Active-site mapping of a Populus xyloglucan endo-transglycosylase with a library of xylogluco-oligosaccharides.
Identifieur interne : 003A02 ( Main/Exploration ); précédent : 003A01; suivant : 003A03Active-site mapping of a Populus xyloglucan endo-transglycosylase with a library of xylogluco-oligosaccharides.
Auteurs : Marc Saura-Valls [Espagne] ; Régis Fauré ; Harry Brumer ; Tuula T. Teeri ; Sylvain Cottaz ; Hugues Driguez ; Antoni PlanasSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 2008.
Descripteurs français
- KwdFr :
- MESH :
- enzymologie : Populus.
- métabolisme : Bibliothèques de petites molécules, Glycosyltransferase, Naphtalènes, Oligosaccharides.
- Cinétique, Facteurs temps, Sites de fixation, Électrophorèse capillaire.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Glycosyltransferases, Naphthalenes, Oligosaccharides, Small Molecule Libraries.
- enzymology : Populus.
- Binding Sites, Electrophoresis, Capillary, Kinetics, Time Factors.
Abstract
Restructuring the network of xyloglucan (XG) and cellulose during plant cell wall morphogenesis involves the action of xyloglucan endo-transglycosylases (XETs). They cleave the XG chains and transfer the enzyme-bound XG fragment to another XG molecule, thus allowing transient loosening of the cell wall and also incorporation of nascent XG during expansion. The substrate specificity of a XET from Populus (PttXET16-34) has been analyzed by mapping the enzyme binding site with a library of xylogluco-oligosaccharides as donor substrates using a labeled heptasaccharide as acceptor. The extended binding cleft of the enzyme is composed of four negative and three positive subsites (with the catalytic residues between subsites -1 and +1). Donor binding is dominated by the higher affinity of the XXXG moiety (G=Glcbeta(1-->4) and X=Xylalpha(1-->6)Glcbeta(1-->4)) of the substrate for positive subsites, whereas negative subsites have a more relaxed specificity, able to bind (and transfer to the acceptor) a cello-oligosaccharyl moiety of hybrid substrates such as GGGGXXXG. Subsite mapping with k(cat)/K(m) values for the donor substrates showed that a GG-unit on negative and -XXG on positive subsites are the minimal requirements for activity. Subsites -2 and -3 (for backbone Glc residues) and +2' (for Xyl substitution at Glc in subsite +2) have the largest contribution to transition state stabilization. GalGXXXGXXXG (Gal=Galbeta(1-->4)) is the best donor substrate with a "blocked" nonreducing end that prevents polymerization reactions and yields a single transglycosylation product. Its kinetics have unambiguously established that the enzyme operates by a ping-pong mechanism with competitive inhibition by the acceptor.
DOI: 10.1074/jbc.M803058200
PubMed: 18511421
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Active-site mapping of a Populus xyloglucan endo-transglycosylase with a library of xylogluco-oligosaccharides.</title><author><name sortKey="Saura Valls, Marc" sort="Saura Valls, Marc" uniqKey="Saura Valls M" first="Marc" last="Saura-Valls">Marc Saura-Valls</name><affiliation wicri:level="2"><nlm:affiliation>Laboratory of Biochemistry, Institut Químic de Sarrià, Universitat Ramon Llull, 08017 Barcelona, Spain.</nlm:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>Laboratory of Biochemistry, Institut Químic de Sarrià, Universitat Ramon Llull, 08017 Barcelona</wicri:regionArea><placeName><region nuts="2" type="communauté">Catalogne</region></placeName></affiliation></author><author><name sortKey="Faure, Regis" sort="Faure, Regis" uniqKey="Faure R" first="Régis" last="Fauré">Régis Fauré</name></author><author><name sortKey="Brumer, Harry" sort="Brumer, Harry" uniqKey="Brumer H" first="Harry" last="Brumer">Harry Brumer</name></author><author><name sortKey="Teeri, Tuula T" sort="Teeri, Tuula T" uniqKey="Teeri T" first="Tuula T" last="Teeri">Tuula T. Teeri</name></author><author><name sortKey="Cottaz, Sylvain" sort="Cottaz, Sylvain" uniqKey="Cottaz S" first="Sylvain" last="Cottaz">Sylvain Cottaz</name></author><author><name sortKey="Driguez, Hugues" sort="Driguez, Hugues" uniqKey="Driguez H" first="Hugues" last="Driguez">Hugues Driguez</name></author><author><name