An exo-beta-1,3-galactanase having a novel beta-1,3-galactan-binding module from Phanerochaete chrysosporium.
Identifieur interne : 000858 ( Main/Exploration ); précédent : 000857; suivant : 000859An exo-beta-1,3-galactanase having a novel beta-1,3-galactan-binding module from Phanerochaete chrysosporium.
Auteurs : Hitomi Ichinose [Japon] ; Makoto Yoshida ; Toshihisa Kotake ; Atsushi Kuno ; Kiyohiko Igarashi ; Yoichi Tsumuraya ; Masahiro Samejima ; Jun Hirabayashi ; Hideyuki Kobayashi ; Satoshi KanekoSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 2005.
Descripteurs français
- KwdFr :
- Données de séquences moléculaires (MeSH), Galactanes (métabolisme), Glycosidases (composition chimique), Glycosidases (génétique), Glycosidases (métabolisme), Liaison aux protéines (MeSH), Phanerochaete (enzymologie), Phanerochaete (génétique), Pichia (génétique), Protéines fongiques (composition chimique), Protéines fongiques (génétique), Protéines fongiques (métabolisme), Spécificité du substrat (MeSH), Structure tertiaire des protéines (MeSH), Séquence d'acides aminés (MeSH), Séquence nucléotidique (MeSH).
- MESH :
- composition chimique : Glycosidases, Protéines fongiques.
- enzymologie : Phanerochaete.
- génétique : Glycosidases, Phanerochaete, Pichia, Protéines fongiques.
- métabolisme : Galactanes, Glycosidases, Protéines fongiques.
- Données de séquences moléculaires, Liaison aux protéines, Spécificité du substrat, Structure tertiaire des protéines, Séquence d'acides aminés, Séquence nucléotidique.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Base Sequence (MeSH), Fungal Proteins (chemistry), Fungal Proteins (genetics), Fungal Proteins (metabolism), Galactans (metabolism), Glycoside Hydrolases (chemistry), Glycoside Hydrolases (genetics), Glycoside Hydrolases (metabolism), Molecular Sequence Data (MeSH), Phanerochaete (enzymology), Phanerochaete (genetics), Pichia (genetics), Protein Binding (MeSH), Protein Structure, Tertiary (MeSH), Substrate Specificity (MeSH).
- MESH :
- chemical , chemistry : Fungal Proteins, Glycoside Hydrolases.
- chemical , genetics : Fungal Proteins, Glycoside Hydrolases.
- chemical , metabolism : Fungal Proteins, Galactans, Glycoside Hydrolases.
- enzymology : Phanerochaete.
- genetics : Phanerochaete, Pichia.
- Amino Acid Sequence, Base Sequence, Molecular Sequence Data, Protein Binding, Protein Structure, Tertiary, Substrate Specificity.
Abstract
An exo-beta-1,3-galactanase gene from Phanerochaete chrysosporium has been cloned, sequenced, and expressed in Pichia pastoris. The complete amino acid sequence of the exo-beta-1,3-galactanase indicated that the enzyme consists of an N-terminal catalytic module with similarity to glycoside hydrolase family 43 and an additional unknown functional domain similar to carbohydrate-binding module family 6 (CBM6) in the C-terminal region. The molecular mass of the recombinant enzyme was estimated as 55 kDa based on SDS-PAGE. The enzyme showed reactivity only toward beta-1,3-linked galactosyl oligosaccharides and polysaccharide as substrates but did not hydrolyze beta-1,4-linked galacto-oligosaccharides, beta-1,6-linked galacto-oligosaccharides, pectic galactan, larch arabinogalactan, arabinan, gum arabic, debranched arabinan, laminarin, soluble birchwood xylan, or soluble oat spelled xylan. The enzyme also did not hydrolyze beta-1,3-galactosyl galactosaminide, beta-1,3-galactosyl glucosaminide, or beta-1,3-galactosyl arabinofuranoside, suggesting that it specifically cleaves the internal beta-1,3-linkage of two galactosyl residues. High performance liquid chromatographic analysis of the hydrolysis products showed that the enzyme produced galactose from beta-1,3-galactan in an exo-acting manner. However, no activity toward p-nitrophenyl beta-galactopyranoside was detected. When incubated with arabinogalactan proteins, the enzyme produced oligosaccharides together with galactose, suggesting that it is able to bypass beta-1,6-linked galactosyl side chains. The C-terminal CBM6 did not show any affinity for known substrates of CBM6 such as xylan, cellulose, and beta-1,3-glucan, although it bound beta-1,3-galactan when analyzed by affinity electrophoresis. Frontal affinity chromatography for the CBM6 moiety using several kinds of terminal galactose-containing oligosaccharides as the analytes clearly indicated that the CBM6 specifically interacted with oligosaccharides containing a beta-1,3-galactobiose moiety. When the degree of polymerization of galactose oligomers was increased, the binding affinity of the CBM6 showed no marked change.
