Substrate specificities of two tau class glutathione transferases inducible by 2,4,6-trinitrotoluene in poplar.
Identifieur interne : 001B29 ( Main/Exploration ); précédent : 001B28; suivant : 001B30Substrate specificities of two tau class glutathione transferases inducible by 2,4,6-trinitrotoluene in poplar.
Auteurs : Yaman Musdal [Suède] ; Bengt Mannervik [Suède]Source :
- Biochimica et biophysica acta [ 0006-3002 ] ; 2015.
Descripteurs français
- KwdFr :
- 2,4,6-Trinitro-toluène (pharmacologie), Cinétique (MeSH), Cristallisation (MeSH), Données de séquences moléculaires (MeSH), Glutathione transferase (composition chimique), Glutathione transferase (métabolisme), Induction enzymatique (effets des médicaments et des substances chimiques), Modèles moléculaires (MeSH), Sites de fixation (MeSH), Spécificité du substrat (MeSH), Séquence d'acides aminés (MeSH).
- MESH :
- composition chimique : Glutathione transferase.
- effets des médicaments et des substances chimiques : Induction enzymatique.
- métabolisme : Glutathione transferase.
- pharmacologie : 2,4,6-Trinitro-toluène.
- Cinétique, Cristallisation, Données de séquences moléculaires, Modèles moléculaires, Sites de fixation, Spécificité du substrat, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Binding Sites (MeSH), Crystallization (MeSH), Enzyme Induction (drug effects), Glutathione Transferase (chemistry), Glutathione Transferase (metabolism), Kinetics (MeSH), Models, Molecular (MeSH), Molecular Sequence Data (MeSH), Substrate Specificity (MeSH), Trinitrotoluene (pharmacology).
- MESH :
- chemical , chemistry : Glutathione Transferase.
- drug effects : Enzyme Induction.
- chemical , metabolism : Glutathione Transferase.
- chemical , pharmacology : Trinitrotoluene.
- Amino Acid Sequence, Binding Sites, Crystallization, Kinetics, Models, Molecular, Molecular Sequence Data, Substrate Specificity.
Abstract
BACKGROUND
The genome of poplar (Populus trichocarpa) encodes 81 glutathione transferases (GSTs) annotated in eight distinct classes. The tau class is considered the most versatile in the biotransformation of xenobiotics and is composed of 58 GSTs. Two of the enzymes, GSTU16 and GSTU45, have particular interest since their expression is induced by exposure of poplar tissues to 2,4,6-trinitrotoluene (TNT) and could potentially be involved in the metabolism of this toxic environmental contaminant.
RESULTS
DNA encoding these GSTs was synthesized and the proteins were heterologously expressed in Escherichia coli and the purified enzymes were characterized.
MAJOR CONCLUSIONS
GSTU16 assayed with a number of conventional GST substrates showed the highest specific activity (60μmolmin⁻¹ mg⁻¹) with phenethyl isothiocyanate, 150-fold higher than that with CDNB. By contrast, GSTU45 showed CDNB as the most active substrate (3.3μmolmin⁻¹ mg⁻¹) whereas all of the 16 alternative substrates tested yielded significantly lower activities. Homology modeling suggested that the aromatic residues Phe10 and Tyr107 in the active site of GSTU16 are promoting the high activity with PEITC and other substrates with aromatic side-chains. Nonetheless, TNT was a poor substrate for GSTU16 as well as for GSTU45 with a specific activity of 0.05nmolmin⁻¹ mg⁻¹ for both enzymes.
GENERAL SIGNIFICANCE
GSTU16 and GSTU45 do not play a major role in the degradation of TNT in poplar.
