Kinetics of substrate transglycosylation by glycoside hydrolase family 3 glucan (1-->3)-beta-glucosidase from the white-rot fungus Phanerochaete chrysosporium.
Identifieur interne : 000870 ( Main/Curation ); précédent : 000869; suivant : 000871Kinetics of substrate transglycosylation by glycoside hydrolase family 3 glucan (1-->3)-beta-glucosidase from the white-rot fungus Phanerochaete chrysosporium.
Auteurs : Rie Kawai [Japon] ; Kiyohiko Igarashi ; Motomitsu Kitaoka ; Tadashi Ishii ; Masahiro SamejimaSource :
- Carbohydrate research [ 0008-6215 ] ; 2004.
Descripteurs français
- KwdFr :
- Chromatographie sur couche mince (MeSH), Cinétique (MeSH), Diholoside (métabolisme), Glucan 1,3-beta-glucosidase (antagonistes et inhibiteurs), Glucan 1,3-beta-glucosidase (métabolisme), Glycosylation (MeSH), Oligosaccharides (MeSH), Phanerochaete (enzymologie), Spécificité du substrat (MeSH), Séquence glucidique (MeSH).
- MESH :
- antagonistes et inhibiteurs : Glucan 1,3-beta-glucosidase.
- enzymologie : Phanerochaete.
- métabolisme : Diholoside, Glucan 1,3-beta-glucosidase.
- Chromatographie sur couche mince, Cinétique, Glycosylation, Oligosaccharides, Spécificité du substrat, Séquence glucidique.
English descriptors
- KwdEn :
- Carbohydrate Sequence (MeSH), Chromatography, Thin Layer (MeSH), Disaccharides (metabolism), Glucan 1,3-beta-Glucosidase (antagonists & inhibitors), Glucan 1,3-beta-Glucosidase (metabolism), Glycosylation (MeSH), Kinetics (MeSH), Oligosaccharides (MeSH), Phanerochaete (enzymology), Substrate Specificity (MeSH).
- MESH :
- chemical , antagonists & inhibitors : Glucan 1,3-beta-Glucosidase.
- chemical , metabolism : Disaccharides, Glucan 1,3-beta-Glucosidase.
- enzymology : Phanerochaete.
- Carbohydrate Sequence, Chromatography, Thin Layer, Glycosylation, Kinetics, Oligosaccharides, Substrate Specificity.
Abstract
To elucidate the interaction between substrate inhibition and substrate transglycosylation of retaining glycoside hydrolases (GHs), a steady-state kinetic study was performed for the GH family 3 glucan (1-->3)-beta-glucosidase from the white-rot fungus Phanerochaete chrysosporium, using laminarioligosaccharides as substrates. When laminaribiose was incubated with the enzyme, a transglycosylation product was detected by thin-layer chromatography. The product was purified by size-exclusion chromatography, and was identified as a 6-O-glucosyl-laminaribiose (beta-D-Glcp-(1-->6)-beta-D-Glcp-(1-->3)-D-Glc) by 1H NMR spectroscopy and electrospray ionization mass spectrometry analysis. In steady-state kinetic studies, an apparent decrease of laminaribiose hydrolysis was observed at high concentrations of the substrate, and the plots of glucose production versus substrate concentration were thus fitted to a modified Michaelis-Menten equation including hydrolytic and transglycosylation parameters (K(m), K(m2), k(cat), k(cat2)). The rate of 6-O-glucosyl-laminaribiose production estimated by high-performance anion-exchange chromatography coincided with the theoretical rate calculated using these parameters, clearly indicating that substrate inhibition of this enzyme is fully explained by substrate transglycosylation. Moreover, when K(m), k(cat), and affinity for glucosyl-enzyme intermediates (K(m2)) were estimated for laminarioligosaccharides (DP=3-5), the K(m) value of laminaribiose was approximately 5-9 times higher than those of the other oligosaccharides (DP=3-5), whereas the K(m2) values were independent of the DP of the substrates. The kinetics of transglycosylation by the enzyme could be well interpreted in terms of the subsite affinities estimated from the hydrolytic parameters (K(m) and k(cat)), and a possible mechanism of transglycosylation is proposed.
