Serveur d'exploration sur le phanerochaete

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Hydrolysis of beta-1,3/1,6-glucan by glycoside hydrolase family 16 endo-1,3(4)-beta-glucanase from the basidiomycete Phanerochaete chrysosporium.

Identifieur interne : 000773 ( Main/Exploration ); précédent : 000772; suivant : 000774

Hydrolysis of beta-1,3/1,6-glucan by glycoside hydrolase family 16 endo-1,3(4)-beta-glucanase from the basidiomycete Phanerochaete chrysosporium.

Auteurs : Rie Kawai [Japon] ; Kiyohiko Igarashi ; Makoto Yoshida ; Motomitsu Kitaoka ; Masahiro Samejima

Source :

RBID : pubmed:16374635

Descripteurs français

English descriptors

Abstract

When Phanerochaete chrysosporium was grown with laminarin (a beta-1,3/1,6-glucan) as the sole carbon source, a beta-1,3-glucanase with a molecular mass of 36 kDa was produced as a major extracellular protein. The cDNA encoding this enzyme was cloned, and the deduced amino acid sequence revealed that this enzyme belongs to glycoside hydrolase family 16; it was named Lam16A. Recombinant Lam16A, expressed in the methylotrophic yeast Pichia pastoris, randomly hydrolyzes linear beta-1,3-glucan, branched beta-1,3/1,6-glucan, and beta-1,3-1,4-glucan, suggesting that the enzyme is a typical endo-1,3(4)-beta-glucanase (EC 3.2.1.6) with broad substrate specificity for beta-1,3-glucans. When laminarin and lichenan were used as substrates, Lam16A produced 6-O-glucosyl-laminaritriose (beta-D-Glcp-(1->6)-beta-D-Glcp-(1->3)-beta-D-Glcp-(1->3)-D-Glc) and 4-O-glucosyl-laminaribiose (beta-D-Glcp-(1->4)-beta-D-Glcp-(1->3)-D-Glc), respectively, as one of the major products. These results suggested that the enzyme strictly recognizes beta-D-Glcp-(1->3)-D-Glcp at subsites -2 and -1, whereas it permits 6-O-glucosyl substitution at subsite +1 and a beta-1,4-glucosidic linkage at the catalytic site. Consequently, Lam16A generates non-branched oligosaccharide from branched beta-1,3/1,6-glucan and, thus, may contribute to the effective degradation of such molecules in combination with other extracellular beta-1,3-glucanases.

DOI: 10.1007/s00253-005-0214-4
PubMed: 16374635


Affiliations:


