Recombinant expression and enzymatic characterization of PttCel9A, a KOR homologue from Populus tremula x tremuloides.
Identifieur interne : 004205 ( Main/Exploration ); précédent : 004204; suivant : 004206Recombinant expression and enzymatic characterization of PttCel9A, a KOR homologue from Populus tremula x tremuloides.
Auteurs : Emma R. Master [Suède] ; Ulla J. Rudsander ; Weilin Zhou ; Hongbin Henriksson ; Christina Divne ; Stuart Denman ; David B. Wilson ; Tuula T. TeeriSource :
- Biochemistry [ 0006-2960 ] ; 2004.
Descripteurs français
- KwdFr :
- Arabidopsis (enzymologie), Cations divalents (métabolisme), Cellulose (analogues et dérivés), Cellulose (métabolisme), Chlorure de calcium (métabolisme), Chlorures (métabolisme), Cinétique (MeSH), Composés du zinc (métabolisme), Concentration en ions d'hydrogène (MeSH), Données de séquences moléculaires (MeSH), Hydrolyse (MeSH), Mutagenèse dirigée (MeSH), N-Glycosyl hydrolases (biosynthèse), N-Glycosyl hydrolases (génétique), N-Glycosyl hydrolases (isolement et purification), N-Glycosyl hydrolases (métabolisme), Oligosaccharides (métabolisme), Pichia (enzymologie), Pichia (génétique), Polymères (métabolisme), Populus (enzymologie), Populus (génétique), Protéines recombinantes (biosynthèse), Protéines recombinantes (composition chimique), Protéines végétales (biosynthèse), Protéines végétales (génétique), Protéines végétales (isolement et purification), Protéines végétales (métabolisme), Similitude de séquences d'acides aminés (MeSH), Spécificité du substrat (MeSH), Séquence d'acides aminés (MeSH), Tétroses (métabolisme).
- MESH :
- analogues et dérivés : Cellulose.
- biosynthèse : N-Glycosyl hydrolases, Protéines recombinantes, Protéines végétales.
- composition chimique : Protéines recombinantes.
- enzymologie : Arabidopsis, Pichia, Populus.
- génétique : N-Glycosyl hydrolases, Pichia, Populus, Protéines végétales.
- isolement et purification : N-Glycosyl hydrolases, Protéines végétales.
- métabolisme : Cations divalents, Cellulose, Chlorure de calcium, Chlorures, Composés du zinc, N-Glycosyl hydrolases, Oligosaccharides, Polymères, Protéines végétales, Tétroses.
- Cinétique, Concentration en ions d'hydrogène, Données de séquences moléculaires, Hydrolyse, Mutagenèse dirigée, Similitude de séquences d'acides aminés, Spécificité du substrat, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Arabidopsis (enzymology), Calcium Chloride (metabolism), Cations, Divalent (metabolism), Cellulose (analogs & derivatives), Cellulose (metabolism), Chlorides (metabolism), Hydrogen-Ion Concentration (MeSH), Hydrolysis (MeSH), Kinetics (MeSH), Molecular Sequence Data (MeSH), Mutagenesis, Site-Directed (MeSH), N-Glycosyl Hydrolases (biosynthesis), N-Glycosyl Hydrolases (genetics), N-Glycosyl Hydrolases (isolation & purification), N-Glycosyl Hydrolases (metabolism), Oligosaccharides (metabolism), Pichia (enzymology), Pichia (genetics), Plant Proteins (biosynthesis), Plant Proteins (genetics), Plant Proteins (isolation & purification), Plant Proteins (metabolism), Polymers (metabolism), Populus (enzymology), Populus (genetics), Recombinant Proteins (biosynthesis), Recombinant Proteins (chemistry), Sequence Homology, Amino Acid (MeSH), Substrate Specificity (MeSH), Tetroses (metabolism), Zinc Compounds (metabolism).
- MESH :
- chemical , analogs & derivatives : Cellulose.
- chemical , biosynthesis : N-Glycosyl Hydrolases, Plant Proteins, Recombinant Proteins.
- chemical , chemistry : Recombinant Proteins.
- chemical , genetics : N-Glycosyl Hydrolases, Plant Proteins.
- chemical , isolation & purification : N-Glycosyl Hydrolases, Plant Proteins.
