Glycosynthase activity of hybrid aspen xyloglucan endo-transglycosylase PttXET16-34 nucleophile mutants.
Identifieur interne : 003B70 ( Main/Exploration ); précédent : 003B69; suivant : 003B71Glycosynthase activity of hybrid aspen xyloglucan endo-transglycosylase PttXET16-34 nucleophile mutants.
Auteurs : Kathleen Piens [Suède] ; Anna-Maria Henriksson ; Fredrika Gullfot ; Marie Lopez ; Régis Fauré ; Farid M. Ibatullin ; Tuula T. Teeri ; Hugues Driguez ; Harry BrumerSource :
- Organic & biomolecular chemistry [ 1477-0520 ] ; 2007.
Descripteurs français
- KwdFr :
- Catalyse (MeSH), Cinétique (MeSH), Fluor (composition chimique), Glycosidases (métabolisme), Glycosyltransferase (génétique), Glycosyltransferase (métabolisme), Hydrolyse (MeSH), Mutagenèse dirigée (MeSH), Oligosaccharides (métabolisme), Populus (enzymologie), Sites de fixation (MeSH), Spectrométrie de masse ESI (MeSH), Spécificité du substrat (MeSH), Stéréoisomérie (MeSH).
- MESH :
- composition chimique : Fluor.
- enzymologie : Populus.
- génétique : Glycosyltransferase.
- métabolisme : Glycosidases, Glycosyltransferase, Oligosaccharides.
- Catalyse, Cinétique, Hydrolyse, Mutagenèse dirigée, Sites de fixation, Spectrométrie de masse ESI, Spécificité du substrat, Stéréoisomérie.
English descriptors
- KwdEn :
- Binding Sites (MeSH), Catalysis (MeSH), Fluorine (chemistry), Glycoside Hydrolases (metabolism), Glycosyltransferases (genetics), Glycosyltransferases (metabolism), Hydrolysis (MeSH), Kinetics (MeSH), Mutagenesis, Site-Directed (MeSH), Oligosaccharides (metabolism), Populus (enzymology), Spectrometry, Mass, Electrospray Ionization (MeSH), Stereoisomerism (MeSH), Substrate Specificity (MeSH).
- MESH :
- chemical , chemistry : Fluorine.
- chemical , genetics : Glycosyltransferases.
- chemical , metabolism : Glycoside Hydrolases, Glycosyltransferases, Oligosaccharides.
- enzymology : Populus.
- Binding Sites, Catalysis, Hydrolysis, Kinetics, Mutagenesis, Site-Directed, Spectrometry, Mass, Electrospray Ionization, Stereoisomerism, Substrate Specificity.
Abstract
Glycosynthases are active-site mutants of glycoside hydrolases that catalyse glycosyl transfer using suitable activated donor substrates without competing product hydrolysis (S. M. Hancock, M. D. Vaughan and S. G. Withers, Curr. Opin. Chem. Biol., 2006, 10, 509-519). Site-directed mutagenesis of the catalytic nucleophile, Glu-85, of a Populus tremula x tremuloides xyloglucan endo-transglycosylase (PttXET16-34, EC 2.4.1.207) into alanine, glycine, and serine yielded enzymes with glycosynthase activity. Product analysis indicated that PttXET16-34 E85A in particular was able to catalyse regio- and stereospecific homo- and hetero-condensations of alpha-xylogluco-oligosaccharyl fluoride donors XXXGalphaF and XLLGalphaF to produce xyloglucans with regular sidechain substitution patterns. This substrate promiscuity contrasts that of the Humicola insolens Cel7B E197A glycosynthase, which was not able to polymerise the di-galactosylated substrate XLLGalphaF. The production of the PttXET16-34 E85A xyloglucosynthase thus expands the repertoire of glycosynthases to include those capable of synthesising structurally homogenenous xyloglucans for applications.
DOI: 10.1039/b714570e
PubMed: 18043802
Affiliations:
Links toward previous steps (curation, corpus...)
