A Phanerochaete chrysosporium beta-D-glucosidase/beta-D-xylosidase with specificity for (1-->3)-beta-D-glucan linkages.
Identifieur interne : 000D73 ( Main/Exploration ); précédent : 000D72; suivant : 000D74A Phanerochaete chrysosporium beta-D-glucosidase/beta-D-xylosidase with specificity for (1-->3)-beta-D-glucan linkages.
Auteurs : J L Copa-Pati O [Royaume-Uni] ; P. BrodaSource :
- Carbohydrate research [ 0008-6215 ] ; 1994.
Descripteurs français
- KwdFr :
- Agaricales (enzymologie), Chromatographie d'échange d'ions (MeSH), Chromatographie sur gel (MeSH), Cinétique (MeSH), Conformation des glucides (MeSH), Données de séquences moléculaires (MeSH), Glucanes (métabolisme), Masse moléculaire (MeSH), Spécificité du substrat (MeSH), Séquence glucidique (MeSH), Ultrafiltration (MeSH), Xylosidases (isolement et purification), Xylosidases (métabolisme), bêta-Glucosidase (isolement et purification), bêta-Glucosidase (métabolisme), Électrophorèse sur gel de polyacrylamide (MeSH).
- MESH :
- enzymologie : Agaricales.
- isolement et purification : Xylosidases, bêta-Glucosidase.
- métabolisme : Glucanes, Xylosidases, bêta-Glucosidase.
- Chromatographie d'échange d'ions, Chromatographie sur gel, Cinétique, Conformation des glucides, Données de séquences moléculaires, Masse moléculaire, Spécificité du substrat, Séquence glucidique, Ultrafiltration, Électrophorèse sur gel de polyacrylamide.
English descriptors
- KwdEn :
- Agaricales (enzymology), Carbohydrate Conformation (MeSH), Carbohydrate Sequence (MeSH), Chromatography, Gel (MeSH), Chromatography, Ion Exchange (MeSH), Electrophoresis, Polyacrylamide Gel (MeSH), Glucans (metabolism), Kinetics (MeSH), Molecular Sequence Data (MeSH), Molecular Weight (MeSH), Substrate Specificity (MeSH), Ultrafiltration (MeSH), Xylosidases (isolation & purification), Xylosidases (metabolism), beta-Glucosidase (isolation & purification), beta-Glucosidase (metabolism).
- MESH :
- chemical , isolation & purification : Xylosidases, beta-Glucosidase.
- chemical , metabolism : Glucans, Xylosidases, beta-Glucosidase.
- enzymology : Agaricales.
- Carbohydrate Conformation, Carbohydrate Sequence, Chromatography, Gel, Chromatography, Ion Exchange, Electrophoresis, Polyacrylamide Gel, Kinetics, Molecular Sequence Data, Molecular Weight, Substrate Specificity, Ultrafiltration.
Abstract
Phanerochaete chrysosporium is the best studied organism with respect to lignin degradation, but its degradation of the xylan component of lignocellulose is only now being studied. When grown on oat spelt xylan (mainly arabinoxylan), it produces an enzyme with beta-D-xylosidase and beta-D-glucosidase activity. This enzyme was purified by ultrafiltration followed by ammonium sulphate precipitation, anion-exchange chromatography using DEAE Biogel and Mono Q, and gel filtration using Superose 12. It is extracellular, with an apparent M(r) value of 44,500 as determined by SDS-PAGE; the pI is 4.67 and activity is maximal at pH 5 and 60 degrees C. The enzyme is of particular interest because its principal activity is against laminaribiose (3-O-beta-D-glucopyranosyl-D-glucopyranose and laminarin [(1-->3)-beta-D-glucan with ca. 3% of beta-(1-->6) branches] rather than cellobiose and xylobiose. It was competitively inhibited by D-glucono-1,5-lactone and deoxynojirimycin; with p-nitrophenyl beta-D-xylopyranoside as substrate, the Ki values were 32 and 87.5 microM, respectively, and with p-nitrophenyl beta-D-glucopyranoside, they were 35 and 68.7 microM, respectively. The Km values with p-nitrophenyl beta-D-xylopyranoside and p-nitrophenyl beta-D-glucopyranoside as substrates were 3.51 and 5.30 mM, respectively.
