Cloning and characterization of a thermostable cellobiose dehydrogenase from Sporotrichum thermophile.
Identifieur interne : 000B42 ( Main/Exploration ); précédent : 000B41; suivant : 000B43Cloning and characterization of a thermostable cellobiose dehydrogenase from Sporotrichum thermophile.
Auteurs : S S Subramaniam [États-Unis] ; S R Nagalla ; V. RenganathanSource :
- Archives of biochemistry and biophysics [ 0003-9861 ] ; 1999.
Descripteurs français
- KwdFr :
- ADN complémentaire (MeSH), Alignement de séquences (MeSH), Banque de gènes (MeSH), Carbohydrate dehydrogenases (composition chimique), Carbohydrate dehydrogenases (isolement et purification), Carbohydrate dehydrogenases (métabolisme), Chromatographie d'échange d'ions (MeSH), Chromatographie sur gel (MeSH), Cinétique (MeSH), Clonage moléculaire (MeSH), Données de séquences moléculaires (MeSH), Flavines (analyse), Fragments peptidiques (composition chimique), Hème (métabolisme), Masse moléculaire (MeSH), Phanerochaete (enzymologie), Protéines recombinantes (composition chimique), Protéines recombinantes (isolement et purification), Protéines recombinantes (métabolisme), Similitude de séquences d'acides aminés (MeSH), Sites de fixation (MeSH), Sporothrix (enzymologie), Sporothrix (génétique), Spécificité du substrat (MeSH), Stabilité enzymatique (MeSH), Séquence d'acides aminés (MeSH), Température élevée (MeSH), Thermodynamique (MeSH).
- MESH :
- analyse : Flavines.
- composition chimique : Carbohydrate dehydrogenases, Fragments peptidiques, Protéines recombinantes.
- enzymologie : Phanerochaete, Sporothrix.
- génétique : Sporothrix.
- isolement et purification : Carbohydrate dehydrogenases, Protéines recombinantes.
- métabolisme : Carbohydrate dehydrogenases, Hème, Protéines recombinantes.
- ADN complémentaire, Alignement de séquences, Banque de gènes, Chromatographie d'échange d'ions, Chromatographie sur gel, Cinétique, Clonage moléculaire, Données de séquences moléculaires, Masse moléculaire, Similitude de séquences d'acides aminés, Sites de fixation, Spécificité du substrat, Stabilité enzymatique, Séquence d'acides aminés, Température élevée, Thermodynamique.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Binding Sites (MeSH), Carbohydrate Dehydrogenases (chemistry), Carbohydrate Dehydrogenases (isolation & purification), Carbohydrate Dehydrogenases (metabolism), Chromatography, Gel (MeSH), Chromatography, Ion Exchange (MeSH), Cloning, Molecular (MeSH), DNA, Complementary (MeSH), Enzyme Stability (MeSH), Flavins (analysis), Gene Library (MeSH), Heme (metabolism), Hot Temperature (MeSH), Kinetics (MeSH), Molecular Sequence Data (MeSH), Molecular Weight (MeSH), Peptide Fragments (chemistry), Phanerochaete (enzymology), Recombinant Proteins (chemistry), Recombinant Proteins (isolation & purification), Recombinant Proteins (metabolism), Sequence Alignment (MeSH), Sequence Homology, Amino Acid (MeSH), Sporothrix (enzymology), Sporothrix (genetics), Substrate Specificity (MeSH), Thermodynamics (MeSH).
- MESH :
- chemical , analysis : Flavins.
- chemical , chemistry : Carbohydrate Dehydrogenases, Peptide Fragments, Recombinant Proteins.
- chemical , isolation & purification : Carbohydrate Dehydrogenases, Recombinant Proteins.
- chemical , metabolism : Carbohydrate Dehydrogenases, Heme, Recombinant Proteins.
- enzymology : Phanerochaete, Sporothrix.
- genetics : Sporothrix.