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Ibatullin</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="Driguez, Hugues" sort="Driguez, Hugues" uniqKey="Driguez H" first="Hugues" last="Driguez">Hugues Driguez</name></author><author><name sortKey="Brumer, Harry" sort="Brumer, Harry" uniqKey="Brumer H" first="Harry" last="Brumer">Harry Brumer</name></author></analytic><series><title level="j">Organic & biomolecular chemistry</title><idno type="ISSN">1477-0520</idno><imprint><date when="2007" type="published">2007</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Binding Sites (MeSH)</term><term>Catalysis (MeSH)</term><term>Fluorine (chemistry)</term><term>Glycoside Hydrolases (metabolism)</term><term>Glycosyltransferases (genetics)</term><term>Glycosyltransferases (metabolism)</term><term>Hydrolysis (MeSH)</term><term>Kinetics (MeSH)</term><term>Mutagenesis, Site-Directed (MeSH)</term><term>Oligosaccharides (metabolism)</term><term>Populus (enzymology)</term><term>Spectrometry, Mass, Electrospray Ionization (MeSH)</term><term>Stereoisomerism (MeSH)</term><term>Substrate Specificity (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Catalyse (MeSH)</term><term>Cinétique (MeSH)</term><term>Fluor (composition chimique)</term><term>Glycosidases (métabolisme)</term><term>Glycosyltransferase (génétique)</term><term>Glycosyltransferase (métabolisme)</term><term>Hydrolyse (MeSH)</term><term>Mutagenèse dirigée (MeSH)</term><term>Oligosaccharides (métabolisme)</term><term>Populus (enzymologie)</term><term>Sites de fixation (MeSH)</term><term>Spectrométrie de masse ESI (MeSH)</term><term>Spécificité du substrat (MeSH)</term><term>Stéréoisomérie (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Fluorine</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Glycosyltransferases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glycoside Hydrolases</term><term>Glycosyltransferases</term><term>Oligosaccharides</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Fluor</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="génétique" xml:lang="fr"><term>Glycosyltransferase</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glycosidases</term><term>Glycosyltransferase</term><term>Oligosaccharides</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Binding Sites</term><term>Catalysis</term><term>Hydrolysis</term><term>Kinetics</term><term>Mutagenesis, Site-Directed</term><term>Spectrometry, Mass, Electrospray Ionization</term><term>Stereoisomerism</term><term>Substrate Specificity</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Catalyse</term><term>Cinétique</term><term>Hydrolyse</term><term>Mutagenèse dirigée</term><term>Sites de fixation</term><term>Spectrométrie de masse ESI</term><term>Spécificité du substrat</term><term>Stéréoisomérie</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Glycosynthases are active-site mutants of glycoside hydrolases that catalyse glycosyl transfer using suitable activated donor substrates without competing product hydrolysis (S. M. Hancock, M. D. Vaughan and S. G. Withers, Curr. Opin. Chem. Biol., 2006, 10, 509-519). Site-directed mutagenesis of the catalytic nucleophile, Glu-85, of a Populus tremula x tremuloides xyloglucan endo-transglycosylase (PttXET16-34, EC 2.4.1.207) into alanine, glycine, and serine yielded enzymes with glycosynthase activity. Product analysis indicated that PttXET16-34 E85A in particular was able to catalyse regio- and stereospecific homo- and hetero-condensations of alpha-xylogluco-oligosaccharyl fluoride donors XXXGalphaF and XLLGalphaF to produce xyloglucans with regular sidechain substitution patterns. This substrate promiscuity contrasts that of the Humicola insolens Cel7B E197A glycosynthase, which was not able to polymerise the di-galactosylated substrate XLLGalphaF. The production of the PttXET16-34 E85A xyloglucosynthase thus expands the repertoire of glycosynthases to include those capable of synthesising structurally homogenenous xyloglucans for applications.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">18043802</PMID><DateCompleted><Year>2008</Year><Month>03</Month><Day>18</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">1477-0520</ISSN><JournalIssue CitedMedium="Print"><Volume>5</Volume><Issue>24</Issue><PubDate><Year>2007</Year><Month>Dec</Month><Day>21</Day></PubDate></JournalIssue><Title>Organic & biomolecular chemistry</Title><ISOAbbreviation>Org Biomol Chem</ISOAbbreviation></Journal><ArticleTitle>Glycosynthase activity of hybrid aspen xyloglucan endo-transglycosylase PttXET16-34 nucleophile mutants.