Trade-off between processivity and hydrolytic velocity of cellobiohydrolases at the surface of crystalline cellulose.
Identifieur interne : 000293 ( Main/Exploration ); précédent : 000292; suivant : 000294Trade-off between processivity and hydrolytic velocity of cellobiohydrolases at the surface of crystalline cellulose.
Auteurs : Akihiko Nakamura [Japon] ; Hiroki Watanabe ; Takuya Ishida ; Takayuki Uchihashi ; Masahisa Wada ; Toshio Ando ; Kiyohiko Igarashi ; Masahiro SamejimaSource :
- Journal of the American Chemical Society [ 1520-5126 ] ; 2014.
Descripteurs français
- KwdFr :
- Cellulose (composition chimique), Cellulose (métabolisme), Cellulose 1,4-beta-cellobiosidase (composition chimique), Cellulose 1,4-beta-cellobiosidase (métabolisme), Cinétique (MeSH), Conformation des protéines (MeSH), Hydrolyse (MeSH), Modèles moléculaires (MeSH), Mouvement (MeSH), Phanerochaete (enzymologie), Propriétés de surface (MeSH), Trichoderma (enzymologie).
- MESH :
- composition chimique : Cellulose, Cellulose 1,4-beta-cellobiosidase.
- enzymologie : Phanerochaete, Trichoderma.
- métabolisme : Cellulose, Cellulose 1,4-beta-cellobiosidase.
- Cinétique, Conformation des protéines, Hydrolyse, Modèles moléculaires, Mouvement, Propriétés de surface.
English descriptors
- KwdEn :
- Cellulose (chemistry), Cellulose (metabolism), Cellulose 1,4-beta-Cellobiosidase (chemistry), Cellulose 1,4-beta-Cellobiosidase (metabolism), Hydrolysis (MeSH), Kinetics (MeSH), Models, Molecular (MeSH), Movement (MeSH), Phanerochaete (enzymology), Protein Conformation (MeSH), Surface Properties (MeSH), Trichoderma (enzymology).
- MESH :
- chemical , chemistry : Cellulose, Cellulose 1,4-beta-Cellobiosidase.
- chemical , metabolism : Cellulose, Cellulose 1,4-beta-Cellobiosidase.
- enzymology : Phanerochaete, Trichoderma.
- Hydrolysis, Kinetics, Models, Molecular, Movement, Protein Conformation, Surface Properties.
Abstract
Analysis of heterogeneous catalysis at an interface is difficult because of the variety of reaction sites and the difficulty of observing the reaction. Enzymatic hydrolysis of cellulose by cellulases is a typical heterogeneous reaction at a solid/liquid interface, and a key parameter of such reactions on polymeric substrates is the processivity, i.e., the number of catalytic cycles that can occur without detachment of the enzyme from the substrate. In this study, we evaluated the reactions of three closely related glycoside hydrolase family 7 cellobiohydrolases from filamentous fungi at the molecular level by means of high-speed atomic force microscopy to investigate the structure-function relationship of the cellobiohydrolases on crystalline cellulose. We found that high moving velocity of enzyme molecules on the surface is associated with a high dissociation rate constant from the substrate, which means weak interaction between enzyme and substrate. Moreover, higher values of processivity were associated with more loop regions covering the subsite cleft, which may imply higher binding affinity. Loop regions covering the subsites result in stronger interaction, which decreases the velocity but increases the processivity. These results indicate that there is a trade-off between processivity and hydrolytic velocity among processive cellulases.