DOI: 10.1016/j.carres.2004.09.019
PubMed: 15582611
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sortKey="Kitaoka, Motomitsu" sort="Kitaoka, Motomitsu" uniqKey="Kitaoka M" first="Motomitsu" last="Kitaoka">Motomitsu Kitaoka</name></author><author><name sortKey="Ishii, Tadashi" sort="Ishii, Tadashi" uniqKey="Ishii T" first="Tadashi" last="Ishii">Tadashi Ishii</name></author><author><name sortKey="Samejima, Masahiro" sort="Samejima, Masahiro" uniqKey="Samejima M" first="Masahiro" last="Samejima">Masahiro Samejima</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2004">2004</date><idno type="RBID">pubmed:15582611</idno><idno type="pmid">15582611</idno><idno type="doi">10.1016/j.carres.2004.09.019</idno><idno type="wicri:Area/Main/Corpus">000870</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000870</idno><idno type="wicri:Area/Main/Curation">000870</idno><idno type="wicri:explorRef" wicri:stream="Main" 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Igarashi</name></author><author><name sortKey="Kitaoka, Motomitsu" sort="Kitaoka, Motomitsu" uniqKey="Kitaoka M" first="Motomitsu" last="Kitaoka">Motomitsu Kitaoka</name></author><author><name sortKey="Ishii, Tadashi" sort="Ishii, Tadashi" uniqKey="Ishii T" first="Tadashi" last="Ishii">Tadashi Ishii</name></author><author><name sortKey="Samejima, Masahiro" sort="Samejima, Masahiro" uniqKey="Samejima M" first="Masahiro" last="Samejima">Masahiro Samejima</name></author></analytic><series><title level="j">Carbohydrate research</title><idno type="ISSN">0008-6215</idno><imprint><date when="2004" type="published">2004</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Carbohydrate Sequence (MeSH)</term><term>Chromatography, Thin Layer (MeSH)</term><term>Disaccharides (metabolism)</term><term>Glucan 1,3-beta-Glucosidase (antagonists & inhibitors)</term><term>Glucan 1,3-beta-Glucosidase (metabolism)</term><term>Glycosylation (MeSH)</term><term>Kinetics (MeSH)</term><term>Oligosaccharides (MeSH)</term><term>Phanerochaete (enzymology)</term><term>Substrate Specificity (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Chromatographie sur couche mince (MeSH)</term><term>Cinétique (MeSH)</term><term>Diholoside (métabolisme)</term><term>Glucan 1,3-beta-glucosidase (antagonistes et inhibiteurs)</term><term>Glucan 1,3-beta-glucosidase (métabolisme)</term><term>Glycosylation (MeSH)</term><term>Oligosaccharides (MeSH)</term><term>Phanerochaete (enzymologie)</term><term>Spécificité du substrat (MeSH)</term><term>Séquence glucidique (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Glucan 1,3-beta-Glucosidase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Disaccharides</term><term>Glucan 1,3-beta-Glucosidase</term></keywords><keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>Glucan 1,3-beta-glucosidase</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="métabolisme" xml:lang="fr"><term>Diholoside</term><term>Glucan 1,3-beta-glucosidase</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Carbohydrate Sequence</term><term>Chromatography, Thin Layer</term><term>Glycosylation</term><term>Kinetics</term><term>Oligosaccharides</term><term>Substrate Specificity</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Chromatographie sur couche mince</term><term>Cinétique</term><term>Glycosylation</term><term>Oligosaccharides</term><term>Spécificité du substrat</term><term>Séquence glucidique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">To elucidate the interaction between substrate inhibition and substrate transglycosylation of retaining glycoside hydrolases (GHs), a steady-state kinetic study was performed for the GH family 3 glucan (1-->3)-beta-glucosidase from the white-rot fungus Phanerochaete chrysosporium, using laminarioligosaccharides as substrates. When laminaribiose was incubated with the enzyme, a transglycosylation product was detected by thin-layer chromatography. The product was purified by size-exclusion chromatography, and was identified as a 6-O-glucosyl-laminaribiose (beta-D-Glcp-(1-->6)-beta-D-Glcp-(1-->3)-D-Glc) by 1H NMR spectroscopy and electrospray ionization mass spectrometry analysis. In steady-state kinetic studies, an apparent decrease of laminaribiose hydrolysis was observed at high concentrations of the substrate, and the plots of glucose production versus substrate concentration were thus fitted to a modified Michaelis-Menten equation including hydrolytic and transglycosylation parameters (K(m), K(m2), k(cat), k(cat2)). The rate of 6-O-glucosyl-laminaribiose production estimated by high-performance anion-exchange chromatography coincided with the theoretical rate calculated using these parameters, clearly indicating that substrate inhibition of this enzyme is fully explained by substrate transglycosylation. Moreover, when K(m), k(cat), and affinity for glucosyl-enzyme intermediates (K(m2)) were estimated for laminarioligosaccharides (DP=3-5), the K(m) value of laminaribiose was approximately 5-9 times higher than those of the other oligosaccharides (DP=3-5), whereas the K(m2) values were independent of the DP of the substrates. The kinetics of transglycosylation by the enzyme could be well interpreted in terms of the subsite affinities estimated from the hydrolytic parameters (K(m) and k(cat)), and a possible mechanism of transglycosylation is proposed.