Purification and characterization of glutathione conjugate reductase: a component of the tetrachlorohydroquinone reductive dehalogenase system from Phanerochaete chrysosporium.
Identifieur interne : 000A28 ( Main/Exploration ); précédent : 000A27; suivant : 000A29Purification and characterization of glutathione conjugate reductase: a component of the tetrachlorohydroquinone reductive dehalogenase system from Phanerochaete chrysosporium.
Auteurs : G V Reddy [États-Unis] ; M H GoldSource :
- Archives of biochemistry and biophysics [ 0003-9861 ] ; 2001.
Descripteurs français
- KwdFr :
- Concentration en ions d'hydrogène (MeSH), Glutathion (métabolisme), Hydrolases (isolement et purification), Hydrolases (métabolisme), Lipoprotéines LDL (isolement et purification), Métaux (pharmacologie), Oxidoreductases (isolement et purification), Oxidoreductases (métabolisme), Phanerochaete (enzymologie), Spécificité du substrat (MeSH), Température (MeSH), Thiols (métabolisme).
- MESH :
- enzymologie : Phanerochaete.
- isolement et purification : Hydrolases, Lipoprotéines LDL, Oxidoreductases.
- métabolisme : Glutathion, Hydrolases, Oxidoreductases, Thiols.
- pharmacologie : Métaux.
- Concentration en ions d'hydrogène, Spécificité du substrat, Température.
English descriptors
- KwdEn :
- Glutathione (metabolism), Hydrogen-Ion Concentration (MeSH), Hydrolases (isolation & purification), Hydrolases (metabolism), Lipoproteins, LDL (isolation & purification), Metals (pharmacology), Oxidoreductases (isolation & purification), Oxidoreductases (metabolism), Phanerochaete (enzymology), Substrate Specificity (MeSH), Sulfhydryl Compounds (metabolism), Temperature (MeSH).
- MESH :
- chemical , isolation & purification : Hydrolases, Lipoproteins, LDL, Oxidoreductases.
- chemical , metabolism : Glutathione, Hydrolases, Oxidoreductases, Sulfhydryl Compounds.
- chemical , pharmacology : Metals.
- enzymology : Phanerochaete.
- Hydrogen-Ion Concentration, Substrate Specificity, Temperature.
Abstract
A membrane-bound glutathione S-transferase and a soluble glutathione conjugate reductase constitute the reductive dehalogenase system of P. chrysosporium. This enzyme system reductively removes chlorine substituents from tetrachlorohydroquinone, a metabolite of pentachlorophenol. The membrane-bound glutathione S-transferase converts tetrachlorohydroquinone to S-glutathionyltrichloro-1,4-hydroquinone, which is subsequently reduced to 3,5,6-trichlorohydroquinone by the soluble glutathione conjugate reductase (GCR). This GCR can accept glutathione, dithiothreitol, cysteine, or beta-mercaptoethanol as cosubstrates. GCR was purified to apparent homogeneity by ion-exchange and covalent chromatography. The enzyme exhibits optimum activity at pH 6.0 and 55 degrees C and appears to be a homodimer with a M(r) of approximately 60 kDa. Activity increases as the number of chlorine substituents on the hydroquinone ring is increased. GCR has an apparent K(m) of approximately 33 microM and an apparent k(cat) of approximately 3.43 s(-1) for 2-S-glutathionyl-3,5,6-trichloro-1,4-hydroquinone. Inhibitors of GCR include Cd(2+), Fe(2+), Mn(2+), iodoacetic acid, and p-chloromercuribenzoic acid, suggesting the presence of a catalytic cysteine thiol(s) at the active site. When glutathione is used as a cosubstrate, reduction of S-glutathionyltrichloro-1,4-hydroquinone is accompanied by the production of trichlorohydroquinone and oxidized glutathione in a 1:1 ratio. A mechanism for this novel enzyme is proposed.