DOI: 10.1021/ja4119994
PubMed: 24571226
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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first="Hiroki" last="Watanabe">Hiroki Watanabe</name></author><author><name sortKey="Ishida, Takuya" sort="Ishida, Takuya" uniqKey="Ishida T" first="Takuya" last="Ishida">Takuya Ishida</name></author><author><name sortKey="Uchihashi, Takayuki" sort="Uchihashi, Takayuki" uniqKey="Uchihashi T" first="Takayuki" last="Uchihashi">Takayuki Uchihashi</name></author><author><name sortKey="Wada, Masahisa" sort="Wada, Masahisa" uniqKey="Wada M" first="Masahisa" last="Wada">Masahisa Wada</name></author><author><name sortKey="Ando, Toshio" sort="Ando, Toshio" uniqKey="Ando T" first="Toshio" last="Ando">Toshio Ando</name></author><author><name sortKey="Igarashi, Kiyohiko" sort="Igarashi, Kiyohiko" uniqKey="Igarashi K" first="Kiyohiko" last="Igarashi">Kiyohiko Igarashi</name></author><author><name sortKey="Samejima, Masahiro" sort="Samejima, Masahiro" uniqKey="Samejima M" first="Masahiro" last="Samejima">Masahiro Samejima</name></author></titleStmt><publicationStmt><idno 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University of Tokyo , Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Biomaterial Sciences, Graduate School of Agricultural and Life Sciences, The University of Tokyo , Yayoi, Bunkyo-ku, Tokyo 113-8657</wicri:regionArea><placeName><settlement type="city">Tokyo</settlement><region type="région">Région de Kantō</region></placeName></affiliation></author><author><name sortKey="Watanabe, Hiroki" sort="Watanabe, Hiroki" uniqKey="Watanabe H" first="Hiroki" last="Watanabe">Hiroki Watanabe</name></author><author><name sortKey="Ishida, Takuya" sort="Ishida, Takuya" uniqKey="Ishida T" first="Takuya" last="Ishida">Takuya Ishida</name></author><author><name sortKey="Uchihashi, Takayuki" sort="Uchihashi, Takayuki" uniqKey="Uchihashi T" first="Takayuki" last="Uchihashi">Takayuki Uchihashi</name></author><author><name sortKey="Wada, Masahisa" sort="Wada, Masahisa" uniqKey="Wada M" first="Masahisa" last="Wada">Masahisa Wada</name></author><author><name sortKey="Ando, Toshio" sort="Ando, Toshio" uniqKey="Ando T" first="Toshio" last="Ando">Toshio Ando</name></author><author><name sortKey="Igarashi, Kiyohiko" sort="Igarashi, Kiyohiko" uniqKey="Igarashi K" first="Kiyohiko" last="Igarashi">Kiyohiko Igarashi</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">Journal of the American Chemical Society</title><idno type="eISSN">1520-5126</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Cellulose (chemistry)</term><term>Cellulose (metabolism)</term><term>Cellulose 1,4-beta-Cellobiosidase (chemistry)</term><term>Cellulose 1,4-beta-Cellobiosidase (metabolism)</term><term>Hydrolysis (MeSH)</term><term>Kinetics (MeSH)</term><term>Models, Molecular (MeSH)</term><term>Movement (MeSH)</term><term>Phanerochaete (enzymology)</term><term>Protein Conformation (MeSH)</term><term>Surface Properties (MeSH)</term><term>Trichoderma (enzymology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Cellulose (composition chimique)</term><term>Cellulose (métabolisme)</term><term>Cellulose 1,4-beta-cellobiosidase (composition chimique)</term><term>Cellulose 1,4-beta-cellobiosidase (métabolisme)</term><term>Cinétique (MeSH)</term><term>Conformation des protéines (MeSH)</term><term>Hydrolyse (MeSH)</term><term>Modèles moléculaires (MeSH)</term><term>Mouvement (MeSH)</term><term>Phanerochaete (enzymologie)</term><term>Propriétés de surface (MeSH)</term><term>Trichoderma (enzymologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cellulose</term><term>Cellulose 1,4-beta-Cellobiosidase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cellulose</term><term>Cellulose 1,4-beta-Cellobiosidase</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Cellulose</term><term>Cellulose 1,4-beta-cellobiosidase</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Phanerochaete</term><term>Trichoderma</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Phanerochaete</term><term>Trichoderma</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cellulose</term><term>Cellulose 1,4-beta-cellobiosidase</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Hydrolysis</term><term>Kinetics</term><term>Models, Molecular</term><term>Movement</term><term>Protein Conformation</term><term>Surface Properties</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cinétique</term><term>Conformation des protéines</term><term>Hydrolyse</term><term>Modèles 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Enzymatic hydrolysis of cellulose by cellulases is a typical heterogeneous reaction at a solid/liquid interface, and a key parameter of such reactions on polymeric substrates is the processivity, i.e., the number of catalytic cycles that can occur without detachment of the enzyme from the substrate. In this study, we evaluated the reactions of three closely related glycoside hydrolase family 7 cellobiohydrolases from filamentous fungi at the molecular level by means of high-speed atomic force microscopy to investigate the structure-function relationship of the cellobiohydrolases on crystalline cellulose. We found that high moving velocity of enzyme molecules on the surface is associated with a high dissociation rate constant from the substrate, which means weak interaction between enzyme and substrate. Moreover, higher values of processivity were associated with more loop regions covering the subsite cleft, which may imply higher binding affinity. Loop regions covering the subsites result in stronger interaction, which decreases the velocity but increases the processivity. These results indicate that there is a trade-off between processivity and hydrolytic velocity among processive cellulases. