TLXI, a novel type of xylanase inhibitor from wheat (Triticum aestivum) belonging to the thaumatin family.
Identifieur interne : 000358 ( Main/Exploration ); précédent : 000357; suivant : 000359TLXI, a novel type of xylanase inhibitor from wheat (Triticum aestivum) belonging to the thaumatin family.
Auteurs : Ellen Fierens [Belgique] ; Sigrid Rombouts ; Kurt Gebruers ; Hans Goesaert ; Kristof Brijs ; Johnny Beaugrand ; Guido Volckaert ; Steven Van Campenhout ; Paul Proost ; Christophe M. Courtin ; Jan A. DelcourSource :
- The Biochemical journal [ 1470-8728 ] ; 2007.
Descripteurs français
- KwdFr :
- Antienzymes (composition chimique), Antienzymes (isolement et purification), Cinétique (MeSH), Clonage moléculaire (MeSH), Données de séquences moléculaires (MeSH), Endo-1,4-beta xylanases (antagonistes et inhibiteurs), Facteurs temps (MeSH), Glycosylation (MeSH), Méthanesulfonates (composition chimique), Peptide-N4-(N-acetyl-beta-glucosaminyl) asparagine amidase (métabolisme), Protéines végétales (composition chimique), Spectrométrie de masse (MeSH), Séquence d'acides aminés (MeSH), Séquence nucléotidique (MeSH), Triticum (composition chimique), Xylanes (métabolisme), Électrophorèse sur gel de polyacrylamide (MeSH).
- MESH :
- antagonistes et inhibiteurs : Endo-1,4-beta xylanases.
- composition chimique : Antienzymes, Méthanesulfonates, Protéines végétales, Triticum.
- isolement et purification : Antienzymes.
- métabolisme : Peptide-N4-(N-acetyl-beta-glucosaminyl) asparagine amidase, Xylanes.
- Cinétique, Clonage moléculaire, Données de séquences moléculaires, Facteurs temps, Glycosylation, Spectrométrie de masse, Séquence d'acides aminés, Séquence nucléotidique, Électrophorèse sur gel de polyacrylamide.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Base Sequence (MeSH), Cloning, Molecular (MeSH), Electrophoresis, Polyacrylamide Gel (MeSH), Endo-1,4-beta Xylanases (antagonists & inhibitors), Enzyme Inhibitors (chemistry), Enzyme Inhibitors (isolation & purification), Glycosylation (MeSH), Kinetics (MeSH), Mass Spectrometry (MeSH), Mesylates (chemistry), Molecular Sequence Data (MeSH), Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase (metabolism), Plant Proteins (chemistry), Time Factors (MeSH), Triticum (chemistry), Xylans (metabolism).
- MESH :
- chemical , antagonists & inhibitors : Endo-1,4-beta Xylanases.
- chemical , chemistry : Enzyme Inhibitors, Mesylates, Plant Proteins.
- chemical , isolation & purification : Enzyme Inhibitors.
- chemical , metabolism : Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase, Xylans.
- chemistry : Triticum.
- Amino Acid Sequence, Base Sequence, Cloning, Molecular, Electrophoresis, Polyacrylamide Gel, Glycosylation, Kinetics, Mass Spectrometry, Molecular Sequence Data, Time Factors.
Abstract
Wheat (Triticum aestivum) contains a previously unknown type of xylanase (EC 3.2.1.8) inhibitor, which is described in the present paper for the first time. Based on its >60% similarity to TLPs (thaumatin-like proteins) and the fact that it contains the Prosite PS00316 thaumatin family signature, it is referred to as TLXI (thaumatin-like xylanase inhibitor). TLXI is a basic (pI> or =9.3 in isoelectric focusing) protein with a molecular mass of approx. 18-kDa (determined by SDS/PAGE) and it occurs in wheat with varying extents of glycosylation. The TLXI gene sequence encodes a 26-amino-acid signal sequence followed by a 151-amino-acid mature protein with a calculated molecular mass of 15.6-kDa and pI of 8.38. The mature TLXI protein was expressed successfully in Pichia pastoris, resulting in a 21-kDa (determined by SDS/PAGE) recombinant protein (rTLXI). Polyclonal antibodies raised against TLXI purified from wheat react with epitopes of rTLXI as well as with those of thaumatin, demonstrating high structural similarity between these three proteins. TLXI has a unique inhibition specificity. It is a non-competitive inhibitor of a number of glycoside hydrolase family 11 xylanases, but it is inactive towards glycoside hydrolase family 10 xylanases. Progress curves show that TLXI is a slow tight-binding inhibitor, with a K(i) of approx. 60-nM. Except for zeamatin, an alpha-amylase/trypsin inhibitor from maize (Zea mays), no other enzyme inhibitor is currently known among the TLPs. TLXI thus represents a novel type of inhibitor within this group of proteins.