- chemical , metabolism : Calcium Chloride, Cations, Divalent, Cellulose, Chlorides, N-Glycosyl Hydrolases, Oligosaccharides, Plant Proteins, Polymers, Tetroses, Zinc Compounds.
- enzymology : Arabidopsis, Pichia, Populus.
- genetics : Pichia, Populus.
- Amino Acid Sequence, Hydrogen-Ion Concentration, Hydrolysis, Kinetics, Molecular Sequence Data, Mutagenesis, Site-Directed, Sequence Homology, Amino Acid, Substrate Specificity.
Abstract
PttCel9A is a membrane-bound, family 9 glycosyl hydrolase from Populus tremula x tremuloides that is upregulated during secondary cell wall synthesis. The catalytic domain of PttCel9A, Delta(1-105)PttCel9A, was purified, and its activity was compared to TfCel9A and TfCel9B from Thermobifida fusca. Since aromatic amino acids involved in substrate binding at subsites -4, -3, and -2 are missing in PttCel9A, the activity of TfCel9A mutant enzymes W256S, W209A, and W313G was also investigated. Delta(1-105)PttCel9A hydrolyzed a comparatively narrow range of polymeric substrates, and the preferred substrate was (carboxymethyl)cellulose 4M. Moreover, Delta(1-105)PttCel9A did not hydrolyze oligosaccharides shorter than cellopentaose, whereas TfCel9A and TfCel9B hydrolyzed cellotetraose and cellotriose, respectively. These data suggest that the preferred substrates of PttCel9A are long, low-substituted, soluble cellulosic polymers. At 30 degrees C and pH 6.0, the kcat for cellohexaose of Delta(1-105)PttCel9A, TfCel9A, and TfCel9B were 0.023 +/- 0.001, 16.9 +/- 2.0, and 1.3 +/- 0.2, respectively. The catalytic efficiency (kcat/Km) of TfCel9B was 39% of that of TfCel9A, whereas the catalytic efficiency of Delta(1-105)PttCel9A was 0.04% of that of TfCel9A. Removing tryptophan residues at subsites -4, -3, and -2 decreased the efficiency of cellohexaose hydrolysis by TfCel9A. Mutation of W313 to G had the most drastic effect, producing a mutant enzyme with 1% of the catalytic efficiency of TfCel9A. The apparent narrow substrate range and catalytic efficiency of PttCel9A are correlated with a lack of aromatic amino acids in the substrate binding cleft and may be necessary to prevent excessive hydrolysis of cell wall polysaccharides during cell wall formation.
DOI: 10.1021/bi049453x
PubMed: 15287736
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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<term>Arabidopsis (enzymology)</term>
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<term>Cations, Divalent (metabolism)</term>
<term>Cellulose (analogs & derivatives)</term>
<term>Cellulose (metabolism)</term>
<term>Chlorides (metabolism)</term>
<term>Hydrogen-Ion Concentration (MeSH)</term>
<term>Hydrolysis (MeSH)</term>
<term>Kinetics (MeSH)</term>
<term>Molecular Sequence Data (MeSH)</term>
<term>Mutagenesis, Site-Directed (MeSH)</term>
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<term>N-Glycosyl Hydrolases (genetics)</term>
<term>N-Glycosyl Hydrolases (isolation & purification)</term>
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<term>Tetroses (metabolism)</term>
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<term>Chlorure de calcium (métabolisme)</term>
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<term>Composés du zinc (métabolisme)</term>
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<term>N-Glycosyl hydrolases (génétique)</term>
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<term>Oligosaccharides (métabolisme)</term>
<term>Pichia (enzymologie)</term>
<term>Pichia (génétique)</term>
<term>Polymères (métabolisme)</term>
<term>Populus (enzymologie)</term>
<term>Populus (génétique)</term>
<term>Protéines recombinantes (biosynthèse)</term>
<term>Protéines recombinantes (composition chimique)</term>
<term>Protéines végétales (biosynthèse)</term>
<term>Protéines végétales (génétique)</term>
<term>Protéines végétales (isolement et purification)</term>
<term>Protéines végétales (métabolisme)</term>
<term>Similitude de séquences d'acides aminés (MeSH)</term>
<term>Spécificité du substrat (MeSH)</term>
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<term>Plant Proteins</term>
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<term>Tetroses</term>
<term>Zinc Compounds</term>
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<term>Protéines végétales</term>
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<term>Hydrogen-Ion Concentration</term>
<term>Hydrolysis</term>
<term>Kinetics</term>
<term>Molecular Sequence Data</term>
<term>Mutagenesis, Site-Directed</term>
<term>Sequence Homology, Amino Acid</term>
<term>Substrate Specificity</term>
