Trade-off between processivity and hydrolytic velocity of cellobiohydrolases at the surface of crystalline cellulose.
Identifieur interne : 000329 ( Main/Corpus ); précédent : 000328; suivant : 000330Trade-off between processivity and hydrolytic velocity of cellobiohydrolases at the surface of crystalline cellulose.
Auteurs : Akihiko Nakamura ; Hiroki Watanabe ; Takuya Ishida ; Takayuki Uchihashi ; Masahisa Wada ; Toshio Ando ; Kiyohiko Igarashi ; Masahiro SamejimaSource :
- Journal of the American Chemical Society [ 1520-5126 ] ; 2014.
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
Links to Exploration step
pubmed:24571226Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Trade-off between processivity and hydrolytic velocity of cellobiohydrolases at the surface of crystalline cellulose.</title>
<author><name sortKey="Nakamura, Akihiko" sort="Nakamura, Akihiko" uniqKey="Nakamura A" first="Akihiko" last="Nakamura">Akihiko Nakamura</name>
<affiliation><nlm:affiliation>Department of Biomaterial Sciences, Graduate School of Agricultural and Life Sciences, The University of Tokyo , Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan.</nlm:affiliation>
</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>
</titleStmt>
<publicationStmt><idno type="wicri:source">PubMed</idno>
<date when="2014">2014</date>
<idno type="RBID">pubmed:24571226</idno>
<idno type="pmid">24571226</idno>
<idno type="doi">10.1021/ja4119994</idno>
<idno type="wicri:Area/Main/Corpus">000329</idno>
<idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000329</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en">Trade-off between processivity and hydrolytic velocity of cellobiohydrolases at the surface of crystalline cellulose.</title>
<author><name sortKey="Nakamura, Akihiko" sort="Nakamura, Akihiko" uniqKey="Nakamura A" first="Akihiko" last="Nakamura">Akihiko Nakamura</name>
<affiliation><nlm:affiliation>Department of Biomaterial Sciences, Graduate School of Agricultural and Life Sciences, The University of Tokyo , Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan.</nlm:affiliation>
</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="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="enzymology" xml:lang="en"><term>Phanerochaete</term>
<term>Trichoderma</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>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">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. </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>
</record>
Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Bois/explor/PhanerochaeteV1/Data/Main/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000329 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Corpus/biblio.hfd -nk 000329 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien |wiki= Bois |area= PhanerochaeteV1 |flux= Main |étape= Corpus |type= RBID |clé= pubmed:24571226 |texte= Trade-off between processivity and hydrolytic velocity of cellobiohydrolases at the surface of crystalline cellulose. }}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Corpus/RBID.i -Sk "pubmed:24571226" \ | HfdSelect -Kh $EXPLOR_AREA/Data/Main/Corpus/biblio.hfd \ | NlmPubMed2Wicri -a PhanerochaeteV1
![]() | This area was generated with Dilib version V0.6.37. | ![]() |