sortKey="Planas, Antoni" sort="Planas, Antoni" uniqKey="Planas A" first="Antoni" last="Planas">Antoni Planas</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2008">2008</date><idno type="RBID">pubmed:18511421</idno><idno type="pmid">18511421</idno><idno type="doi">10.1074/jbc.M803058200</idno><idno type="wicri:Area/Main/Corpus">003877</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">003877</idno><idno type="wicri:Area/Main/Curation">003877</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">003877</idno><idno type="wicri:Area/Main/Exploration">003877</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Active-site mapping of a Populus xyloglucan endo-transglycosylase with a library of xylogluco-oligosaccharides.</title><author><name sortKey="Saura Valls, Marc" sort="Saura Valls, Marc" uniqKey="Saura Valls M" first="Marc" last="Saura-Valls">Marc Saura-Valls</name><affiliation wicri:level="2"><nlm:affiliation>Laboratory of Biochemistry, Institut Químic de Sarrià, Universitat Ramon Llull, 08017 Barcelona, Spain.</nlm:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>Laboratory of Biochemistry, Institut Químic de Sarrià, Universitat Ramon Llull, 08017 Barcelona</wicri:regionArea><placeName><region nuts="2" type="communauté">Catalogne</region></placeName></affiliation></author><author><name sortKey="Faure, Regis" sort="Faure, Regis" uniqKey="Faure R" first="Régis" last="Fauré">Régis Fauré</name></author><author><name sortKey="Brumer, Harry" sort="Brumer, Harry" uniqKey="Brumer H" first="Harry" last="Brumer">Harry Brumer</name></author><author><name sortKey="Teeri, Tuula T" sort="Teeri, Tuula T" uniqKey="Teeri T" first="Tuula T" last="Teeri">Tuula T. Teeri</name></author><author><name sortKey="Cottaz, Sylvain" sort="Cottaz, Sylvain" uniqKey="Cottaz S" first="Sylvain" last="Cottaz">Sylvain Cottaz</name></author><author><name sortKey="Driguez, Hugues" sort="Driguez, Hugues" uniqKey="Driguez H" first="Hugues" last="Driguez">Hugues Driguez</name></author><author><name sortKey="Planas, Antoni" sort="Planas, Antoni" uniqKey="Planas A" first="Antoni" last="Planas">Antoni Planas</name></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="ISSN">0021-9258</idno><imprint><date when="2008" type="published">2008</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Binding Sites (MeSH)</term><term>Electrophoresis, Capillary (MeSH)</term><term>Glycosyltransferases (metabolism)</term><term>Kinetics (MeSH)</term><term>Naphthalenes (metabolism)</term><term>Oligosaccharides (metabolism)</term><term>Populus (enzymology)</term><term>Small Molecule Libraries (metabolism)</term><term>Time Factors (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Bibliothèques de petites molécules (métabolisme)</term><term>Cinétique (MeSH)</term><term>Facteurs temps (MeSH)</term><term>Glycosyltransferase (métabolisme)</term><term>Naphtalènes (métabolisme)</term><term>Oligosaccharides (métabolisme)</term><term>Populus (enzymologie)</term><term>Sites de fixation (MeSH)</term><term>Électrophorèse capillaire (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glycosyltransferases</term><term>Naphthalenes</term><term>Oligosaccharides</term><term>Small Molecule Libraries</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Populus</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Populus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Bibliothèques de petites molécules</term><term>Glycosyltransferase</term><term>Naphtalènes</term><term>Oligosaccharides</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Binding Sites</term><term>Electrophoresis, Capillary</term><term>Kinetics</term><term>Time Factors</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cinétique</term><term>Facteurs temps</term><term>Sites de fixation</term><term>Électrophorèse capillaire</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Restructuring the network of xyloglucan (XG) and cellulose during plant cell wall morphogenesis involves the action of xyloglucan endo-transglycosylases (XETs). They cleave the XG chains and transfer the enzyme-bound XG fragment to another XG molecule, thus allowing transient loosening of the cell wall and also