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Le document en format XML

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<term>Amino Acid Sequence (MeSH)</term>
<term>Base Sequence (MeSH)</term>
<term>Carbohydrate Sequence (MeSH)</term>
<term>Cellulase (genetics)</term>
<term>Cellulase (isolation & purification)</term>
<term>Cellulase (metabolism)</term>
<term>Chromatography, Thin Layer (methods)</term>
<term>Cloning, Molecular (methods)</term>
<term>DNA, Complementary (chemistry)</term>
<term>DNA, Complementary (genetics)</term>
<term>Electrophoresis, Polyacrylamide Gel (methods)</term>
<term>Fungal Proteins (genetics)</term>
<term>Fungal Proteins (isolation & purification)</term>
<term>Fungal Proteins (metabolism)</term>
<term>Glycoside Hydrolases (genetics)</term>
<term>Glycoside Hydrolases (isolation & purification)</term>
<term>Glycoside Hydrolases (metabolism)</term>
<term>Hydrolysis (MeSH)</term>
<term>Molecular Sequence Data (MeSH)</term>
<term>Molecular Structure (MeSH)</term>
<term>Phanerochaete (enzymology)</term>
<term>Phanerochaete (genetics)</term>
<term>Phanerochaete (metabolism)</term>
<term>Pichia (genetics)</term>
<term>Sequence Alignment (MeSH)</term>
<term>Sequence Analysis, DNA (MeSH)</term>
<term>Sequence Homology, Amino Acid (MeSH)</term>
<term>beta-Glucans (chemistry)</term>
<term>beta-Glucans (metabolism)</term>
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<term>ADN complémentaire (composition chimique)</term>
<term>ADN complémentaire (génétique)</term>
<term>Alignement de séquences (MeSH)</term>
<term>Analyse de séquence d'ADN (MeSH)</term>
<term>Cellulase (génétique)</term>
<term>Cellulase (isolement et purification)</term>
<term>Cellulase (métabolisme)</term>
<term>Chromatographie sur couche mince (méthodes)</term>
<term>Clonage moléculaire (méthodes)</term>
<term>Données de séquences moléculaires (MeSH)</term>
<term>Glycosidases (génétique)</term>
<term>Glycosidases (isolement et purification)</term>
<term>Glycosidases (métabolisme)</term>
<term>Hydrolyse (MeSH)</term>
<term>Phanerochaete (enzymologie)</term>
<term>Phanerochaete (génétique)</term>
<term>Phanerochaete (métabolisme)</term>
<term>Pichia (génétique)</term>
<term>Protéines fongiques (génétique)</term>
<term>Protéines fongiques (isolement et purification)</term>
<term>Protéines fongiques (métabolisme)</term>
<term>Similitude de séquences d'acides aminés (MeSH)</term>
<term>Structure moléculaire (MeSH)</term>
<term>Séquence d'acides aminés (MeSH)</term>
<term>Séquence glucidique (MeSH)</term>
<term>Séquence nucléotidique (MeSH)</term>
<term>bêta-Glucanes (composition chimique)</term>
<term>bêta-Glucanes (métabolisme)</term>
<term>Électrophorèse sur gel de polyacrylamide (méthodes)</term>
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<term>DNA, Complementary</term>
<term>beta-Glucans</term>
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<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en">
<term>Cellulase</term>
<term>DNA, Complementary</term>
<term>Fungal Proteins</term>
<term>Glycoside Hydrolases</term>
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<keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en">
<term>Cellulase</term>
<term>Fungal Proteins</term>
<term>Glycoside Hydrolases</term>
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<term>Cellulase</term>
<term>Fungal Proteins</term>
<term>Glycoside Hydrolases</term>
<term>beta-Glucans</term>
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<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr">
<term>ADN complémentaire</term>
<term>bêta-Glucanes</term>
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<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr">
<term>Phanerochaete</term>
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<keywords scheme="MESH" qualifier="enzymology" xml:lang="en">
<term>Phanerochaete</term>
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<keywords scheme="MESH" qualifier="genetics" xml:lang="en">
<term>Phanerochaete</term>
<term>Pichia</term>
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<keywords scheme="MESH" qualifier="génétique" xml:lang="fr">
<term>ADN complémentaire</term>
<term>Cellulase</term>
<term>Glycosidases</term>
<term>Phanerochaete</term>
<term>Pichia</term>
<term>Protéines fongiques</term>
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<keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr">
<term>Cellulase</term>
<term>Glycosidases</term>
<term>Protéines fongiques</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en">
<term>Phanerochaete</term>
</keywords>
<keywords scheme="MESH" qualifier="methods" xml:lang="en">
<term>Chromatography, Thin Layer</term>
<term>Cloning, Molecular</term>
<term>Electrophoresis, Polyacrylamide Gel</term>
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<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr">
<term>Cellulase</term>
<term>Glycosidases</term>
<term>Phanerochaete</term>
<term>Protéines fongiques</term>
<term>bêta-Glucanes</term>
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<keywords scheme="MESH" qualifier="méthodes" xml:lang="fr">
<term>Chromatographie sur couche mince</term>
<term>Clonage moléculaire</term>
<term>Électrophorèse sur gel de polyacrylamide</term>
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<term>Amino Acid Sequence</term>
<term>Base Sequence</term>
<term>Carbohydrate Sequence</term>
<term>Hydrolysis</term>
<term>Molecular Sequence Data</term>
<term>Molecular Structure</term>
<term>Sequence Alignment</term>
<term>Sequence Analysis, DNA</term>
<term>Sequence Homology, Amino Acid</term>
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<term>Alignement de séquences</term>
<term>Analyse de séquence d'ADN</term>
<term>Données de séquences moléculaires</term>
<term>Hydrolyse</term>
<term>Similitude de séquences d'acides aminés</term>
<term>Structure moléculaire</term>
<term>Séquence d'acides aminés</term>
<term>Séquence glucidique</term>
<term>Séquence nucléotidique</term>
