxylic Ester Hydrolases (metabolism), Drug Discovery, Drug Evaluation, Preclinical, Enzyme Activation (drug effects), Enzyme Inhibitors (chemistry), Enzyme Inhibitors (pharmacology), Fungi (enzymology), Hydrogen-Ion Concentration, Molecular Sequence Data, Plants (enzymology), Polyphenols (pharmacology), Sequence Alignment, Small Molecule Libraries, Substrate Specificity.
- MESH :
- chemical , antagonists & inhibitors : Carboxylic Ester Hydrolases.
- chemical , chemistry : Carboxylic Ester Hydrolases, Enzyme Inhibitors.
- chemical , isolation & purification : Carboxylic Ester Hydrolases.
- chemical , metabolism : Carboxylic Ester Hydrolases.
- drug effects : Enzyme Activation.
- enzymology : Fungi, Plants.
- chemical , pharmacology : Enzyme Inhibitors, Polyphenols.
- Amino Acid Sequence, Drug Discovery, Drug Evaluation, Preclinical, Hydrogen-Ion Concentration, Molecular Sequence Data, Sequence Alignment, Small Molecule Libraries, Substrate Specificity.
Abstract
Pectin methylesterases (PMEs) play a central role in pectin remodeling during plant development. They are also present in phytopathogens such as bacteria and fungi. We investigated the substrate specificity and pH dependence of plant and fungi PMEs using tailor-made pectic substrates. For this purpose, we used two plant PMEs (from orange peel: Citrus sinensis and from Arabidopsis thaliana) and one fungal PME (from Botrytis cinerea). We showed that plant and fungi PMEs differed in their substrate specificity and pH dependence, and that there were some differences between plant PMEs. We further investigated the inhibition of these enzyme activities using characterized polyphenols such as catechins and tannic acid. We showed that PMEs differed in their sensitivity to chemical compounds. In particular, fungal PME was not sensitive to inhibition. Finally, we screened for novel chemical inhibitors of PMEs using a chemical library of ∼3600 compounds. We identified a hundred new inhibitors of plant PMEs, but none had an effect on the fungal enzyme. This study sheds new light on the specificity of pectin methylesterases and provides new tools to modulate their activity.
DOI: 10.1016/j.ijbiomac.2015.08.066
PubMed: 26342461
Links to Exploration step
pubmed:26342461Le document en format XML
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Electronic address: corinne.pau-roblot@u-picardie.fr.</nlm:affiliation></affiliation></author></analytic><series><title level="j">International journal of biological macromolecules</title><idno type="eISSN">1879-0003</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</term><term>Carboxylic Ester Hydrolases (antagonists & inhibitors)</term><term>Carboxylic Ester Hydrolases (chemistry)</term><term>Carboxylic Ester Hydrolases (isolation & purification)</term><term>Carboxylic Ester Hydrolases (metabolism)</term><term>Drug Discovery</term><term>Drug Evaluation, Preclinical</term><term>Enzyme Activation (drug effects)</term><term>Enzyme Inhibitors (chemistry)</term><term>Enzyme Inhibitors (pharmacology)</term><term>Fungi (enzymology)</term><term>Hydrogen-Ion Concentration</term><term>Molecular Sequence Data</term><term>Plants (enzymology)</term><term>Polyphenols (pharmacology)</term><term>Sequence Alignment</term><term>Small Molecule Libraries</term><term>Substrate Specificity</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Carboxylic Ester Hydrolases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Carboxylic Ester Hydrolases</term><term>Enzyme Inhibitors</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Carboxylic Ester Hydrolases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Carboxylic Ester Hydrolases</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Enzyme Activation</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Fungi</term><term>Plants</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Enzyme Inhibitors</term><term>Polyphenols</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Drug Discovery</term><term>Drug Evaluation, Preclinical</term><term>Hydrogen-Ion Concentration</term><term>Molecular Sequence Data</term><term>Sequence Alignment</term><term>Small Molecule Libraries</term><term>Substrate Specificity</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Pectin methylesterases (PMEs) play a central role in pectin remodeling during plant development. They are also present in phytopathogens such as bacteria and fungi. We investigated the substrate specificity and pH dependence of plant and fungi PMEs using tailor-made pectic substrates. For this purpose, we used two plant PMEs (from orange peel: Citrus sinensis and from Arabidopsis thaliana) and one fungal PME (from Botrytis cinerea). We showed that plant and fungi PMEs differed in their substrate specificity and pH dependence, and that there were some differences between plant PMEs. We further investigated the inhibition of these enzyme activities using characterized polyphenols such as catechins and tannic acid. We showed that PMEs differed in their sensitivity to chemical compounds. In particular, fungal PME was not sensitive to inhibition. Finally, we screened for novel chemical inhibitors of PMEs using a chemical library of ∼3600 compounds. We identified a hundred new inhibitors of plant PMEs, but none had an effect on the fungal enzyme. This study sheds new light on the specificity of pectin methylesterases and provides new tools to modulate their activity.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">26342461</PMID><DateCreated><Year>2015</Year><Month>12</Month><Day>22</Day></DateCreated><DateCompleted><Year>2016</Year><Month>10</Month><Day>13</Day></DateCompleted><DateRevised><Year>2016</Year><Month>10</Month><Day>14</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1879-0003</ISSN><JournalIssue CitedMedium="Internet"><Volume>81</Volume><PubDate><Year>2015</Year><Month>Nov</Month></PubDate></JournalIssue><Title>International journal of biological macromolecules</Title><ISOAbbreviation>Int. J. Biol. Macromol.</ISOAbbreviation></Journal><ArticleTitle>Substrate specificity of plant and fungi pectin methylesterases: Identification of novel inhibitors of PMEs.