incorporation of nascent XG during expansion. The substrate specificity of a XET from Populus (PttXET16-34) has been analyzed by mapping the enzyme binding site with a library of xylogluco-oligosaccharides as donor substrates using a labeled heptasaccharide as acceptor. The extended binding cleft of the enzyme is composed of four negative and three positive subsites (with the catalytic residues between subsites -1 and +1). Donor binding is dominated by the higher affinity of the XXXG moiety (G=Glcbeta(1-->4) and X=Xylalpha(1-->6)Glcbeta(1-->4)) of the substrate for positive subsites, whereas negative subsites have a more relaxed specificity, able to bind (and transfer to the acceptor) a cello-oligosaccharyl moiety of hybrid substrates such as GGGGXXXG. Subsite mapping with k(cat)/K(m) values for the donor substrates showed that a GG-unit on negative and -XXG on positive subsites are the minimal requirements for activity. Subsites -2 and -3 (for backbone Glc residues) and +2' (for Xyl substitution at Glc in subsite +2) have the largest contribution to transition state stabilization. GalGXXXGXXXG (Gal=Galbeta(1-->4)) is the best donor substrate with a "blocked" nonreducing end that prevents polymerization reactions and yields a single transglycosylation product. Its kinetics have unambiguously established that the enzyme operates by a ping-pong mechanism with competitive inhibition by the acceptor.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">18511421</PMID><DateCompleted><Year>2008</Year><Month>09</Month><Day>17</Day></DateCompleted><DateRevised><Year>2016</Year><Month>11</Month><Day>24</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0021-9258</ISSN><JournalIssue CitedMedium="Print"><Volume>283</Volume><Issue>32</Issue><PubDate><Year>2008</Year><Month>Aug</Month><Day>08</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Active-site mapping of a Populus xyloglucan endo-transglycosylase with a library of xylogluco-oligosaccharides.</ArticleTitle><Pagination><MedlinePgn>21853-63</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1074/jbc.M803058200</ELocationID><Abstract><AbstractText>Restructuring the network of xyloglucan (XG) and cellulose during plant cell wall morphogenesis involves the action of xyloglucan endo-transglycosylases (XETs). They cleave the XG chains and transfer the enzyme-bound XG fragment to another XG molecule, thus allowing transient loosening of the cell wall and also incorporation of nascent XG during expansion. The substrate specificity of a XET from Populus (PttXET16-34) has been analyzed by mapping the enzyme binding site with a library of xylogluco-oligosaccharides as donor substrates using a labeled heptasaccharide as acceptor. The extended binding cleft of the enzyme is composed of four negative and three positive subsites (with the catalytic residues between subsites -1 and +1). Donor binding is dominated by the higher affinity of the XXXG moiety (G=Glcbeta(1-->4) and X=Xylalpha(1-->6)Glcbeta(1-->4)) of the substrate for positive subsites, whereas negative subsites have a more relaxed specificity, able to bind (and transfer to the acceptor) a cello-oligosaccharyl moiety of hybrid substrates such as GGGGXXXG. Subsite mapping with k(cat)/K(m) values for the donor substrates showed that a GG-unit on negative and -XXG on positive subsites are the minimal requirements for activity. Subsites -2 and -3 (for backbone Glc residues) and +2' (for Xyl substitution at Glc in subsite +2) have the largest contribution to transition state stabilization. GalGXXXGXXXG (Gal=Galbeta(1-->4)) is the best donor substrate with a "blocked" nonreducing end that prevents polymerization reactions and yields a single transglycosylation product. Its kinetics have unambiguously established that the enzyme operates by a ping-pong mechanism with competitive inhibition by the acceptor.