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">24571226</PMID><DateCompleted><Year>2014</Year><Month>11</Month><Day>25</Day></DateCompleted><DateRevised><Year>2014</Year><Month>03</Month><Day>26</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1520-5126</ISSN><JournalIssue CitedMedium="Internet"><Volume>136</Volume><Issue>12</Issue><PubDate><Year>2014</Year><Month>Mar</Month><Day>26</Day></PubDate></JournalIssue><Title>Journal of the American Chemical Society</Title><ISOAbbreviation>J Am Chem Soc</ISOAbbreviation></Journal><ArticleTitle>Trade-off between processivity and hydrolytic velocity of cellobiohydrolases at the surface of crystalline cellulose.</ArticleTitle><Pagination><MedlinePgn>4584-92</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1021/ja4119994</ELocationID><Abstract><AbstractText>Analysis of heterogeneous catalysis at an interface is difficult because of the variety of reaction sites and the difficulty of observing the reaction. Enzymatic hydrolysis of cellulose by cellulases is a typical heterogeneous reaction at a solid/liquid interface, and a key parameter of such reactions on polymeric substrates is the processivity, i.e., the number of catalytic cycles that can occur without detachment of the enzyme from the substrate. In this study, we evaluated the reactions of three closely related glycoside hydrolase family 7 cellobiohydrolases from filamentous fungi at the molecular level by means of high-speed atomic force microscopy to investigate the structure-function relationship of the cellobiohydrolases on crystalline cellulose. We found that high moving velocity of enzyme molecules on the surface is associated with a high dissociation rate constant from the substrate, which means weak interaction between enzyme and substrate. Moreover, higher values of processivity were associated with more loop regions covering the subsite cleft, which may imply higher binding affinity. Loop regions covering the subsites result in stronger interaction, which decreases the velocity but increases the processivity. These results indicate that there is a trade-off between processivity and hydrolytic velocity among processive cellulases. </AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Nakamura</LastName><ForeName>Akihiko</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Department of Biomaterial Sciences, Graduate School of Agricultural and Life Sciences, The University of Tokyo , Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Watanabe</LastName><ForeName>Hiroki</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Ishida</LastName><ForeName>Takuya</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Uchihashi</LastName><ForeName>Takayuki</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Wada</LastName><ForeName>Masahisa</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Ando</LastName><ForeName>Toshio</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Igarashi</LastName><ForeName>Kiyohiko</ForeName><Initials>K</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><ArticleDate DateType="Electronic"><Year>2014</Year><Month>03</Month><Day>14</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Am Chem Soc</MedlineTA><NlmUniqueID>7503056</NlmUniqueID><ISSNLinking>0002-7863</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>9004-34-6</RegistryNumber><NameOfSubstance UI="D002482">Cellulose</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.91</RegistryNumber><NameOfSubstance UI="D043366">Cellulose 1,4-beta-Cellobiosidase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D002482" MajorTopicYN="N">Cellulose</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D043366" MajorTopicYN="N">Cellulose 1,4-beta-Cellobiosidase</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="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009068" MajorTopicYN="N">Movement</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020075" MajorTopicYN="N">Phanerochaete</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013499" MajorTopicYN="N">Surface Properties</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014242" MajorTopicYN="N">Trichoderma</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2014</Year><Month>2</Month><Day>28</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2014</Year><Month>2</Month><Day>28</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2014</Year><Month>12</Month><Day>15</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">24571226</ArticleId><ArticleId IdType="doi">10.1021/ja4119994</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Japon</li></country><region><li>Région de Kantō</li></region><settlement><li>Tokyo</li></settlement></list><tree><noCountry><name sortKey="Ando, Toshio" sort="Ando, Toshio" uniqKey="Ando T" first="Toshio" last="Ando">Toshio Ando</name><name sortKey="Igarashi, Kiyohiko" sort="Igarashi, Kiyohiko" uniqKey="Igarashi K" first="Kiyohiko" last="Igarashi">Kiyohiko Igarashi</name><name sortKey="Ishida, Takuya" sort="Ishida, Takuya" uniqKey="Ishida T" first="Takuya" last="Ishida">Takuya Ishida</name><name sortKey="Samejima, Masahiro" sort="Samejima, Masahiro" uniqKey="Samejima M" first="Masahiro" last="Samejima">Masahiro Samejima</name><name sortKey="Uchihashi, Takayuki" sort="Uchihashi, Takayuki" uniqKey="Uchihashi T" first="Takayuki" last="Uchihashi">Takayuki Uchihashi</name><name sortKey="Wada, Masahisa" sort="Wada, Masahisa" uniqKey="Wada M" first="Masahisa" last="Wada">Masahisa Wada</name><name sortKey="Watanabe, Hiroki" sort="Watanabe, Hiroki" uniqKey="Watanabe H" first="Hiroki" last="Watanabe">Hiroki Watanabe</name></noCountry><country name="Japon"><region name="Région de Kantō"><name sortKey="Nakamura, Akihiko" sort="Nakamura, Akihiko" uniqKey="Nakamura A" first="Akihiko" last="Nakamura">Akihiko Nakamura</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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