DOI: 10.1006/abbi.2001.2417
PubMed: 11437359
Affiliations:
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Le document en format XML
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Graduate Institute of Science and Technology, Beaverton, Oregon 97006-8921, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biochemistry and Molecular Biology, Oregon Graduate Institute of Science and Technology, Beaverton, Oregon 97006-8921</wicri:regionArea><wicri:noRegion>Oregon 97006-8921</wicri:noRegion></affiliation></author><author><name sortKey="Gold, M H" sort="Gold, M H" uniqKey="Gold M" first="M H" last="Gold">M H Gold</name></author></analytic><series><title level="j">Archives of biochemistry and biophysics</title><idno type="ISSN">0003-9861</idno><imprint><date when="2001" type="published">2001</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Glutathione (metabolism)</term><term>Hydrogen-Ion Concentration (MeSH)</term><term>Hydrolases (isolation & purification)</term><term>Hydrolases (metabolism)</term><term>Lipoproteins, LDL (isolation & purification)</term><term>Metals (pharmacology)</term><term>Oxidoreductases (isolation & purification)</term><term>Oxidoreductases (metabolism)</term><term>Phanerochaete (enzymology)</term><term>Substrate Specificity (MeSH)</term><term>Sulfhydryl Compounds (metabolism)</term><term>Temperature (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Concentration en ions d'hydrogène (MeSH)</term><term>Glutathion (métabolisme)</term><term>Hydrolases (isolement et purification)</term><term>Hydrolases (métabolisme)</term><term>Lipoprotéines LDL (isolement et purification)</term><term>Métaux (pharmacologie)</term><term>Oxidoreductases (isolement et purification)</term><term>Oxidoreductases (métabolisme)</term><term>Phanerochaete (enzymologie)</term><term>Spécificité du substrat (MeSH)</term><term>Température (MeSH)</term><term>Thiols (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Hydrolases</term><term>Lipoproteins, LDL</term><term>Oxidoreductases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutathione</term><term>Hydrolases</term><term>Oxidoreductases</term><term>Sulfhydryl Compounds</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Metals</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Phanerochaete</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Phanerochaete</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Hydrolases</term><term>Lipoprotéines LDL</term><term>Oxidoreductases</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glutathion</term><term>Hydrolases</term><term>Oxidoreductases</term><term>Thiols</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Métaux</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Hydrogen-Ion Concentration</term><term>Substrate Specificity</term><term>Temperature</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Concentration en ions d'hydrogène</term><term>Spécificité du substrat</term><term>Température</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">A membrane-bound glutathione S-transferase and a soluble glutathione conjugate reductase constitute the reductive dehalogenase system of P. chrysosporium. This enzyme system reductively removes chlorine substituents from tetrachlorohydroquinone, a metabolite of pentachlorophenol. The membrane-bound glutathione S-transferase converts tetrachlorohydroquinone to S-glutathionyltrichloro-1,4-hydroquinone, which is subsequently reduced to 3,5,6-trichlorohydroquinone by the soluble glutathione conjugate reductase (GCR). This GCR can accept glutathione, dithiothreitol, cysteine, or beta-mercaptoethanol as cosubstrates. GCR was purified to apparent homogeneity by ion-exchange and covalent chromatography. The enzyme exhibits optimum activity at pH 6.0 and 55 degrees C and appears to be a homodimer with a M(r) of approximately 60 kDa. Activity increases as the number of chlorine substituents on the hydroquinone ring is increased. GCR has an apparent K(m) of approximately 33 microM and an apparent k(cat) of approximately 3.43 s(-1) for 2-S-glutathionyl-3,5,6-trichloro-1,4-hydroquinone. Inhibitors of GCR include Cd(2+), Fe(2+), Mn(2+), iodoacetic acid, and p-chloromercuribenzoic acid, suggesting the presence of a catalytic cysteine thiol(s) at the active site. When glutathione is used as a cosubstrate, reduction of S-glutathionyltrichloro-1,4-hydroquinone is accompanied by the production of trichlorohydroquinone and oxidized glutathione in a 1:1 ratio. A mechanism for this novel enzyme is proposed.