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Saura-Valls</LastName><ForeName>Marc</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Laboratory of Biochemistry, Institut Químic de Sarrià, Universitat Ramon Llull, 08017 Barcelona, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Fauré</LastName><ForeName>Régis</ForeName><Initials>R</Initials></Author><Author ValidYN="Y"><LastName>Brumer</LastName><ForeName>Harry</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Teeri</LastName><ForeName>Tuula T</ForeName><Initials>TT</Initials></Author><Author ValidYN="Y"><LastName>Cottaz</LastName><ForeName>Sylvain</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Driguez</LastName><ForeName>Hugues</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Planas</LastName><ForeName>Antoni</ForeName><Initials>A</Initials></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>2008</Year><Month>05</Month><Day>28</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Biol Chem</MedlineTA><NlmUniqueID>2985121R</NlmUniqueID><ISSNLinking>0021-9258</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D009281">Naphthalenes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D009844">Oligosaccharides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054852">Small Molecule Libraries</NameOfSubstance></Chemical><Chemical><RegistryNumber>D33V8NB7KB</RegistryNumber><NameOfSubstance UI="C046465">8-amino-1,3,6-naphthalenetrisulfonic acid</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.4.-</RegistryNumber><NameOfSubstance UI="D016695">Glycosyltransferases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.4.1.-</RegistryNumber><NameOfSubstance UI="C073693">xyloglucan endotransglycosylase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019075" MajorTopicYN="N">Electrophoresis, Capillary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016695" MajorTopicYN="N">Glycosyltransferases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009281" MajorTopicYN="N">Naphthalenes</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009844" MajorTopicYN="N">Oligosaccharides</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D032107" MajorTopicYN="N">Populus</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054852" MajorTopicYN="N">Small Molecule Libraries</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013997" MajorTopicYN="N">Time Factors</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2008</Year><Month>5</Month><Day>31</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2008</Year><Month>9</Month><Day>18</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2008</Year><Month>5</Month><Day>31</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">18511421</ArticleId><ArticleId IdType="pii">M803058200</ArticleId><ArticleId IdType="doi">10.1074/jbc.M803058200</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Espagne</li></country><region><li>Catalogne</li></region></list><tree><noCountry><name sortKey="Brumer, Harry" sort="Brumer, Harry" uniqKey="Brumer H" first="Harry" last="Brumer">Harry Brumer</name><name sortKey="Cottaz, Sylvain" sort="Cottaz, Sylvain" uniqKey="Cottaz S" first="Sylvain" last="Cottaz">Sylvain Cottaz</name><name sortKey="Driguez, Hugues" sort="Driguez, Hugues" uniqKey="Driguez H" first="Hugues" last="Driguez">Hugues Driguez</name><name sortKey="Faure, Regis" sort="Faure, Regis" uniqKey="Faure R" first="Régis" last="Fauré">Régis Fauré</name><name sortKey="Planas, Antoni" sort="Planas, Antoni" uniqKey="Planas A" first="Antoni" last="Planas">Antoni Planas</name><name sortKey="Teeri, Tuula T" sort="Teeri, Tuula T" uniqKey="Teeri T" first="Tuula T" last="Teeri">Tuula T. Teeri</name></noCountry><country name="Espagne"><region name="Catalogne"><name sortKey="Saura Valls, Marc" sort="Saura Valls, Marc" uniqKey="Saura Valls M" first="Marc" last="Saura-Valls">Marc Saura-Valls</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Bois/explor/PoplarV1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 003A02 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 003A02 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Bois
|area= PoplarV1
|flux= Main
|étape= Exploration
|type= RBID
|clé= pubmed:18511421
|texte= Active-site mapping of a Populus xyloglucan endo-transglycosylase with a library of xylogluco-oligosaccharides.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:18511421" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a PoplarV1
| This area was generated with Dilib version V0.6.37. |  |