DOI: 10.1042/BJ20061291
PubMed: 17269932
PubMed Central: PMC1876379
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Courtin</name></author><author><name sortKey="Delcour, Jan A" sort="Delcour, Jan A" uniqKey="Delcour J" first="Jan A" last="Delcour">Jan A. Delcour</name></author></analytic><series><title level="j">The Biochemical journal</title><idno type="eISSN">1470-8728</idno><imprint><date when="2007" type="published">2007</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Base Sequence (MeSH)</term><term>Cloning, Molecular (MeSH)</term><term>Electrophoresis, Polyacrylamide Gel (MeSH)</term><term>Endo-1,4-beta Xylanases (antagonists & inhibitors)</term><term>Enzyme Inhibitors (chemistry)</term><term>Enzyme Inhibitors (isolation & purification)</term><term>Glycosylation (MeSH)</term><term>Kinetics (MeSH)</term><term>Mass Spectrometry (MeSH)</term><term>Mesylates (chemistry)</term><term>Molecular Sequence Data (MeSH)</term><term>Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase (metabolism)</term><term>Plant Proteins (chemistry)</term><term>Time Factors (MeSH)</term><term>Triticum (chemistry)</term><term>Xylans (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Antienzymes (composition chimique)</term><term>Antienzymes (isolement et purification)</term><term>Cinétique (MeSH)</term><term>Clonage moléculaire (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Endo-1,4-beta xylanases (antagonistes et inhibiteurs)</term><term>Facteurs temps (MeSH)</term><term>Glycosylation (MeSH)</term><term>Méthanesulfonates (composition chimique)</term><term>Peptide-N4-(N-acetyl-beta-glucosaminyl) asparagine amidase (métabolisme)</term><term>Protéines végétales (composition chimique)</term><term>Spectrométrie de masse (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Séquence nucléotidique (MeSH)</term><term>Triticum (composition chimique)</term><term>Xylanes (métabolisme)</term><term>Électrophorèse sur gel de polyacrylamide (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Endo-1,4-beta Xylanases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Enzyme Inhibitors</term><term>Mesylates</term><term>Plant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Enzyme Inhibitors</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase</term><term>Xylans</term></keywords><keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>Endo-1,4-beta xylanases</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Triticum</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Antienzymes</term><term>Méthanesulfonates</term><term>Protéines végétales</term><term>Triticum</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Antienzymes</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Peptide-N4-(N-acetyl-beta-glucosaminyl) asparagine amidase</term><term>Xylanes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Base Sequence</term><term>Cloning, Molecular</term><term>Electrophoresis, Polyacrylamide Gel</term><term>Glycosylation</term><term>Kinetics</term><term>Mass Spectrometry</term><term>Molecular Sequence Data</term><term>Time Factors</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cinétique</term><term>Clonage moléculaire</term><term>Données de séquences moléculaires</term><term>Facteurs temps</term><term>Glycosylation</term><term>Spectrométrie de masse</term><term>Séquence d'acides aminés</term><term>Séquence nucléotidique</term><term>Électrophorèse sur gel de polyacrylamide</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Wheat (Triticum aestivum) contains a previously unknown type of xylanase (EC 3.2.1.8) inhibitor, which is described in the present paper for the first time. Based on its >60% similarity to TLPs (thaumatin-like proteins) and the fact that it contains the Prosite PS00316 thaumatin family signature, it is referred to as TLXI (thaumatin-like xylanase inhibitor). TLXI is a basic (pI> or =9.3 in isoelectric focusing) protein with a molecular mass of approx. 