Effect of single active-site cleft mutation on product specificity in a thermostable bacterial cellulase.
Identifieur interne : 004597 ( Main/Exploration ); précédent : 004596; suivant : 004598Effect of single active-site cleft mutation on product specificity in a thermostable bacterial cellulase.
Auteurs : Tauna R. Rignall [États-Unis] ; John O. Baker ; Suzanne L. Mccarter ; William S. Adney ; Todd B. Vinzant ; Stephen R. Decker ; Michael E. HimmelSource :
- Applied biochemistry and biotechnology [ 0273-2289 ] ; 2002.
Descripteurs français
- KwdFr :
- Actinomycetales (enzymologie), Cellulase (composition chimique), Cellulase (génétique), Cellulase (métabolisme), Conformation des protéines (MeSH), Cristallographie aux rayons X (MeSH), Domaine catalytique (MeSH), Modèles moléculaires (MeSH), Mutagenèse dirigée (MeSH), Protéines recombinantes (composition chimique), Protéines recombinantes (métabolisme), Sites de fixation (MeSH), Spécificité du substrat (MeSH), Stabilité enzymatique (MeSH), Substitution d'acide aminé (MeSH), Séquence d'acides aminés (MeSH), Température élevée (MeSH), Thermodynamique (MeSH).
- MESH :
- composition chimique : Cellulase, Protéines recombinantes.
- enzymologie : Actinomycetales.
- génétique : Cellulase.
- métabolisme : Cellulase, Protéines recombinantes.
- Conformation des protéines, Cristallographie aux rayons X, Domaine catalytique, Modèles moléculaires, Mutagenèse dirigée, Sites de fixation, Spécificité du substrat, Stabilité enzymatique, Substitution d'acide aminé, Séquence d'acides aminés, Température élevée, Thermodynamique.
English descriptors
- KwdEn :
- Actinomycetales (enzymology), Amino Acid Sequence (MeSH), Amino Acid Substitution (MeSH), Binding Sites (MeSH), Catalytic Domain (MeSH), Cellulase (chemistry), Cellulase (genetics), Cellulase (metabolism), Crystallography, X-Ray (MeSH), Enzyme Stability (MeSH), Hot Temperature (MeSH), Models, Molecular (MeSH), Mutagenesis, Site-Directed (MeSH), Protein Conformation (MeSH), Recombinant Proteins (chemistry), Recombinant Proteins (metabolism), Substrate Specificity (MeSH), Thermodynamics (MeSH).
- MESH :
- chemical , chemistry : Cellulase, Recombinant Proteins.
- enzymology : Actinomycetales.
- chemical , genetics : Cellulase.
- chemical , metabolism : Cellulase, Recombinant Proteins.
- Amino Acid Sequence, Amino Acid Substitution, Binding Sites, Catalytic Domain, Crystallography, X-Ray, Enzyme Stability, Hot Temperature, Models, Molecular, Mutagenesis, Site-Directed, Protein Conformation, Substrate Specificity, Thermodynamics.
Abstract
Mutation of a single active-site cleft tyrosyl residue to a glycyl residue significantly changes the mixture of products released from phosphoric acid-swollen cellulose (PSC) by EIcd, the catalytic domain of the endoglucanase-I from Acidothermus cellulolyticus. The percentage of glucose in the product stream is almost 40% greater for the Y245G mutant (and for an additional double mutant, Y245G/Q204A) than for the wild type enzyme. Comparisons of results for digestion PSC and of pretreated yellow poplar suggest that the observed shifts in product specificity are connected to the hydrolysis of a more easily digestible fraction of both substrates. A model is presented that relates the changes in product specificity to a mutation-driven shift in indexing of the polymeric substrate along the extended binding-site cleft.