</ArticleTitle><Pagination><MedlinePgn>681-91</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.ijbiomac.2015.08.066</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0141-8130(15)00613-3</ELocationID><Abstract><AbstractText>Pectin methylesterases (PMEs) play a central role in pectin remodeling during plant development. They are also present in phytopathogens such as bacteria and fungi. We investigated the substrate specificity and pH dependence of plant and fungi PMEs using tailor-made pectic substrates. For this purpose, we used two plant PMEs (from orange peel: Citrus sinensis and from Arabidopsis thaliana) and one fungal PME (from Botrytis cinerea). We showed that plant and fungi PMEs differed in their substrate specificity and pH dependence, and that there were some differences between plant PMEs. We further investigated the inhibition of these enzyme activities using characterized polyphenols such as catechins and tannic acid. We showed that PMEs differed in their sensitivity to chemical compounds. In particular, fungal PME was not sensitive to inhibition. Finally, we screened for novel chemical inhibitors of PMEs using a chemical library of ∼3600 compounds. We identified a hundred new inhibitors of plant PMEs, but none had an effect on the fungal enzyme. This study sheds new light on the specificity of pectin methylesterases and provides new tools to modulate their activity.</AbstractText><CopyrightInformation>Copyright © 2015 Elsevier B.V. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>L'Enfant</LastName><ForeName>Mélanie</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Unité de Biologie des Plantes et Innovation, EA3900, Université de Picardie Jules Verne, 33 rue Saint Leu, 80039 Amiens Cedex, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Domon</LastName><ForeName>Jean-Marc</ForeName><Initials>JM</Initials><AffiliationInfo><Affiliation>Unité de Biologie des Plantes et Innovation, EA3900, Université de Picardie Jules Verne, 33 rue Saint Leu, 80039 Amiens Cedex, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Rayon</LastName><ForeName>Catherine</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Unité de Biologie des Plantes et Innovation, EA3900, Université de Picardie Jules Verne, 33 rue Saint Leu, 80039 Amiens Cedex, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Desnos</LastName><ForeName>Thierry</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>CEA Cadarache, SBVME/LBDP, Bât 178, 13108 Saint-Paul-les-Durance Cedex, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ralet</LastName><ForeName>Marie-Christine</ForeName><Initials>MC</Initials><AffiliationInfo><Affiliation>INRA, UR 1268, Biopolymères, Interactions, Assemblages, BP 71627, 44316 Nantes Cedex 03, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Bonnin</LastName><ForeName>Estelle</ForeName><Initials>E</Initials><AffiliationInfo><Affiliation>INRA, UR 1268, Biopolymères, Interactions, Assemblages, BP 71627, 44316 Nantes Cedex 03, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Pelloux</LastName><ForeName>Jérôme</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Unité de Biologie des Plantes et Innovation, EA3900, Université de Picardie Jules Verne, 33 rue Saint Leu, 80039 Amiens Cedex, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Pau-Roblot</LastName><ForeName>Corinne</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Unité de Biologie des Plantes et Innovation, EA3900, Université de Picardie Jules Verne, 33 rue Saint Leu, 80039 Amiens Cedex, France. Electronic address: corinne.pau-roblot@u-picardie.fr.</Affiliation></AffiliationInfo></Author></AuthorList><Language>ENG</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2015</Year><Month>Sep</Month><Day>03</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Int J Biol Macromol</MedlineTA><NlmUniqueID>7909578</NlmUniqueID><ISSNLinking>0141-8130</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004791">Enzyme Inhibitors</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D059808">Polyphenols</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054852">Small Molecule Libraries</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.1.1.-</RegistryNumber><NameOfSubstance UI="D002265">Carboxylic Ester Hydrolases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.1.1.11</RegistryNumber><NameOfSubstance UI="C022323">pectinesterase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002265" MajorTopicYN="N">Carboxylic Ester Hydrolases</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D055808" MajorTopicYN="N">Drug Discovery</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004353" MajorTopicYN="N">Drug Evaluation, Preclinical</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004789" MajorTopicYN="N">Enzyme Activation</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004791" MajorTopicYN="N">Enzyme Inhibitors</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005658" MajorTopicYN="N">Fungi</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006863" MajorTopicYN="N">Hydrogen-Ion Concentration</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010944" MajorTopicYN="N">Plants</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D059808" MajorTopicYN="N">Polyphenols</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016415" MajorTopicYN="N">Sequence Alignment</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054852" MajorTopicYN="N">Small Molecule Libraries</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Catechins</Keyword><Keyword MajorTopicYN="N">Chemical inhibitors</Keyword><Keyword MajorTopicYN="N">Chemical library</Keyword><Keyword MajorTopicYN="N">EGCG</Keyword><Keyword MajorTopicYN="N">Pectin methylesterase</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2015</Year><Month>6</Month><Day>10</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2015</Year><Month>8</Month><Day>27</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2015</Year><Month>8</Month><Day>28</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2015</Year><Month>9</Month><Day>7</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2015</Year><Month>9</Month><Day>8</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2016</Year><Month>10</Month><Day>14</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">26342461</ArticleId><ArticleId IdType="pii">S0141-8130(15)00613-3</ArticleId><ArticleId IdType="doi">10.1016/j.ijbiomac.2015.08.066</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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