18-kDa (determined by SDS/PAGE) and it occurs in wheat with varying extents of glycosylation. The TLXI gene sequence encodes a 26-amino-acid signal sequence followed by a 151-amino-acid mature protein with a calculated molecular mass of 15.6-kDa and pI of 8.38. The mature TLXI protein was expressed successfully in Pichia pastoris, resulting in a 21-kDa (determined by SDS/PAGE) recombinant protein (rTLXI). Polyclonal antibodies raised against TLXI purified from wheat react with epitopes of rTLXI as well as with those of thaumatin, demonstrating high structural similarity between these three proteins. TLXI has a unique inhibition specificity. It is a non-competitive inhibitor of a number of glycoside hydrolase family 11 xylanases, but it is inactive towards glycoside hydrolase family 10 xylanases. Progress curves show that TLXI is a slow tight-binding inhibitor, with a K(i) of approx. 60-nM. Except for zeamatin, an alpha-amylase/trypsin inhibitor from maize (Zea mays), no other enzyme inhibitor is currently known among the TLPs. TLXI thus represents a novel type of inhibitor within this group of proteins.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17269932</PMID><DateCompleted><Year>2007</Year><Month>05</Month><Day>07</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1470-8728</ISSN><JournalIssue CitedMedium="Internet"><Volume>403</Volume><Issue>3</Issue><PubDate><Year>2007</Year><Month>May</Month><Day>01</Day></PubDate></JournalIssue><Title>The Biochemical journal</Title><ISOAbbreviation>Biochem J</ISOAbbreviation></Journal><ArticleTitle>TLXI, a novel type of xylanase inhibitor from wheat (Triticum aestivum) belonging to the thaumatin family.</ArticleTitle><Pagination><MedlinePgn>583-91</MedlinePgn></Pagination><Abstract><AbstractText>Wheat (Triticum aestivum) contains a previously unknown type of xylanase (EC 3.2.1.8) inhibitor, which is described in the present paper for the first time. Based on its >60% similarity to TLPs (thaumatin-like proteins) and the fact that it contains the Prosite PS00316 thaumatin family signature, it is referred to as TLXI (thaumatin-like xylanase inhibitor). TLXI is a basic (pI> or =9.3 in isoelectric focusing) protein with a molecular mass of approx. 18-kDa (determined by SDS/PAGE) and it occurs in wheat with varying extents of glycosylation. The TLXI gene sequence encodes a 26-amino-acid signal sequence followed by a 151-amino-acid mature protein with a calculated molecular mass of 15.6-kDa and pI of 8.38. The mature TLXI protein was expressed successfully in Pichia pastoris, resulting in a 21-kDa (determined by SDS/PAGE) recombinant protein (rTLXI). Polyclonal antibodies raised against TLXI purified from wheat react with epitopes of rTLXI as well as with those of thaumatin, demonstrating high structural similarity between these three proteins. TLXI has a unique inhibition specificity. It is a non-competitive inhibitor of a number of glycoside hydrolase family 11 xylanases, but it is inactive towards glycoside hydrolase family 10 xylanases. Progress curves show that TLXI is a slow tight-binding inhibitor, with a K(i) of approx. 60-nM. Except for zeamatin, an alpha-amylase/trypsin inhibitor from maize (Zea mays), no other enzyme inhibitor is currently known among the TLPs. TLXI thus represents a novel type of inhibitor within this group of proteins.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Fierens</LastName><ForeName>Ellen</ForeName><Initials>E</Initials><AffiliationInfo><Affiliation>Laboratory of Food Chemistry and Biochemistry, Katholieke Universiteit Leuven, Kasteelpark Arenberg 20, B-3001 Leuven, Belgium.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Rombouts</LastName><ForeName>Sigrid</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Gebruers</LastName><ForeName>Kurt</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Goesaert</LastName><ForeName>Hans</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Brijs</LastName><ForeName>Kristof</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Beaugrand</LastName><ForeName>Johnny</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Volckaert</LastName><ForeName>Guido</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Van Campenhout</LastName><ForeName>Steven</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Proost</LastName><ForeName>Paul</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Courtin</LastName><ForeName>Christophe M</ForeName><Initials>CM</Initials></Author><Author ValidYN="Y"><LastName>Delcour</LastName><ForeName>Jan A</ForeName><Initials>JA</Initials></Author></AuthorList><Language>eng</Language><DataBankList