DOI: 10.1385/abab:98-100:1-9:383
PubMed: 12018266
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Adney</name></author><author><name sortKey="Vinzant, Todd B" sort="Vinzant, Todd B" uniqKey="Vinzant T" first="Todd B" last="Vinzant">Todd B. Vinzant</name></author><author><name sortKey="Decker, Stephen R" sort="Decker, Stephen R" uniqKey="Decker S" first="Stephen R" last="Decker">Stephen R. Decker</name></author><author><name sortKey="Himmel, Michael E" sort="Himmel, Michael E" uniqKey="Himmel M" first="Michael E" last="Himmel">Michael E. Himmel</name></author></analytic><series><title level="j">Applied biochemistry and biotechnology</title><idno type="ISSN">0273-2289</idno><imprint><date when="2002" type="published">2002</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Actinomycetales (enzymology)</term><term>Amino Acid Sequence (MeSH)</term><term>Amino Acid Substitution (MeSH)</term><term>Binding Sites (MeSH)</term><term>Catalytic Domain (MeSH)</term><term>Cellulase (chemistry)</term><term>Cellulase (genetics)</term><term>Cellulase (metabolism)</term><term>Crystallography, X-Ray (MeSH)</term><term>Enzyme Stability (MeSH)</term><term>Hot Temperature (MeSH)</term><term>Models, Molecular (MeSH)</term><term>Mutagenesis, Site-Directed (MeSH)</term><term>Protein Conformation (MeSH)</term><term>Recombinant Proteins (chemistry)</term><term>Recombinant Proteins (metabolism)</term><term>Substrate Specificity (MeSH)</term><term>Thermodynamics (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Actinomycetales (enzymologie)</term><term>Cellulase (composition chimique)</term><term>Cellulase (génétique)</term><term>Cellulase (métabolisme)</term><term>Conformation des protéines (MeSH)</term><term>Cristallographie aux rayons X (MeSH)</term><term>Domaine catalytique (MeSH)</term><term>Modèles moléculaires (MeSH)</term><term>Mutagenèse dirigée (MeSH)</term><term>Protéines recombinantes (composition chimique)</term><term>Protéines recombinantes (métabolisme)</term><term>Sites de fixation (MeSH)</term><term>Spécificité du substrat (MeSH)</term><term>Stabilité enzymatique (MeSH)</term><term>Substitution d'acide aminé (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Température élevée (MeSH)</term><term>Thermodynamique (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cellulase</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Cellulase</term><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Actinomycetales</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Actinomycetales</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Cellulase</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Cellulase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cellulase</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cellulase</term><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Amino Acid Substitution</term><term>Binding Sites</term><term>Catalytic Domain</term><term>Crystallography, X-Ray</term><term>Enzyme Stability</term><term>Hot Temperature</term><term>Models, Molecular</term><term>Mutagenesis, Site-Directed</term><term>Protein Conformation</term><term>Substrate Specificity</term><term>Thermodynamics</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Conformation des protéines</term><term>Cristallographie aux rayons X</term><term>Domaine catalytique</term><term>Modèles moléculaires</term><term>Mutagenèse dirigée</term><term>Sites de fixation</term><term>Spécificité du substrat</term><term>Stabilité enzymatique</term><term>Substitution d'acide aminé</term><term>Séquence d'acides aminés</term><term>Température élevée</term><term>Thermodynamique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Mutation of a single active-site cleft tyrosyl residue to a glycyl residue significantly changes the mixture of products released from phosphoric acid-swollen cellulose (PSC) by EIcd, the catalytic domain of the endoglucanase-I from Acidothermus cellulolyticus. The percentage of glucose in the product stream is almost 40% greater for the Y245G mutant (and for an additional double mutant, Y245G/Q204A) than for the wild type enzyme. Comparisons of results for digestion PSC and of pretreated yellow poplar suggest that the observed shifts in product specificity are connected to the hydrolysis of a more easily digestible fraction of both substrates. A model is presented that relates the changes in product specificity to a mutation-driven shift in indexing of the polymeric substrate along the extended binding-site cleft.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">12018266</PMID><DateCompleted><Year>2002</Year><Month>11</Month><Day>06</Day></DateCompleted><DateRevised><Year>2019</Year><Month>09</Month><Day>10</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0273-2289</ISSN><JournalIssue CitedMedium="Print"><Volume>98-100</Volume><PubDate><Year>2002</Year><Season>Spring</Season></PubDate></JournalIssue><Title>Applied biochemistry and biotechnology</Title><ISOAbbreviation>Appl Biochem Biotechnol</ISOAbbreviation></Journal><ArticleTitle>Effect of single active-site cleft mutation on product specificity in a thermostable bacterial cellulase.