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 : 000803 ( Main/Corpus ); précédent : 000802; suivant : 000804Hydrolysis 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 ; Kiyohiko Igarashi ; Makoto Yoshida ; Motomitsu Kitaoka ; Masahiro SamejimaSource :
- Applied microbiology and biotechnology [ 0175-7598 ] ; 2006.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Base Sequence (MeSH), Carbohydrate Sequence (MeSH), Cellulase (genetics), Cellulase (isolation & purification), Cellulase (metabolism), Chromatography, Thin Layer (methods), Cloning, Molecular (methods), DNA, Complementary (chemistry), DNA, Complementary (genetics), Electrophoresis, Polyacrylamide Gel (methods), Fungal Proteins (genetics), Fungal Proteins (isolation & purification), Fungal Proteins (metabolism), Glycoside Hydrolases (genetics), Glycoside Hydrolases (isolation & purification), Glycoside Hydrolases (metabolism), Hydrolysis (MeSH), Molecular Sequence Data (MeSH), Molecular Structure (MeSH), Phanerochaete (enzymology), Phanerochaete (genetics), Phanerochaete (metabolism), Pichia (genetics), Sequence Alignment (MeSH), Sequence Analysis, DNA (MeSH), Sequence Homology, Amino Acid (MeSH), beta-Glucans (chemistry), beta-Glucans (metabolism).
- MESH :
- chemical , chemistry : DNA, Complementary, beta-Glucans.
- chemical , genetics : Cellulase, DNA, Complementary, Fungal Proteins, Glycoside Hydrolases.
- chemical , isolation & purification : Cellulase, Fungal Proteins, Glycoside Hydrolases.
- chemical , metabolism : Cellulase, Fungal Proteins, Glycoside Hydrolases, beta-Glucans.
- enzymology : Phanerochaete.
- genetics : Phanerochaete, Pichia.
- metabolism : Phanerochaete.
- methods : Chromatography, Thin Layer, Cloning, Molecular, Electrophoresis, Polyacrylamide Gel.
- Amino Acid Sequence, Base Sequence, Carbohydrate Sequence, Hydrolysis, Molecular Sequence Data, Molecular Structure, Sequence Alignment, Sequence Analysis, DNA, Sequence Homology, Amino Acid.
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
Links to Exploration step
pubmed:16374635Le document en format XML
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<author><name sortKey="Kawai, Rie" sort="Kawai, Rie" uniqKey="Kawai R" first="Rie" last="Kawai">Rie Kawai</name>
<affiliation><nlm: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.</nlm:affiliation>
</affiliation>
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<author><name sortKey="Igarashi, Kiyohiko" sort="Igarashi, Kiyohiko" uniqKey="Igarashi K" first="Kiyohiko" last="Igarashi">Kiyohiko Igarashi</name>
</author>
<author><name sortKey="Yoshida, Makoto" sort="Yoshida, Makoto" uniqKey="Yoshida M" first="Makoto" last="Yoshida">Makoto Yoshida</name>
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<author><name sortKey="Kitaoka, Motomitsu" sort="Kitaoka, Motomitsu" uniqKey="Kitaoka M" first="Motomitsu" last="Kitaoka">Motomitsu Kitaoka</name>
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<author><name sortKey="Samejima, Masahiro" sort="Samejima, Masahiro" uniqKey="Samejima M" first="Masahiro" last="Samejima">Masahiro Samejima</name>
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<sourceDesc><biblStruct><analytic><title xml:lang="en">Hydrolysis of beta-1,3/1,6-glucan by glycoside hydrolase family 16 endo-1,3(4)-beta-glucanase from the basidiomycete Phanerochaete chrysosporium.</title>
<author><name sortKey="Kawai, Rie" sort="Kawai, Rie" uniqKey="Kawai R" first="Rie" last="Kawai">Rie Kawai</name>
<affiliation><nlm: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.</nlm:affiliation>
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<author><name sortKey="Igarashi, Kiyohiko" sort="Igarashi, Kiyohiko" uniqKey="Igarashi K" first="Kiyohiko" last="Igarashi">Kiyohiko Igarashi</name>
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<author><name sortKey="Yoshida, Makoto" sort="Yoshida, Makoto" uniqKey="Yoshida M" first="Makoto" last="Yoshida">Makoto Yoshida</name>
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<author><name sortKey="Kitaoka, Motomitsu" sort="Kitaoka, Motomitsu" uniqKey="Kitaoka M" first="Motomitsu" last="Kitaoka">Motomitsu Kitaoka</name>
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<author><name sortKey="Samejima, Masahiro" sort="Samejima, Masahiro" uniqKey="Samejima M" first="Masahiro" last="Samejima">Masahiro Samejima</name>
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<series><title level="j">Applied microbiology and biotechnology</title>
<idno type="ISSN">0175-7598</idno>
<imprint><date when="2006" type="published">2006</date>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><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>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>DNA, Complementary</term>
<term>beta-Glucans</term>
</keywords>
<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>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Cellulase</term>
<term>Fungal Proteins</term>
<term>Glycoside Hydrolases</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cellulase</term>
<term>Fungal Proteins</term>
<term>Glycoside Hydrolases</term>
<term>beta-Glucans</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Phanerochaete</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Phanerochaete</term>
<term>Pichia</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>
</keywords>
<keywords scheme="MESH" xml:lang="en"><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>
</keywords>
</textClass>
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<front><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>
</front>
</TEI>
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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>
</Abstract>
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<AffiliationInfo><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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