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15582611</PMID><DateCompleted><Year>2005</Year><Month>05</Month><Day>24</Day></DateCompleted><DateRevised><Year>2015</Year><Month>11</Month><Day>19</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0008-6215</ISSN><JournalIssue CitedMedium="Print"><Volume>339</Volume><Issue>18</Issue><PubDate><Year>2004</Year><Month>Dec</Month><Day>27</Day></PubDate></JournalIssue><Title>Carbohydrate research</Title><ISOAbbreviation>Carbohydr Res</ISOAbbreviation></Journal><ArticleTitle>Kinetics of substrate transglycosylation by glycoside hydrolase family 3 glucan (1-->3)-beta-glucosidase from the white-rot fungus Phanerochaete chrysosporium.</ArticleTitle><Pagination><MedlinePgn>2851-7</MedlinePgn></Pagination><Abstract><AbstractText>To elucidate the interaction between substrate inhibition and substrate transglycosylation of retaining glycoside hydrolases (GHs), a steady-state kinetic study was performed for the GH family 3 glucan (1-->3)-beta-glucosidase from the white-rot fungus Phanerochaete chrysosporium, using laminarioligosaccharides as substrates. When laminaribiose was incubated with the enzyme, a transglycosylation product was detected by thin-layer chromatography. The product was purified by size-exclusion chromatography, and was identified as a 6-O-glucosyl-laminaribiose (beta-D-Glcp-(1-->6)-beta-D-Glcp-(1-->3)-D-Glc) by 1H NMR spectroscopy and electrospray ionization mass spectrometry analysis. In steady-state kinetic studies, an apparent decrease of laminaribiose hydrolysis was observed at high concentrations of the substrate, and the plots of glucose production versus substrate concentration were thus fitted to a modified Michaelis-Menten equation including hydrolytic and transglycosylation parameters (K(m), K(m2), k(cat), k(cat2)). The rate of 6-O-glucosyl-laminaribiose production estimated by high-performance anion-exchange chromatography coincided with the theoretical rate calculated using these parameters, clearly indicating that substrate inhibition of this enzyme is fully explained by substrate transglycosylation. Moreover, when K(m), k(cat), and affinity for glucosyl-enzyme intermediates (K(m2)) were estimated for laminarioligosaccharides (DP=3-5), the K(m) value of laminaribiose was approximately 5-9 times higher than those of the other oligosaccharides (DP=3-5), whereas the K(m2) values were independent of the DP of the substrates. The kinetics of transglycosylation by the enzyme could be well interpreted in terms of the subsite affinities estimated from the hydrolytic parameters (K(m) and k(cat)), and a possible mechanism of transglycosylation is proposed.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Kawai</LastName><ForeName>Rie</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Department of Biomaterials Sciences, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Igarashi</LastName><ForeName>Kiyohiko</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Kitaoka</LastName><ForeName>Motomitsu</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Ishii</LastName><ForeName>Tadashi</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Samejima</LastName><ForeName>Masahiro</ForeName><Initials>M</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></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Carbohydr Res</MedlineTA><NlmUniqueID>0043535</NlmUniqueID><ISSNLinking>0008-6215</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004187">Disaccharides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D009844">Oligosaccharides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0WN3D69UW4</RegistryNumber><NameOfSubstance UI="C014637">laminaribiose</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.58</RegistryNumber><NameOfSubstance UI="D043326">Glucan 1,3-beta-Glucosidase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D002240" MajorTopicYN="N">Carbohydrate Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002855" MajorTopicYN="N">Chromatography, Thin Layer</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004187" MajorTopicYN="N">Disaccharides</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D043326" MajorTopicYN="N">Glucan 1,3-beta-Glucosidase</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006031" MajorTopicYN="N">Glycosylation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009844" MajorTopicYN="N">Oligosaccharides</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020075" MajorTopicYN="N">Phanerochaete</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2004</Year><Month>08</Month><Day>27</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2004</Year><Month>09</Month><Day>28</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2004</Year><Month>09</Month><Day>28</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2004</Year><Month>12</Month><Day>8</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2005</Year><Month>5</Month><Day>25</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2004</Year><Month>12</Month><Day>8</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">15582611</ArticleId><ArticleId IdType="pii">S0008-6215(04)00428-8</ArticleId><ArticleId IdType="doi">10.1016/j.carres.2004.09.019</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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