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<term>Concentration en ions d'hydrogène</term>
<term>Données de séquences moléculaires</term>
<term>Hydrolyse</term>
<term>Mutagenèse dirigée</term>
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<front><div type="abstract" xml:lang="en">PttCel9A is a membrane-bound, family 9 glycosyl hydrolase from Populus tremula x tremuloides that is upregulated during secondary cell wall synthesis. The catalytic domain of PttCel9A, Delta(1-105)PttCel9A, was purified, and its activity was compared to TfCel9A and TfCel9B from Thermobifida fusca. Since aromatic amino acids involved in substrate binding at subsites -4, -3, and -2 are missing in PttCel9A, the activity of TfCel9A mutant enzymes W256S, W209A, and W313G was also investigated. Delta(1-105)PttCel9A hydrolyzed a comparatively narrow range of polymeric substrates, and the preferred substrate was (carboxymethyl)cellulose 4M. Moreover, Delta(1-105)PttCel9A did not hydrolyze oligosaccharides shorter than cellopentaose, whereas TfCel9A and TfCel9B hydrolyzed cellotetraose and cellotriose, respectively. These data suggest that the preferred substrates of PttCel9A are long, low-substituted, soluble cellulosic polymers. At 30 degrees C and pH 6.0, the kcat for cellohexaose of Delta(1-105)PttCel9A, TfCel9A, and TfCel9B were 0.023 +/- 0.001, 16.9 +/- 2.0, and 1.3 +/- 0.2, respectively. The catalytic efficiency (kcat/Km) of TfCel9B was 39% of that of TfCel9A, whereas the catalytic efficiency of Delta(1-105)PttCel9A was 0.04% of that of TfCel9A. Removing tryptophan residues at subsites -4, -3, and -2 decreased the efficiency of cellohexaose hydrolysis by TfCel9A. Mutation of W313 to G had the most drastic effect, producing a mutant enzyme with 1% of the catalytic efficiency of TfCel9A. The apparent narrow substrate range and catalytic efficiency of PttCel9A are correlated with a lack of aromatic amino acids in the substrate binding cleft and may be necessary to prevent excessive hydrolysis of cell wall polysaccharides during cell wall formation.</div>
</front>
</TEI>
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<DateCompleted><Year>2004</Year>
<Month>09</Month>
<Day>30</Day>
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<DateRevised><Year>2013</Year>
<Month>11</Month>
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<Title>Biochemistry</Title>
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<ArticleTitle>Recombinant expression and enzymatic characterization of PttCel9A, a KOR homologue from Populus tremula x tremuloides.</ArticleTitle>
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<Abstract><AbstractText>PttCel9A is a membrane-bound, family 9 glycosyl hydrolase from Populus tremula x tremuloides that is upregulated during secondary cell wall synthesis. The catalytic domain of PttCel9A, Delta(1-105)PttCel9A, was purified, and its activity was compared to TfCel9A and TfCel9B from Thermobifida fusca. Since aromatic amino acids involved in substrate binding at subsites -4, -3, and -2 are missing in PttCel9A, the activity of TfCel9A mutant enzymes W256S, W209A, and W313G was also investigated. Delta(1-105)PttCel9A hydrolyzed a comparatively narrow range of polymeric substrates, and the preferred substrate was (carboxymethyl)cellulose 4M. Moreover, Delta(1-105)PttCel9A did not hydrolyze oligosaccharides shorter than cellopentaose, whereas TfCel9A and TfCel9B hydrolyzed cellotetraose and cellotriose, respectively. These data suggest that the preferred substrates of PttCel9A are long, low-substituted, soluble cellulosic polymers. At 30 degrees C and pH 6.0, the kcat for cellohexaose of Delta(1-105)PttCel9A, TfCel9A, and TfCel9B were 0.023 +/- 0.001, 16.9 +/- 2.0, and 1.3 +/- 0.2, respectively. The catalytic efficiency (kcat/Km) of TfCel9B was 39% of that of TfCel9A, whereas the catalytic efficiency of Delta(1-105)PttCel9A was 0.04% of that of TfCel9A. Removing tryptophan residues at subsites -4, -3, and -2 decreased the efficiency of cellohexaose hydrolysis by TfCel9A. Mutation of W313 to G had the most drastic effect, producing a mutant enzyme with 1% of the catalytic efficiency of TfCel9A. The apparent narrow substrate range and catalytic efficiency of PttCel9A are correlated with a lack of aromatic amino acids in the substrate binding cleft and may be necessary to prevent excessive hydrolysis of cell wall polysaccharides during cell wall formation.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Master</LastName>
<ForeName>Emma R</ForeName>
<Initials>ER</Initials>