</ArticleTitle><Pagination><MedlinePgn>383-94</MedlinePgn></Pagination><Abstract><AbstractText>Mutation of a single active-site cleft tyrosyl residue to a glycyl residue significantly changes the mixture of products released from phosphoric acid-swollen cellulose (PSC) by EIcd, the catalytic domain of the endoglucanase-I from Acidothermus cellulolyticus. The percentage of glucose in the product stream is almost 40% greater for the Y245G mutant (and for an additional double mutant, Y245G/Q204A) than for the wild type enzyme. Comparisons of results for digestion PSC and of pretreated yellow poplar suggest that the observed shifts in product specificity are connected to the hydrolysis of a more easily digestible fraction of both substrates. A model is presented that relates the changes in product specificity to a mutation-driven shift in indexing of the polymeric substrate along the extended binding-site cleft.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Rignall</LastName><ForeName>Tauna R</ForeName><Initials>TR</Initials><AffiliationInfo><Affiliation>Biotechnology for Fuels and Chemicals Division, National Bioenergy Center, National Renewable Energy Laboratory, Golden, CO 80401, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Baker</LastName><ForeName>John O</ForeName><Initials>JO</Initials></Author><Author ValidYN="Y"><LastName>McCarter</LastName><ForeName>Suzanne L</ForeName><Initials>SL</Initials></Author><Author ValidYN="Y"><LastName>Adney</LastName><ForeName>William S</ForeName><Initials>WS</Initials></Author><Author ValidYN="Y"><LastName>Vinzant</LastName><ForeName>Todd B</ForeName><Initials>TB</Initials></Author><Author ValidYN="Y"><LastName>Decker</LastName><ForeName>Stephen R</ForeName><Initials>SR</Initials></Author><Author ValidYN="Y"><LastName>Himmel</LastName><ForeName>Michael E</ForeName><Initials>ME</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Appl Biochem Biotechnol</MedlineTA><NlmUniqueID>8208561</NlmUniqueID><ISSNLinking>0273-2289</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.-</RegistryNumber><NameOfSubstance UI="C056374">endoglucanase 1</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.4</RegistryNumber><NameOfSubstance UI="D002480">Cellulase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000192" MajorTopicYN="N">Actinomycetales</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019943" MajorTopicYN="N">Amino Acid Substitution</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020134" MajorTopicYN="N">Catalytic Domain</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002480" MajorTopicYN="N">Cellulase</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018360" MajorTopicYN="N">Crystallography, X-Ray</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004795" MajorTopicYN="N">Enzyme Stability</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006358" MajorTopicYN="N">Hot Temperature</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016297" MajorTopicYN="N">Mutagenesis, Site-Directed</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013816" MajorTopicYN="N">Thermodynamics</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2002</Year><Month>5</Month><Day>23</Day><Hour>10</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2002</Year><Month>11</Month><Day>26</Day><Hour>4</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2002</Year><Month>5</Month><Day>23</Day><Hour>10</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">12018266</ArticleId><ArticleId IdType="doi">10.1385/abab:98-100:1-9:383</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>Colorado</li></region></list><tree><noCountry><name sortKey="Adney, William S" sort="Adney, William S" uniqKey="Adney W" first="William S" last="Adney">William S. Adney</name><name sortKey="Baker, John O" sort="Baker, John O" uniqKey="Baker J" first="John O" last="Baker">John O. Baker</name><name sortKey="Decker, Stephen R" sort="Decker, Stephen R" uniqKey="Decker S" first="Stephen R" last="Decker">Stephen R. Decker</name><name sortKey="Himmel, Michael E" sort="Himmel, Michael E" uniqKey="Himmel M" first="Michael E" last="Himmel">Michael E. Himmel</name><name sortKey="Mccarter, Suzanne L" sort="Mccarter, Suzanne L" uniqKey="Mccarter S" first="Suzanne L" last="Mccarter">Suzanne L. Mccarter</name><name sortKey="Vinzant, Todd B" sort="Vinzant, Todd B" uniqKey="Vinzant T" first="Todd B" last="Vinzant">Todd B. Vinzant</name></noCountry><country name="États-Unis"><region name="Colorado"><name sortKey="Rignall, Tauna R" sort="Rignall, Tauna R" uniqKey="Rignall T" first="Tauna R" last="Rignall">Tauna R. Rignall</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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