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<div type="abstract" xml:lang="en">When Phanerochaete chrysosporium was grown with laminarin (a beta-1,3/1,6-glucan) as the sole carbon source, a beta-1,3-glucanase with a molecular mass of 36 kDa was produced as a major extracellular protein. The cDNA encoding this enzyme was cloned, and the deduced amino acid sequence revealed that this enzyme belongs to glycoside hydrolase family 16; it was named Lam16A. Recombinant Lam16A, expressed in the methylotrophic yeast Pichia pastoris, randomly hydrolyzes linear beta-1,3-glucan, branched beta-1,3/1,6-glucan, and beta-1,3-1,4-glucan, suggesting that the enzyme is a typical endo-1,3(4)-beta-glucanase (EC 3.2.1.6) with broad substrate specificity for beta-1,3-glucans. When laminarin and lichenan were used as substrates, Lam16A produced 6-O-glucosyl-laminaritriose (beta-D-Glcp-(1->6)-beta-D-Glcp-(1->3)-beta-D-Glcp-(1->3)-D-Glc) and 4-O-glucosyl-laminaribiose (beta-D-Glcp-(1->4)-beta-D-Glcp-(1->3)-D-Glc), respectively, as one of the major products. These results suggested that the enzyme strictly recognizes beta-D-Glcp-(1->3)-D-Glcp at subsites -2 and -1, whereas it permits 6-O-glucosyl substitution at subsite +1 and a beta-1,4-glucosidic linkage at the catalytic site. Consequently, Lam16A generates non-branched oligosaccharide from branched beta-1,3/1,6-glucan and, thus, may contribute to the effective degradation of such molecules in combination with other extracellular beta-1,3-glucanases.</div>
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<ArticleTitle>Hydrolysis of beta-1,3/1,6-glucan by glycoside hydrolase family 16 endo-1,3(4)-beta-glucanase from the basidiomycete Phanerochaete chrysosporium.</ArticleTitle>
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<Abstract>
<AbstractText>When Phanerochaete chrysosporium was grown with laminarin (a beta-1,3/1,6-glucan) as the sole carbon source, a beta-1,3-glucanase with a molecular mass of 36 kDa was produced as a major extracellular protein. The cDNA encoding this enzyme was cloned, and the deduced amino acid sequence revealed that this enzyme belongs to glycoside hydrolase family 16; it was named Lam16A. Recombinant Lam16A, expressed in the methylotrophic yeast Pichia pastoris, randomly hydrolyzes linear beta-1,3-glucan, branched beta-1,3/1,6-glucan, and beta-1,3-1,4-glucan, suggesting that the enzyme is a typical endo-1,3(4)-beta-glucanase (EC 3.2.1.6) with broad substrate specificity for beta-1,3-glucans. When laminarin and lichenan were used as substrates, Lam16A produced 6-O-glucosyl-laminaritriose (beta-D-Glcp-(1->6)-beta-D-Glcp-(1->3)-beta-D-Glcp-(1->3)-D-Glc) and 4-O-glucosyl-laminaribiose (beta-D-Glcp-(1->4)-beta-D-Glcp-(1->3)-D-Glc), respectively, as one of the major products. These results suggested that the enzyme strictly recognizes beta-D-Glcp-(1->3)-D-Glcp at subsites -2 and -1, whereas it permits 6-O-glucosyl substitution at subsite +1 and a beta-1,4-glucosidic linkage at the catalytic site. Consequently, Lam16A generates non-branched oligosaccharide from branched beta-1,3/1,6-glucan and, thus, may contribute to the effective degradation of such molecules in combination with other extracellular beta-1,3-glucanases.</AbstractText>
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<Affiliation>Department of Biomaterials Sciences, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo, 113-8657, Japan.</Affiliation>
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<Initials>M</Initials>
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<DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName>
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<DescriptorName UI="D002240" MajorTopicYN="N">Carbohydrate Sequence</DescriptorName>
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<DescriptorName UI="D002480" MajorTopicYN="N">Cellulase</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName>
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<DescriptorName UI="D047071" MajorTopicYN="N">beta-Glucans</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
</MeshHeadingList>
</MedlineCitation>
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<PubMedPubDate PubStatus="received">
<Year>2005</Year>
<Month>09</Month>
<Day>08</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="accepted">
<Year>2005</Year>
<Month>10</Month>
<Day>10</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="revised">
<Year>2005</Year>
<Month>10</Month>
<Day>07</Day>
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<PubMedPubDate PubStatus="pubmed">
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<PubMedPubDate PubStatus="medline">
<Year>2006</Year>
<Month>10</Month>
<Day>13</Day>
<Hour>9</Hour>
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<PubMedPubDate PubStatus="entrez">
<Year>2005</Year>
<Month>12</Month>
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<PublicationStatus>ppublish</PublicationStatus>
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<ArticleId IdType="pubmed">16374635</ArticleId>
<ArticleId IdType="doi">10.1007/s00253-005-0214-4</ArticleId>
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</pubmed>
<affiliations>
<list>
<country>
<li>Japon</li>
</country>
<region>
<li>Région de Kantō</li>
</region>
<settlement>
<li>Tokyo</li>
</settlement>
<orgName>
<li>Université de Tokyo</li>
</orgName>
</list>
<tree>
<noCountry>
<name sortKey="Igarashi, Kiyohiko" sort="Igarashi, Kiyohiko" uniqKey="Igarashi K" first="Kiyohiko" last="Igarashi">Kiyohiko Igarashi</name>
<name sortKey="Kitaoka, Motomitsu" sort="Kitaoka, Motomitsu" uniqKey="Kitaoka M" first="Motomitsu" last="Kitaoka">Motomitsu Kitaoka</name>
<name sortKey="Samejima, Masahiro" sort="Samejima, Masahiro" uniqKey="Samejima M" first="Masahiro" last="Samejima">Masahiro Samejima</name>
<name sortKey="Yoshida, Makoto" sort="Yoshida, Makoto" uniqKey="Yoshida M" first="Makoto" last="Yoshida">Makoto Yoshida</name>
</noCountry>
<country name="Japon">
<region name="Région de Kantō">
<name sortKey="Kawai, Rie" sort="Kawai, Rie" uniqKey="Kawai R" first="Rie" last="Kawai">Rie Kawai</name>
</region>
</country>
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</affiliations>
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   |texte=   Hydrolysis of beta-1,3/1,6-glucan by glycoside hydrolase family 16 endo-1,3(4)-beta-glucanase from the basidiomycete Phanerochaete chrysosporium.
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