- Amino Acid Sequence, Binding Sites, Chromatography, Gel, Chromatography, Ion Exchange, Cloning, Molecular, DNA, Complementary, Enzyme Stability, Gene Library, Hot Temperature, Kinetics, Molecular Sequence Data, Molecular Weight, Sequence Alignment, Sequence Homology, Amino Acid, Substrate Specificity, Thermodynamics.
Abstract
Cellobiose dehydrogenase (CDH) is an extracellular hemoflavoenzyme produced by several wood-degrading fungi. CDH contains one heme b and one FAD per molecule and oxidizes cellobiose to cellobionolactone in the presence of cytochrome c. In this report, a thermostable CDH from the thermophilic ascomycete Sporotrichum thermophile has been purified, cloned, and characterized. The temperature optimum for this CDH reaction was 60 degrees C, and the activation energy for the reaction was 26.3 kJ/mol. The Km and kcat were temperature-dependent and increased as reaction temperature increased. These kinetic properties prove that this CDH is truly thermophilic. A 2.8-kb cDNA was isolated by screening an expression library of S. thermophile with a polyclonal antisera raised against Phanerochaete chrysosporium CDH. The cDNA encoded an 807-amino-acid protein with a predicted mass of 86,332 Da. S. thermophile CDH is organized into three domains, an N-terminal flavin domain, a middle heme domain, and a C-terminal cellulose-binding domain, which shows sequence similarity with the cellulose-binding domains of endoglucanases and cellobiohydrolases from Trichoderma reesei. Comparison with the CDH sequences of P. chrysosporium and Trametes versicolor identified Met 95 and His 143 as potential heme coordinations. EFIG, LGGPM, and VNSTH motifs in the heme domain and the XRXPXTDXPSXDGXRY motif in the flavin domain were identified as CDH-specific motifs. With regard to the amino acid composition, S. thermophile CDH has more disulfide linkages and acidic and basic amino acids compared to CDHs from P. chrysosporium and T. versicolor.
DOI: 10.1006/abbi.1999.1152
PubMed: 10328816
Affiliations:
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Le document en format XML
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Renganathan</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1999">1999</date><idno type="RBID">pubmed:10328816</idno><idno type="pmid">10328816</idno><idno type="doi">10.1006/abbi.1999.1152</idno><idno type="wicri:Area/Main/Corpus">000B45</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000B45</idno><idno type="wicri:Area/Main/Curation">000B45</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000B45</idno><idno type="wicri:Area/Main/Exploration">000B45</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Cloning and characterization of a thermostable cellobiose dehydrogenase from Sporotrichum thermophile.</title><author><name sortKey="Subramaniam, S S" sort="Subramaniam, S S" uniqKey="Subramaniam S" first="S S" last="Subramaniam">S S Subramaniam</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry and Molecular Biology, Oregon Graduate Institute of Science and Technology, Portland, Oregon, 97291-1000, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biochemistry and Molecular Biology, Oregon Graduate Institute of Science and Technology, Portland, Oregon, 97291-1000</wicri:regionArea><wicri:noRegion>97291-1000</wicri:noRegion></affiliation></author><author><name sortKey="Nagalla, S R" sort="Nagalla, S R" uniqKey="Nagalla S" first="S R" last="Nagalla">S R Nagalla</name></author><author><name sortKey="Renganathan, V" sort="Renganathan, V" uniqKey="Renganathan V" first="V" last="Renganathan">V. Renganathan</name></author></analytic><series><title level="j">Archives of biochemistry and biophysics</title><idno type="ISSN">0003-9861</idno><imprint><date when="1999" type="published">1999</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Binding Sites (MeSH)</term><term>Carbohydrate Dehydrogenases (chemistry)</term><term>Carbohydrate Dehydrogenases (isolation & purification)</term><term>Carbohydrate Dehydrogenases (metabolism)</term><term>Chromatography, Gel (MeSH)</term><term>Chromatography, Ion Exchange (MeSH)</term><term>Cloning, Molecular (MeSH)</term><term>DNA, Complementary (MeSH)</term><term>Enzyme Stability (MeSH)</term><term>Flavins (analysis)</term><term>Gene Library (MeSH)</term><term>Heme (metabolism)</term><term>Hot Temperature (MeSH)</term><term>Kinetics (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Molecular Weight 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(MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Flavines (analyse)</term><term>Fragments peptidiques (composition chimique)</term><term>Hème (métabolisme)</term><term>Masse moléculaire (MeSH)</term><term>Phanerochaete (enzymologie)</term><term>Protéines recombinantes (composition chimique)</term><term>Protéines recombinantes (isolement et purification)</term><term>Protéines recombinantes (métabolisme)</term><term>Similitude de séquences d'acides aminés (MeSH)</term><term>Sites de fixation (MeSH)</term><term>Sporothrix (enzymologie)</term><term>Sporothrix (génétique)</term><term>Spécificité du substrat (MeSH)</term><term>Stabilité enzymatique (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="analysis" xml:lang="en"><term>Flavins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" 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Weight</term><term>Sequence Alignment</term><term>Sequence Homology, Amino Acid</term><term>Substrate Specificity</term><term>Thermodynamics</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>ADN complémentaire</term><term>Alignement de séquences</term><term>Banque de gènes</term><term>Chromatographie d'échange d'ions</term><term>Chromatographie sur gel</term><term>Cinétique</term><term>Clonage moléculaire</term><term>Données de séquences moléculaires</term><term>Masse moléculaire</term><term>Similitude de séquences d'acides aminés</term><term>Sites de fixation</term><term>Spécificité du substrat</term><term>Stabilité enzymatique</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">Cellobiose dehydrogenase (CDH) is an extracellular hemoflavoenzyme produced by several wood-degrading fungi. CDH contains one heme b and one FAD per molecule and oxidizes cellobiose to cellobionolactone in the presence of cytochrome c. In this report, a thermostable CDH from the thermophilic ascomycete Sporotrichum thermophile has been purified, cloned, and characterized. The temperature optimum for this CDH reaction was 60 degrees C, and the activation energy for the reaction was 26.3 kJ/mol. The Km and kcat were temperature-dependent and increased as reaction temperature increased. These kinetic properties prove that this CDH is truly thermophilic. A 2.8-kb cDNA was isolated by screening an expression library of S. thermophile with a polyclonal antisera raised against Phanerochaete chrysosporium CDH. The cDNA encoded an 807-amino-acid protein with a predicted mass of 86,332 Da. S. thermophile CDH is organized into three domains, an N-terminal flavin domain, a middle heme domain, and a C-terminal cellulose-binding domain, which shows sequence similarity with the cellulose-binding domains of endoglucanases and cellobiohydrolases from Trichoderma reesei. Comparison with the CDH sequences of P. chrysosporium and Trametes versicolor identified Met 95 and His 143 as potential heme coordinations. EFIG, LGGPM, and VNSTH motifs in the heme domain and the XRXPXTDXPSXDGXRY motif in the flavin domain were identified as CDH-specific motifs. With regard to the amino acid composition, S. thermophile CDH has more disulfide linkages and acidic and basic amino acids compared to CDHs from P. chrysosporium and T. versicolor.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">10328816</PMID><DateCompleted><Year>1999</Year><Month>06</Month><Day>11</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0003-9861</ISSN><JournalIssue CitedMedium="Print"><Volume>365</Volume><Issue>2</Issue><PubDate><Year>1999</Year><Month>May</Month><Day>15</Day></PubDate></JournalIssue><Title>Archives of biochemistry and biophysics</Title><ISOAbbreviation>Arch Biochem Biophys</ISOAbbreviation></Journal><ArticleTitle>Cloning and characterization of a thermostable cellobiose dehydrogenase from Sporotrichum thermophile.</ArticleTitle><Pagination><MedlinePgn>223-30</MedlinePgn></Pagination><Abstract><AbstractText>Cellobiose dehydrogenase (CDH) is an extracellular hemoflavoenzyme produced by several wood-degrading fungi. CDH contains one heme b and one FAD per molecule and oxidizes cellobiose to cellobionolactone in the presence of cytochrome c. In this report, a thermostable CDH from the thermophilic ascomycete Sporotrichum thermophile has been purified, cloned, and characterized. The temperature optimum for this CDH reaction was 60 degrees C, and the activation energy for the reaction was 26.3 kJ/mol. The Km and kcat were temperature-dependent and increased as reaction temperature increased. These kinetic properties prove that this CDH is truly thermophilic. A 2.8-kb cDNA was isolated by screening an expression library of S. thermophile with a polyclonal antisera raised against Phanerochaete chrysosporium CDH. The cDNA encoded an 807-amino-acid protein with a predicted mass of 86,332 Da. S. thermophile CDH is organized into