</ArticleTitle><Pagination><MedlinePgn>3971-8</MedlinePgn></Pagination><Abstract><AbstractText>Glycosynthases are active-site mutants of glycoside hydrolases that catalyse glycosyl transfer using suitable activated donor substrates without competing product hydrolysis (S. M. Hancock, M. D. Vaughan and S. G. Withers, Curr. Opin. Chem. Biol., 2006, 10, 509-519). Site-directed mutagenesis of the catalytic nucleophile, Glu-85, of a Populus tremula x tremuloides xyloglucan endo-transglycosylase (PttXET16-34, EC 2.4.1.207) into alanine, glycine, and serine yielded enzymes with glycosynthase activity. Product analysis indicated that PttXET16-34 E85A in particular was able to catalyse regio- and stereospecific homo- and hetero-condensations of alpha-xylogluco-oligosaccharyl fluoride donors XXXGalphaF and XLLGalphaF to produce xyloglucans with regular sidechain substitution patterns. This substrate promiscuity contrasts that of the Humicola insolens Cel7B E197A glycosynthase, which was not able to polymerise the di-galactosylated substrate XLLGalphaF. The production of the PttXET16-34 E85A xyloglucosynthase thus expands the repertoire of glycosynthases to include those capable of synthesising structurally homogenenous xyloglucans for applications.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Piens</LastName><ForeName>Kathleen</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>School of Biotechnology, Royal Institute of Technology (KTH), AlbaNova University Centre, 106 91, Stockholm, Sweden.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Henriksson</LastName><ForeName>Anna-Maria</ForeName><Initials>AM</Initials></Author><Author ValidYN="Y"><LastName>Gullfot</LastName><ForeName>Fredrika</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Lopez</LastName><ForeName>Marie</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Fauré</LastName><ForeName>Régis</ForeName><Initials>R</Initials></Author><Author ValidYN="Y"><LastName>Ibatullin</LastName><ForeName>Farid M</ForeName><Initials>FM</Initials></Author><Author ValidYN="Y"><LastName>Teeri</LastName><ForeName>Tuula T</ForeName><Initials>TT</Initials></Author><Author ValidYN="Y"><LastName>Driguez</LastName><ForeName>Hugues</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Brumer</LastName><ForeName>Harry</ForeName><Initials>H</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>2007</Year><Month>10</Month><Day>22</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Org Biomol Chem</MedlineTA><NlmUniqueID>101154995</NlmUniqueID><ISSNLinking>1477-0520</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D009844">Oligosaccharides</NameOfSubstance></Chemical><Chemical><RegistryNumber>284SYP0193</RegistryNumber><NameOfSubstance UI="D005461">Fluorine</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><Chemical><RegistryNumber>EC 3.2.1.-</RegistryNumber><NameOfSubstance UI="D006026">Glycoside Hydrolases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002384" MajorTopicYN="N">Catalysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005461" MajorTopicYN="N">Fluorine</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006026" MajorTopicYN="N">Glycoside Hydrolases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016695" MajorTopicYN="N">Glycosyltransferases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006868" MajorTopicYN="N">Hydrolysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016297" MajorTopicYN="N">Mutagenesis, Site-Directed</DescriptorName></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="D021241" MajorTopicYN="N">Spectrometry, Mass, Electrospray Ionization</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013237" MajorTopicYN="N">Stereoisomerism</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2007</Year><Month>11</Month><Day>29</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2008</Year><Month>3</Month><Day>19</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2007</Year><Month>11</Month><Day>29</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">18043802</ArticleId><ArticleId IdType="doi">10.1039/b714570e</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Suède</li></country><region><li>Svealand</li></region><settlement><li>Stockholm</li></settlement></list><tree><noCountry><name sortKey="Brumer, Harry" sort="Brumer, Harry" uniqKey="Brumer H" first="Harry" last="Brumer">Harry Brumer</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="Gullfot, Fredrika" sort="Gullfot, Fredrika" uniqKey="Gullfot F" first="Fredrika" last="Gullfot">Fredrika Gullfot</name><name sortKey="Henriksson, Anna Maria" sort="Henriksson, Anna Maria" uniqKey="Henriksson A" first="Anna-Maria" last="Henriksson">Anna-Maria Henriksson</name><name sortKey="Ibatullin, Farid M" sort="Ibatullin, Farid M" uniqKey="Ibatullin F" first="Farid M" last="Ibatullin">Farid M. Ibatullin</name><name sortKey="Lopez, Marie" sort="Lopez, Marie" uniqKey="Lopez M" first="Marie" last="Lopez">Marie Lopez</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="Suède"><region name="Svealand"><name sortKey="Piens, Kathleen" sort="Piens, Kathleen" uniqKey="Piens K" first="Kathleen" last="Piens">Kathleen Piens</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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