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">11437359</PMID><DateCompleted><Year>2001</Year><Month>08</Month><Day>09</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0003-9861</ISSN><JournalIssue CitedMedium="Print"><Volume>391</Volume><Issue>2</Issue><PubDate><Year>2001</Year><Month>Jul</Month><Day>15</Day></PubDate></JournalIssue><Title>Archives of biochemistry and biophysics</Title><ISOAbbreviation>Arch Biochem Biophys</ISOAbbreviation></Journal><ArticleTitle>Purification and characterization of glutathione conjugate reductase: a component of the tetrachlorohydroquinone reductive dehalogenase system from Phanerochaete chrysosporium.</ArticleTitle><Pagination><MedlinePgn>271-7</MedlinePgn></Pagination><Abstract><AbstractText>A membrane-bound glutathione S-transferase and a soluble glutathione conjugate reductase constitute the reductive dehalogenase system of P. chrysosporium. This enzyme system reductively removes chlorine substituents from tetrachlorohydroquinone, a metabolite of pentachlorophenol. The membrane-bound glutathione S-transferase converts tetrachlorohydroquinone to S-glutathionyltrichloro-1,4-hydroquinone, which is subsequently reduced to 3,5,6-trichlorohydroquinone by the soluble glutathione conjugate reductase (GCR). This GCR can accept glutathione, dithiothreitol, cysteine, or beta-mercaptoethanol as cosubstrates. GCR was purified to apparent homogeneity by ion-exchange and covalent chromatography. The enzyme exhibits optimum activity at pH 6.0 and 55 degrees C and appears to be a homodimer with a M(r) of approximately 60 kDa. Activity increases as the number of chlorine substituents on the hydroquinone ring is increased. GCR has an apparent K(m) of approximately 33 microM and an apparent k(cat) of approximately 3.43 s(-1) for 2-S-glutathionyl-3,5,6-trichloro-1,4-hydroquinone. Inhibitors of GCR include Cd(2+), Fe(2+), Mn(2+), iodoacetic acid, and p-chloromercuribenzoic acid, suggesting the presence of a catalytic cysteine thiol(s) at the active site. When glutathione is used as a cosubstrate, reduction of S-glutathionyltrichloro-1,4-hydroquinone is accompanied by the production of trichlorohydroquinone and oxidized glutathione in a 1:1 ratio. A mechanism for this novel enzyme is proposed.</AbstractText><CopyrightInformation>Copyright 2001 Academic Press.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Reddy</LastName><ForeName>G V</ForeName><Initials>GV</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Molecular Biology, Oregon Graduate Institute of Science and Technology, Beaverton, Oregon 97006-8921, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Gold</LastName><ForeName>M H</ForeName><Initials>MH</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Arch Biochem 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UI="D006867">Hydrolases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.8.1.-</RegistryNumber><NameOfSubstance UI="C078610">2,3,5,6-tetrachloro-4-hydroquinone reductive dehalogenase</NameOfSubstance></Chemical><Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber><NameOfSubstance UI="D005978">Glutathione</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006863" MajorTopicYN="N">Hydrogen-Ion Concentration</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006867" MajorTopicYN="N">Hydrolases</DescriptorName><QualifierName UI="Q000302" MajorTopicYN="Y">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008077" MajorTopicYN="N">Lipoproteins, LDL</DescriptorName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008670" MajorTopicYN="N">Metals</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="N">Oxidoreductases</DescriptorName><QualifierName UI="Q000302" MajorTopicYN="Y">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020075" MajorTopicYN="N">Phanerochaete</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013438" MajorTopicYN="N">Sulfhydryl Compounds</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013696" MajorTopicYN="N">Temperature</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2001</Year><Month>7</Month><Day>5</Day><Hour>10</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2001</Year><Month>8</Month><Day>10</Day><Hour>10</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2001</Year><Month>7</Month><Day>5</Day><Hour>10</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">11437359</ArticleId><ArticleId IdType="doi">10.1006/abbi.2001.2417</ArticleId><ArticleId IdType="pii">S0003986101924178</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country></list><tree><noCountry><name sortKey="Gold, M H" sort="Gold, M H" uniqKey="Gold M" first="M H" last="Gold">M H Gold</name></noCountry><country name="États-Unis"><noRegion><name sortKey="Reddy, G V" sort="Reddy, G V" uniqKey="Reddy G" first="G V" last="Reddy">G V Reddy</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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