three domains, an N-terminal flavin domain, a middle heme domain, and a C-terminal cellulose-binding domain, which shows sequence similarity with the cellulose-binding domains of endoglucanases and cellobiohydrolases from Trichoderma reesei. Comparison with the CDH sequences of P. chrysosporium and Trametes versicolor identified Met 95 and His 143 as potential heme coordinations. EFIG, LGGPM, and VNSTH motifs in the heme domain and the XRXPXTDXPSXDGXRY motif in the flavin domain were identified as CDH-specific motifs. With regard to the amino acid composition, S. thermophile CDH has more disulfide linkages and acidic and basic amino acids compared to CDHs from P. chrysosporium and T. versicolor.</AbstractText><CopyrightInformation>Copyright 1999 Academic Press.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Subramaniam</LastName><ForeName>S S</ForeName><Initials>SS</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Molecular Biology, Oregon Graduate Institute of Science and Technology, Portland, Oregon, 97291-1000, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Nagalla</LastName><ForeName>S R</ForeName><Initials>SR</Initials></Author><Author ValidYN="Y"><LastName>Renganathan</LastName><ForeName>V</ForeName><Initials>V</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>Arch Biochem Biophys</MedlineTA><NlmUniqueID>0372430</NlmUniqueID><ISSNLinking>0003-9861</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D018076">DNA, Complementary</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005415">Flavins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010446">Peptide Fragments</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>42VZT0U6YR</RegistryNumber><NameOfSubstance UI="D006418">Heme</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.-</RegistryNumber><NameOfSubstance UI="D002237">Carbohydrate Dehydrogenases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.99.18</RegistryNumber><NameOfSubstance UI="C019859">cellobiose-quinone oxidoreductase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002237" MajorTopicYN="N">Carbohydrate Dehydrogenases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002850" MajorTopicYN="N">Chromatography, Gel</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002852" MajorTopicYN="N">Chromatography, Ion Exchange</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003001" MajorTopicYN="N">Cloning, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018076" MajorTopicYN="N">DNA, Complementary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004795" MajorTopicYN="N">Enzyme Stability</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005415" MajorTopicYN="N">Flavins</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015723" MajorTopicYN="N">Gene Library</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006418" MajorTopicYN="N">Heme</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006358" MajorTopicYN="N">Hot Temperature</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008970" MajorTopicYN="N">Molecular Weight</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010446" MajorTopicYN="N">Peptide Fragments</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020075" MajorTopicYN="N">Phanerochaete</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016415" MajorTopicYN="N">Sequence Alignment</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017386" MajorTopicYN="N">Sequence Homology, Amino Acid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013175" MajorTopicYN="N">Sporothrix</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</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>1999</Year><Month>5</Month><Day>18</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1999</Year><Month>5</Month><Day>18</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1999</Year><Month>5</Month><Day>18</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">10328816</ArticleId><ArticleId IdType="pii">S0003-9861(99)91152-9</ArticleId><ArticleId IdType="doi">10.1006/abbi.1999.1152</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country></list><tree><noCountry><name sortKey="Nagalla, S R" sort="Nagalla, S R" uniqKey="Nagalla S" first="S R" last="Nagalla">S R Nagalla</name><name sortKey="Renganathan, V" sort="Renganathan, V" uniqKey="Renganathan V" first="V" last="Renganathan">V. Renganathan</name></noCountry><country name="États-Unis"><noRegion><name sortKey="Subramaniam, S S" sort="Subramaniam, S S" uniqKey="Subramaniam S" first="S S" last="Subramaniam">S S Subramaniam</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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