DOI: 10.1016/j.bbagen.2015.05.015
PubMed: 26026470
Affiliations:
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Electronic address: bengt.mannervik@neurochem.su.se.</nlm:affiliation><country xml:lang="fr">Suède</country><wicri:regionArea>Department of Neurochemistry, Stockholm University, SE-10691 Stockholm</wicri:regionArea><orgName type="university">Université de Stockholm</orgName><placeName><settlement type="city">Stockholm</settlement><region nuts="1">Svealand</region><region nuts="1">Comté de Stockholm</region></placeName></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2015">2015</date><idno type="RBID">pubmed:26026470</idno><idno type="pmid">26026470</idno><idno type="doi">10.1016/j.bbagen.2015.05.015</idno><idno type="wicri:Area/Main/Corpus">001C75</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">001C75</idno><idno type="wicri:Area/Main/Curation">001C75</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">001C75</idno><idno type="wicri:Area/Main/Exploration">001C75</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Substrate specificities of two tau class glutathione transferases inducible by 2,4,6-trinitrotoluene in poplar.</title><author><name sortKey="Musdal, Yaman" sort="Musdal, Yaman" uniqKey="Musdal Y" first="Yaman" last="Musdal">Yaman Musdal</name><affiliation wicri:level="4"><nlm:affiliation>Department of Neurochemistry, Stockholm University, SE-10691 Stockholm, Sweden.</nlm:affiliation><country xml:lang="fr">Suède</country><wicri:regionArea>Department of Neurochemistry, Stockholm University, SE-10691 Stockholm</wicri:regionArea><orgName type="university">Université de Stockholm</orgName><placeName><settlement type="city">Stockholm</settlement><region nuts="1">Svealand</region><region nuts="1">Comté de Stockholm</region></placeName></affiliation></author><author><name sortKey="Mannervik, Bengt" sort="Mannervik, Bengt" uniqKey="Mannervik B" first="Bengt" last="Mannervik">Bengt Mannervik</name><affiliation wicri:level="4"><nlm:affiliation>Department of Neurochemistry, Stockholm University, SE-10691 Stockholm, Sweden. Electronic address: bengt.mannervik@neurochem.su.se.</nlm:affiliation><country xml:lang="fr">Suède</country><wicri:regionArea>Department of Neurochemistry, Stockholm University, SE-10691 Stockholm</wicri:regionArea><orgName type="university">Université de Stockholm</orgName><placeName><settlement type="city">Stockholm</settlement><region nuts="1">Svealand</region><region nuts="1">Comté de Stockholm</region></placeName></affiliation></author></analytic><series><title level="j">Biochimica et biophysica acta</title><idno type="ISSN">0006-3002</idno><imprint><date when="2015" type="published">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Binding Sites (MeSH)</term><term>Crystallization (MeSH)</term><term>Enzyme Induction (drug effects)</term><term>Glutathione Transferase (chemistry)</term><term>Glutathione Transferase (metabolism)</term><term>Kinetics (MeSH)</term><term>Models, Molecular (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Substrate Specificity (MeSH)</term><term>Trinitrotoluene (pharmacology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>2,4,6-Trinitro-toluène (pharmacologie)</term><term>Cinétique (MeSH)</term><term>Cristallisation (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Glutathione transferase (composition chimique)</term><term>Glutathione transferase (métabolisme)</term><term>Induction enzymatique (effets des médicaments et des substances chimiques)</term><term>Modèles moléculaires (MeSH)</term><term>Sites de fixation (MeSH)</term><term>Spécificité du substrat (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Glutathione Transferase</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Glutathione transferase</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Enzyme Induction</term></keywords><keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Induction enzymatique</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutathione Transferase</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glutathione transferase</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>2,4,6-Trinitro-toluène</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Trinitrotoluene</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Binding Sites</term><term>Crystallization</term><term>Kinetics</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Substrate Specificity</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cinétique</term><term>Cristallisation</term><term>Données de séquences moléculaires</term><term>Modèles moléculaires</term><term>Sites de fixation</term><term>Spécificité du substrat</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p><b>BACKGROUND</b></p><p>The genome of poplar (Populus trichocarpa) encodes 81 glutathione transferases (GSTs) annotated in eight distinct classes. The tau class is considered the most versatile in the biotransformation of xenobiotics and is composed of 58 GSTs. Two of the enzymes, GSTU16 and GSTU45, have particular interest since their expression is induced by exposure of poplar tissues to 2,4,6-trinitrotoluene (TNT) and could potentially be involved in the metabolism of this toxic environmental contaminant.</p></div><div type="abstract" xml:lang="en"><p><b>RESULTS</b></p><p>DNA encoding these GSTs was synthesized and the proteins were heterologously expressed in Escherichia coli and the purified enzymes were characterized.</p></div><div type="abstract" xml:lang="en"><p><b>MAJOR CONCLUSIONS</b></p><p>GSTU16 assayed with a number of conventional GST substrates showed the highest specific activity (60μmolmin⁻¹ mg⁻¹) with phenethyl isothiocyanate, 150-fold higher than that with CDNB. By contrast, GSTU45 showed CDNB as the most active substrate (3.3μmolmin⁻¹ mg⁻¹) whereas all of the 16 alternative substrates tested yielded significantly lower activities. Homology modeling suggested that the aromatic residues Phe10 and Tyr107 in the active site of GSTU16 are promoting the high activity with PEITC and other substrates with aromatic side-chains. Nonetheless, TNT was a poor substrate for GSTU16 as well as for GSTU45 with a specific activity of 0.05nmolmin⁻¹ mg⁻¹ for both enzymes.