DOI: 10.1074/jbc.M501024200
PubMed: 15866877
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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<term>Base Sequence (MeSH)</term>
<term>Fungal Proteins (chemistry)</term>
<term>Fungal Proteins (genetics)</term>
<term>Fungal Proteins (metabolism)</term>
<term>Galactans (metabolism)</term>
<term>Glycoside Hydrolases (chemistry)</term>
<term>Glycoside Hydrolases (genetics)</term>
<term>Glycoside Hydrolases (metabolism)</term>
<term>Molecular Sequence Data (MeSH)</term>
<term>Phanerochaete (enzymology)</term>
<term>Phanerochaete (genetics)</term>
<term>Pichia (genetics)</term>
<term>Protein Binding (MeSH)</term>
<term>Protein Structure, Tertiary (MeSH)</term>
<term>Substrate Specificity (MeSH)</term>
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<term>Glycosidases (composition chimique)</term>
<term>Glycosidases (génétique)</term>
<term>Glycosidases (métabolisme)</term>
<term>Liaison aux protéines (MeSH)</term>
<term>Phanerochaete (enzymologie)</term>
<term>Phanerochaete (génétique)</term>
<term>Pichia (génétique)</term>
<term>Protéines fongiques (composition chimique)</term>
<term>Protéines fongiques (génétique)</term>
<term>Protéines fongiques (métabolisme)</term>
<term>Spécificité du substrat (MeSH)</term>
<term>Structure tertiaire des protéines (MeSH)</term>
<term>Séquence d'acides aminés (MeSH)</term>
<term>Séquence nucléotidique (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Fungal Proteins</term>
<term>Glycoside Hydrolases</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Fungal Proteins</term>
<term>Glycoside Hydrolases</term>
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<term>Glycoside Hydrolases</term>
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<term>Protéines fongiques</term>
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<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Phanerochaete</term>
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<term>Pichia</term>
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<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Glycosidases</term>
<term>Phanerochaete</term>
<term>Pichia</term>
<term>Protéines fongiques</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Galactanes</term>
<term>Glycosidases</term>
<term>Protéines fongiques</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Base Sequence</term>
<term>Molecular Sequence Data</term>
<term>Protein Binding</term>
<term>Protein Structure, Tertiary</term>
<term>Substrate Specificity</term>
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<term>Liaison aux protéines</term>
<term>Spécificité du substrat</term>
<term>Structure tertiaire des protéines</term>
<term>Séquence d'acides aminés</term>
<term>Séquence nucléotidique</term>
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<front><div type="abstract" xml:lang="en">An exo-beta-1,3-galactanase gene from Phanerochaete chrysosporium has been cloned, sequenced, and expressed in Pichia pastoris. The complete amino acid sequence of the exo-beta-1,3-galactanase indicated that the enzyme consists of an N-terminal catalytic module with similarity to glycoside hydrolase family 43 and an additional unknown functional domain similar to carbohydrate-binding module family 6 (CBM6) in the C-terminal region. The molecular mass of the recombinant enzyme was estimated as 55 kDa based on SDS-PAGE. The enzyme showed reactivity only toward beta-1,3-linked galactosyl oligosaccharides and polysaccharide as substrates but did not hydrolyze beta-1,4-linked galacto-oligosaccharides, beta-1,6-linked galacto-oligosaccharides, pectic galactan, larch arabinogalactan, arabinan, gum arabic, debranched arabinan, laminarin, soluble birchwood xylan, or soluble oat spelled xylan. The enzyme also did not hydrolyze beta-1,3-galactosyl galactosaminide, beta-1,3-galactosyl glucosaminide, or beta-1,3-galactosyl arabinofuranoside, suggesting that it specifically cleaves the internal beta-1,3-linkage of two galactosyl residues. High performance liquid chromatographic analysis of the hydrolysis products showed that the enzyme produced galactose from beta-1,3-galactan in an exo-acting manner. However, no activity toward p-nitrophenyl beta-galactopyranoside was detected. When incubated with arabinogalactan proteins, the enzyme produced oligosaccharides together with galactose, suggesting that it is able to bypass beta-1,6-linked galactosyl side chains. The C-terminal CBM6 did not show any affinity for known substrates of CBM6 such as xylan, cellulose, and beta-1,3-glucan, although it bound beta-1,3-galactan when analyzed by affinity electrophoresis. Frontal affinity chromatography for the CBM6 moiety using several kinds of terminal galactose-containing oligosaccharides as the analytes clearly indicated that the CBM6 specifically interacted with oligosaccharides containing a beta-1,3-galactobiose moiety. When the degree of polymerization of galactose oligomers was increased, the binding affinity of the CBM6 showed no marked change.</div>