<AffiliationInfo><Affiliation>Department of Biotechnology, Royal Institute of Technology (KTH), AlbaNova University Center, Stockholm, Sweden.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Rudsander</LastName>
<ForeName>Ulla J</ForeName>
<Initials>UJ</Initials>
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<Author ValidYN="Y"><LastName>Zhou</LastName>
<ForeName>Weilin</ForeName>
<Initials>W</Initials>
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<Author ValidYN="Y"><LastName>Henriksson</LastName>
<ForeName>Hongbin</ForeName>
<Initials>H</Initials>
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<Author ValidYN="Y"><LastName>Divne</LastName>
<ForeName>Christina</ForeName>
<Initials>C</Initials>
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<Author ValidYN="Y"><LastName>Denman</LastName>
<ForeName>Stuart</ForeName>
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<Author ValidYN="Y"><LastName>Wilson</LastName>
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<Author ValidYN="Y"><LastName>Teeri</LastName>
<ForeName>Tuula T</ForeName>
<Initials>TT</Initials>
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<NameOfSubstance UI="C099423">cellohexaose</NameOfSubstance>
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<CitationSubset>IM</CitationSubset>
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<MeshHeading><DescriptorName UI="D017360" MajorTopicYN="N">Arabidopsis</DescriptorName>
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<MeshHeading><DescriptorName UI="D002712" MajorTopicYN="N">Chlorides</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
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<MeshHeading><DescriptorName UI="D010843" MajorTopicYN="N">Pichia</DescriptorName>
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<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
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<MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName>
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<QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName>
<QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
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<MeshHeading><DescriptorName UI="D032107" MajorTopicYN="N">Populus</DescriptorName>
<QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName>
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<MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName>
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<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D017386" MajorTopicYN="Y">Sequence Homology, Amino Acid</DescriptorName>
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<MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName>
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<MeshHeading><DescriptorName UI="D013780" MajorTopicYN="N">Tetroses</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
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<MeshHeading><DescriptorName UI="D017967" MajorTopicYN="N">Zinc Compounds</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
</MeshHeadingList>
</MedlineCitation>
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<ArticleIdList><ArticleId IdType="pubmed">15287736</ArticleId>
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<affiliations><list><country><li>Suède</li>
</country>
<region><li>Svealand</li>
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<settlement><li>Stockholm</li>
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<tree><noCountry><name sortKey="Denman, Stuart" sort="Denman, Stuart" uniqKey="Denman S" first="Stuart" last="Denman">Stuart Denman</name>
<name sortKey="Divne, Christina" sort="Divne, Christina" uniqKey="Divne C" first="Christina" last="Divne">Christina Divne</name>
<name sortKey="Henriksson, Hongbin" sort="Henriksson, Hongbin" uniqKey="Henriksson H" first="Hongbin" last="Henriksson">Hongbin Henriksson</name>
<name sortKey="Rudsander, Ulla J" sort="Rudsander, Ulla J" uniqKey="Rudsander U" first="Ulla J" last="Rudsander">Ulla J. Rudsander</name>
<name sortKey="Teeri, Tuula T" sort="Teeri, Tuula T" uniqKey="Teeri T" first="Tuula T" last="Teeri">Tuula T. Teeri</name>
<name sortKey="Wilson, David B" sort="Wilson, David B" uniqKey="Wilson D" first="David B" last="Wilson">David B. Wilson</name>
<name sortKey="Zhou, Weilin" sort="Zhou, Weilin" uniqKey="Zhou W" first="Weilin" last="Zhou">Weilin Zhou</name>
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<country name="Suède"><region name="Svealand"><name sortKey="Master, Emma R" sort="Master, Emma R" uniqKey="Master E" first="Emma R" last="Master">Emma R. Master</name>
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