DOI: 10.1016/0008-6215(94)80071-5
PubMed: 8156553
Affiliations:
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">A Phanerochaete chrysosporium beta-D-glucosidase/beta-D-xylosidase with specificity for (1-->3)-beta-D-glucan linkages.</title><author><name sortKey="Copa Pati O, J L" sort="Copa Pati O, J L" uniqKey="Copa Pati O J" first="J L" last="Copa-Pati O">J L Copa-Pati O</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry and Applied Molecular Biology, University of Manchester Institute of Science and Technology, United Kingdom.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Department of Biochemistry and Applied Molecular Biology, University of Manchester Institute of Science and Technology</wicri:regionArea><wicri:noRegion>University of Manchester Institute of Science and Technology</wicri:noRegion></affiliation></author><author><name sortKey="Broda, P" sort="Broda, P" uniqKey="Broda P" first="P" last="Broda">P. Broda</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1994">1994</date><idno type="RBID">pubmed:8156553</idno><idno type="pmid">8156553</idno><idno type="doi">10.1016/0008-6215(94)80071-5</idno><idno type="wicri:Area/Main/Corpus">000D64</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000D64</idno><idno type="wicri:Area/Main/Curation">000D64</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000D64</idno><idno type="wicri:Area/Main/Exploration">000D64</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">A Phanerochaete chrysosporium beta-D-glucosidase/beta-D-xylosidase with specificity for (1-->3)-beta-D-glucan linkages.</title><author><name sortKey="Copa Pati O, J L" sort="Copa Pati O, J L" uniqKey="Copa Pati O J" first="J L" last="Copa-Pati O">J L Copa-Pati O</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry and Applied Molecular Biology, University of Manchester Institute of Science and Technology, United Kingdom.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Department of Biochemistry and Applied Molecular Biology, University of Manchester Institute of Science and Technology</wicri:regionArea><wicri:noRegion>University of Manchester Institute of Science and Technology</wicri:noRegion></affiliation></author><author><name sortKey="Broda, P" sort="Broda, P" uniqKey="Broda P" first="P" last="Broda">P. Broda</name></author></analytic><series><title level="j">Carbohydrate research</title><idno type="ISSN">0008-6215</idno><imprint><date when="1994" type="published">1994</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Agaricales (enzymology)</term><term>Carbohydrate Conformation (MeSH)</term><term>Carbohydrate Sequence (MeSH)</term><term>Chromatography, Gel (MeSH)</term><term>Chromatography, Ion Exchange (MeSH)</term><term>Electrophoresis, Polyacrylamide Gel (MeSH)</term><term>Glucans (metabolism)</term><term>Kinetics (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Molecular Weight (MeSH)</term><term>Substrate Specificity (MeSH)</term><term>Ultrafiltration (MeSH)</term><term>Xylosidases (isolation & purification)</term><term>Xylosidases (metabolism)</term><term>beta-Glucosidase (isolation & purification)</term><term>beta-Glucosidase (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Agaricales (enzymologie)</term><term>Chromatographie d'échange d'ions (MeSH)</term><term>Chromatographie sur gel (MeSH)</term><term>Cinétique (MeSH)</term><term>Conformation des glucides (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Glucanes (métabolisme)</term><term>Masse moléculaire (MeSH)</term><term>Spécificité du substrat (MeSH)</term><term>Séquence glucidique (MeSH)</term><term>Ultrafiltration (MeSH)</term><term>Xylosidases (isolement et purification)</term><term>Xylosidases (métabolisme)</term><term>bêta-Glucosidase (isolement et purification)</term><term>bêta-Glucosidase (métabolisme)</term><term>Électrophorèse sur gel de polyacrylamide (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Xylosidases</term><term>beta-Glucosidase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glucans</term><term>Xylosidases</term><term>beta-Glucosidase</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Agaricales</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Agaricales</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Xylosidases</term><term>bêta-Glucosidase</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glucanes</term><term>Xylosidases</term><term>bêta-Glucosidase</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Carbohydrate Conformation</term><term>Carbohydrate Sequence</term><term>Chromatography, Gel</term><term>Chromatography, Ion Exchange</term><term>Electrophoresis, Polyacrylamide Gel</term><term>Kinetics</term><term>Molecular Sequence Data</term><term>Molecular Weight</term><term>Substrate Specificity</term><term>Ultrafiltration</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Chromatographie d'échange d'ions</term><term>Chromatographie sur gel</term><term>Cinétique</term><term>Conformation des glucides</term><term>Données de séquences moléculaires</term><term>Masse moléculaire</term><term>Spécificité du substrat</term><term>Séquence glucidique</term><term>Ultrafiltration</term><term>Électrophorèse sur gel de polyacrylamide</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Phanerochaete chrysosporium is the best studied organism with respect to lignin degradation, but its degradation of the xylan component of lignocellulose is only now being studied. When grown on oat spelt xylan (mainly arabinoxylan), it produces an enzyme with beta-D-xylosidase and beta-D-glucosidase activity. This enzyme was purified by ultrafiltration followed by ammonium sulphate