</p></div><div type="abstract" xml:lang="en"><p><b>GENERAL SIGNIFICANCE</b></p><p>GSTU16 and GSTU45 do not play a major role in the degradation of TNT in poplar.</p></div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">26026470</PMID><DateCompleted><Year>2015</Year><Month>09</Month><Day>28</Day></DateCompleted><DateRevised><Year>2016</Year><Month>11</Month><Day>26</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0006-3002</ISSN><JournalIssue CitedMedium="Print"><Volume>1850</Volume><Issue>9</Issue><PubDate><Year>2015</Year><Month>Sep</Month></PubDate></JournalIssue><Title>Biochimica et biophysica acta</Title><ISOAbbreviation>Biochim Biophys Acta</ISOAbbreviation></Journal><ArticleTitle>Substrate specificities of two tau class glutathione transferases inducible by 2,4,6-trinitrotoluene in poplar.</ArticleTitle><Pagination><MedlinePgn>1877-83</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.bbagen.2015.05.015</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0304-4165(15)00154-3</ELocationID><Abstract><AbstractText Label="BACKGROUND" NlmCategory="BACKGROUND">The genome of poplar (Populus trichocarpa) encodes 81 glutathione transferases (GSTs) annotated in eight distinct classes. The tau class is considered the most versatile in the biotransformation of xenobiotics and is composed of 58 GSTs. Two of the enzymes, GSTU16 and GSTU45, have particular interest since their expression is induced by exposure of poplar tissues to 2,4,6-trinitrotoluene (TNT) and could potentially be involved in the metabolism of this toxic environmental contaminant.</AbstractText><AbstractText Label="RESULTS" NlmCategory="RESULTS">DNA encoding these GSTs was synthesized and the proteins were heterologously expressed in Escherichia coli and the purified enzymes were characterized.</AbstractText><AbstractText Label="MAJOR CONCLUSIONS" NlmCategory="CONCLUSIONS">GSTU16 assayed with a number of conventional GST substrates showed the highest specific activity (60μmolmin⁻¹ mg⁻¹) with phenethyl isothiocyanate, 150-fold higher than that with CDNB. By contrast, GSTU45 showed CDNB as the most active substrate (3.3μmolmin⁻¹ mg⁻¹) whereas all of the 16 alternative substrates tested yielded significantly lower activities. Homology modeling suggested that the aromatic residues Phe10 and Tyr107 in the active site of GSTU16 are promoting the high activity with PEITC and other substrates with aromatic side-chains. Nonetheless, TNT was a poor substrate for GSTU16 as well as for GSTU45 with a specific activity of 0.05nmolmin⁻¹ mg⁻¹ for both enzymes.</AbstractText><AbstractText Label="GENERAL SIGNIFICANCE" NlmCategory="CONCLUSIONS">GSTU16 and GSTU45 do not play a major role in the degradation of TNT in poplar.</AbstractText><CopyrightInformation>Copyright © 2015 Elsevier B.V. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Musdal</LastName><ForeName>Yaman</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>Department of Neurochemistry, Stockholm University, SE-10691 Stockholm, Sweden.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Mannervik</LastName><ForeName>Bengt</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>Department of Neurochemistry, Stockholm University, SE-10691 Stockholm, Sweden. Electronic address: bengt.mannervik@neurochem.su.se.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2015</Year><Month>05</Month><Day>27</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Biochim Biophys Acta</MedlineTA><NlmUniqueID>0217513</NlmUniqueID><ISSNLinking>0006-3002</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>118-96-7</RegistryNumber><NameOfSubstance UI="D014303">Trinitrotoluene</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.5.1.18</RegistryNumber><NameOfSubstance UI="D005982">Glutathione Transferase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003460" MajorTopicYN="N">Crystallization</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004790" MajorTopicYN="N">Enzyme Induction</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005982" MajorTopicYN="N">Glutathione Transferase</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014303" MajorTopicYN="N">Trinitrotoluene</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Detoxication</Keyword><Keyword MajorTopicYN="N">Glutathione transferase</Keyword><Keyword MajorTopicYN="N">Phytoremediation</Keyword><Keyword MajorTopicYN="N">Populus trichocarpa</Keyword><Keyword MajorTopicYN="N">TNT</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2015</Year><Month>02</Month><Day>14</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2015</Year><Month>04</Month><Day>30</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2015</Year><Month>05</Month><Day>20</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2015</Year><Month>6</Month><Day>1</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2015</Year><Month>6</Month><Day>1</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2015</Year><Month>9</Month><Day>29</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">26026470</ArticleId><ArticleId IdType="pii">S0304-4165(15)00154-3</ArticleId><ArticleId IdType="doi">10.1016/j.bbagen.2015.05.015</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Suède</li></country><region><li>Comté de Stockholm</li><li>Svealand</li></region><settlement><li>Stockholm</li></settlement><orgName><li>Université de Stockholm</li></orgName></list><tree><country name="Suède"><region name="Svealand"><name sortKey="Musdal, Yaman" sort="Musdal, Yaman" uniqKey="Musdal Y" first="Yaman" last="Musdal">Yaman Musdal</name></region><name sortKey="Mannervik, Bengt" sort="Mannervik, Bengt" uniqKey="Mannervik B" first="Bengt" last="Mannervik">Bengt Mannervik</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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