</front>
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<DateCompleted><Year>2005</Year>
<Month>08</Month>
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<Title>The Journal of biological chemistry</Title>
<ISOAbbreviation>J Biol Chem</ISOAbbreviation>
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<ArticleTitle>An exo-beta-1,3-galactanase having a novel beta-1,3-galactan-binding module from Phanerochaete chrysosporium.</ArticleTitle>
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<Abstract><AbstractText>An exo-beta-1,3-galactanase gene from Phanerochaete chrysosporium has been cloned, sequenced, and expressed in Pichia pastoris. The complete amino acid sequence of the exo-beta-1,3-galactanase indicated that the enzyme consists of an N-terminal catalytic module with similarity to glycoside hydrolase family 43 and an additional unknown functional domain similar to carbohydrate-binding module family 6 (CBM6) in the C-terminal region. The molecular mass of the recombinant enzyme was estimated as 55 kDa based on SDS-PAGE. The enzyme showed reactivity only toward beta-1,3-linked galactosyl oligosaccharides and polysaccharide as substrates but did not hydrolyze beta-1,4-linked galacto-oligosaccharides, beta-1,6-linked galacto-oligosaccharides, pectic galactan, larch arabinogalactan, arabinan, gum arabic, debranched arabinan, laminarin, soluble birchwood xylan, or soluble oat spelled xylan. The enzyme also did not hydrolyze beta-1,3-galactosyl galactosaminide, beta-1,3-galactosyl glucosaminide, or beta-1,3-galactosyl arabinofuranoside, suggesting that it specifically cleaves the internal beta-1,3-linkage of two galactosyl residues. High performance liquid chromatographic analysis of the hydrolysis products showed that the enzyme produced galactose from beta-1,3-galactan in an exo-acting manner. However, no activity toward p-nitrophenyl beta-galactopyranoside was detected. When incubated with arabinogalactan proteins, the enzyme produced oligosaccharides together with galactose, suggesting that it is able to bypass beta-1,6-linked galactosyl side chains. The C-terminal CBM6 did not show any affinity for known substrates of CBM6 such as xylan, cellulose, and beta-1,3-glucan, although it bound beta-1,3-galactan when analyzed by affinity electrophoresis. Frontal affinity chromatography for the CBM6 moiety using several kinds of terminal galactose-containing oligosaccharides as the analytes clearly indicated that the CBM6 specifically interacted with oligosaccharides containing a beta-1,3-galactobiose moiety. When the degree of polymerization of galactose oligomers was increased, the binding affinity of the CBM6 showed no marked change.</AbstractText>
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<ForeName>Hitomi</ForeName>
<Initials>H</Initials>
<AffiliationInfo><Affiliation>Biological Function Division, National Food Research Institute, 2-1-12 Kannondai, Tsukuba, Ibaraki 305-8642, Japan.</Affiliation>
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<ForeName>Makoto</ForeName>
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<Author ValidYN="Y"><LastName>Kotake</LastName>
<ForeName>Toshihisa</ForeName>
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<ForeName>Atsushi</ForeName>
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<ForeName>Yoichi</ForeName>
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</list>
<tree><noCountry><name sortKey="Hirabayashi, Jun" sort="Hirabayashi, Jun" uniqKey="Hirabayashi J" first="Jun" last="Hirabayashi">Jun Hirabayashi</name>
<name sortKey="Igarashi, Kiyohiko" sort="Igarashi, Kiyohiko" uniqKey="Igarashi K" first="Kiyohiko" last="Igarashi">Kiyohiko Igarashi</name>
<name sortKey="Kaneko, Satoshi" sort="Kaneko, Satoshi" uniqKey="Kaneko S" first="Satoshi" last="Kaneko">Satoshi Kaneko</name>
<name sortKey="Kobayashi, Hideyuki" sort="Kobayashi, Hideyuki" uniqKey="Kobayashi H" first="Hideyuki" last="Kobayashi">Hideyuki Kobayashi</name>
<name sortKey="Kotake, Toshihisa" sort="Kotake, Toshihisa" uniqKey="Kotake T" first="Toshihisa" last="Kotake">Toshihisa Kotake</name>
<name sortKey="Kuno, Atsushi" sort="Kuno, Atsushi" uniqKey="Kuno A" first="Atsushi" last="Kuno">Atsushi Kuno</name>
<name sortKey="Samejima, Masahiro" sort="Samejima, Masahiro" uniqKey="Samejima M" first="Masahiro" last="Samejima">Masahiro Samejima</name>
<name sortKey="Tsumuraya, Yoichi" sort="Tsumuraya, Yoichi" uniqKey="Tsumuraya Y" first="Yoichi" last="Tsumuraya">Yoichi Tsumuraya</name>
<name sortKey="Yoshida, Makoto" sort="Yoshida, Makoto" uniqKey="Yoshida M" first="Makoto" last="Yoshida">Makoto Yoshida</name>
</noCountry>
<country name="Japon"><noRegion><name sortKey="Ichinose, Hitomi" sort="Ichinose, Hitomi" uniqKey="Ichinose H" first="Hitomi" last="Ichinose">Hitomi Ichinose</name>
</noRegion>
</country>
</tree>
</affiliations>
</record>
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