precipitation, anion-exchange chromatography using DEAE Biogel and Mono Q, and gel filtration using Superose 12. It is extracellular, with an apparent M(r) value of 44,500 as determined by SDS-PAGE; the pI is 4.67 and activity is maximal at pH 5 and 60 degrees C. The enzyme is of particular interest because its principal activity is against laminaribiose (3-O-beta-D-glucopyranosyl-D-glucopyranose and laminarin [(1-->3)-beta-D-glucan with ca. 3% of beta-(1-->6) branches] rather than cellobiose and xylobiose. It was competitively inhibited by D-glucono-1,5-lactone and deoxynojirimycin; with p-nitrophenyl beta-D-xylopyranoside as substrate, the Ki values were 32 and 87.5 microM, respectively, and with p-nitrophenyl beta-D-glucopyranoside, they were 35 and 68.7 microM, respectively. The Km values with p-nitrophenyl beta-D-xylopyranoside and p-nitrophenyl beta-D-glucopyranoside as substrates were 3.51 and 5.30 mM, respectively.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">8156553</PMID><DateCompleted><Year>1994</Year><Month>05</Month><Day>18</Day></DateCompleted><DateRevised><Year>2019</Year><Month>08</Month><Day>13</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0008-6215</ISSN><JournalIssue CitedMedium="Print"><Volume>253</Volume><PubDate><Year>1994</Year><Month>Feb</Month><Day>03</Day></PubDate></JournalIssue><Title>Carbohydrate research</Title><ISOAbbreviation>Carbohydr Res</ISOAbbreviation></Journal><ArticleTitle>A Phanerochaete chrysosporium beta-D-glucosidase/beta-D-xylosidase with specificity for (1-->3)-beta-D-glucan linkages.</ArticleTitle><Pagination><MedlinePgn>265-75</MedlinePgn></Pagination><Abstract><AbstractText>Phanerochaete chrysosporium is the best studied organism with respect to lignin degradation, but its degradation of the xylan component of lignocellulose is only now being studied. When grown on oat spelt xylan (mainly arabinoxylan), it produces an enzyme with beta-D-xylosidase and beta-D-glucosidase activity. This enzyme was purified by ultrafiltration followed by ammonium sulphate precipitation, anion-exchange chromatography using DEAE Biogel and Mono Q, and gel filtration using Superose 12. It is extracellular, with an apparent M(r) value of 44,500 as determined by SDS-PAGE; the pI is 4.67 and activity is maximal at pH 5 and 60 degrees C. The enzyme is of particular interest because its principal activity is against laminaribiose (3-O-beta-D-glucopyranosyl-D-glucopyranose and laminarin [(1-->3)-beta-D-glucan with ca. 3% of beta-(1-->6) branches] rather than cellobiose and xylobiose. It was competitively inhibited by D-glucono-1,5-lactone and deoxynojirimycin; with p-nitrophenyl beta-D-xylopyranoside as substrate, the Ki values were 32 and 87.5 microM, respectively, and with p-nitrophenyl beta-D-glucopyranoside, they were 35 and 68.7 microM, respectively. The Km values with p-nitrophenyl beta-D-xylopyranoside and p-nitrophenyl beta-D-glucopyranoside as substrates were 3.51 and 5.30 mM, respectively.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Copa-Patiño</LastName><ForeName>J L</ForeName><Initials>JL</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Applied Molecular Biology, University of Manchester Institute of Science and Technology, United Kingdom.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Broda</LastName><ForeName>P</ForeName><Initials>P</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="D005936">Glucans</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.-</RegistryNumber><NameOfSubstance UI="D014995">Xylosidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.21</RegistryNumber><NameOfSubstance UI="D001617">beta-Glucosidase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.37</RegistryNumber><NameOfSubstance UI="C026579">exo-1,4-beta-D-xylosidase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000363" MajorTopicYN="N">Agaricales</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002236" MajorTopicYN="N">Carbohydrate Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002240" MajorTopicYN="N">Carbohydrate Sequence</DescriptorName></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="D004591" MajorTopicYN="N">Electrophoresis, Polyacrylamide Gel</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005936" MajorTopicYN="N">Glucans</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></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="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014462" MajorTopicYN="N">Ultrafiltration</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014995" MajorTopicYN="N">Xylosidases</DescriptorName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001617" MajorTopicYN="N">beta-Glucosidase</DescriptorName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1994</Year><Month>2</Month><Day>3</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1994</Year><Month>2</Month><Day>3</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1994</Year><Month>2</Month><Day>3</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">8156553</ArticleId><ArticleId IdType="pii">0008-6215(94)80071-5</ArticleId><ArticleId IdType="doi">10.1016/0008-6215(94)80071-5</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Royaume-Uni</li></country></list><tree><noCountry><name sortKey="Broda, P" sort="Broda, P" uniqKey="Broda P" first="P" last="Broda">P. Broda</name></noCountry><country name="Royaume-Uni"><noRegion><name sortKey="Copa Pati O, J L" sort="Copa Pati O, J L" uniqKey="Copa Pati O J" first="J L" last="Copa-Pati O">J L Copa-Pati O</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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