CompleteYN="Y"><DataBank><DataBankName>GENBANK</DataBankName><AccessionNumberList><AccessionNumber>AJ786602</AccessionNumber></AccessionNumberList></DataBank></DataBankList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Biochem J</MedlineTA><NlmUniqueID>2984726R</NlmUniqueID><ISSNLinking>0264-6021</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004791">Enzyme Inhibitors</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008698">Mesylates</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014990">Xylans</NameOfSubstance></Chemical><Chemical><RegistryNumber>53850-34-3</RegistryNumber><NameOfSubstance UI="C003427">thaumatin protein, plant</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.8</RegistryNumber><NameOfSubstance UI="D043364">Endo-1,4-beta Xylanases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.5.1.52</RegistryNumber><NameOfSubstance UI="D043524">Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase</NameOfSubstance></Chemical><Chemical><RegistryNumber>JE2SY203E8</RegistryNumber><NameOfSubstance UI="C012077">trifluoromethanesulfonic acid</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001483" MajorTopicYN="N">Base Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003001" MajorTopicYN="N">Cloning, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004591" MajorTopicYN="N">Electrophoresis, Polyacrylamide Gel</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D043364" MajorTopicYN="N">Endo-1,4-beta Xylanases</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="Y">antagonists & inhibitors</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004791" MajorTopicYN="N">Enzyme Inhibitors</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006031" MajorTopicYN="N">Glycosylation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013058" MajorTopicYN="N">Mass Spectrometry</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008698" MajorTopicYN="N">Mesylates</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D043524" MajorTopicYN="N">Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013997" MajorTopicYN="N">Time Factors</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014908" MajorTopicYN="N">Triticum</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014990" MajorTopicYN="N">Xylans</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2007</Year><Month>2</Month><Day>3</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate 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IdType="pubmed">1863782</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>Belgique</li></country><region><li>Province du Brabant flamand</li><li>Région flamande</li></region><settlement><li>Louvain</li></settlement><orgName><li>Katholieke Universiteit Leuven</li></orgName></list><tree><noCountry><name sortKey="Beaugrand, Johnny" sort="Beaugrand, Johnny" uniqKey="Beaugrand J" first="Johnny" last="Beaugrand">Johnny Beaugrand</name><name sortKey="Brijs, Kristof" sort="Brijs, Kristof" uniqKey="Brijs K" first="Kristof" last="Brijs">Kristof Brijs</name><name sortKey="Courtin, Christophe M" sort="Courtin, Christophe M" uniqKey="Courtin C" first="Christophe M" last="Courtin">Christophe M. Courtin</name><name sortKey="Delcour, Jan A" sort="Delcour, Jan A" uniqKey="Delcour J" first="Jan A" last="Delcour">Jan A. Delcour</name><name sortKey="Gebruers, Kurt" sort="Gebruers, Kurt" uniqKey="Gebruers K" first="Kurt" last="Gebruers">Kurt Gebruers</name><name sortKey="Goesaert, Hans" sort="Goesaert, Hans" uniqKey="Goesaert H" first="Hans" last="Goesaert">Hans Goesaert</name><name sortKey="Proost, Paul" sort="Proost, Paul" uniqKey="Proost P" first="Paul" last="Proost">Paul Proost</name><name sortKey="Rombouts, Sigrid" sort="Rombouts, Sigrid" uniqKey="Rombouts S" first="Sigrid" last="Rombouts">Sigrid Rombouts</name><name sortKey="Van Campenhout, Steven" sort="Van Campenhout, Steven" uniqKey="Van Campenhout S" first="Steven" last="Van Campenhout">Steven Van Campenhout</name><name sortKey="Volckaert, Guido" sort="Volckaert, Guido" uniqKey="Volckaert G" first="Guido" last="Volckaert">Guido Volckaert</name></noCountry><country name="Belgique"><region name="Région flamande"><name sortKey="Fierens, Ellen" sort="Fierens, Ellen" uniqKey="Fierens E" first="Ellen" last="Fierens">Ellen Fierens</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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