Properties of the arsenate reductase of plasmid R773.
Identifieur interne : 001244 ( Main/Exploration ); précédent : 001243; suivant : 001245Properties of the arsenate reductase of plasmid R773.
Auteurs : T B Gladysheva [États-Unis] ; K L Oden ; B P RosenSource :
- Biochemistry [ 0006-2960 ] ; 1994.
Descripteurs français
- KwdFr :
- Adenosine triphosphatases (antagonistes et inhibiteurs), Adenosine triphosphatases (génétique), Adenosine triphosphatases (métabolisme), Arsenite Transporting ATPases (MeSH), Cinétique (MeSH), Complexes multienzymatiques (MeSH), Escherichia coli (génétique), Oxydoréduction (MeSH), Plasmides (MeSH), Pompes ioniques (MeSH), Spécificité du substrat (MeSH).
- MESH :
- antagonistes et inhibiteurs : Adenosine triphosphatases.
- génétique : Adenosine triphosphatases, Escherichia coli.
- métabolisme : Adenosine triphosphatases.
- Arsenite Transporting ATPases, Cinétique, Complexes multienzymatiques, Oxydoréduction, Plasmides, Pompes ioniques, Spécificité du substrat.
English descriptors
- KwdEn :
- Adenosine Triphosphatases (antagonists & inhibitors), Adenosine Triphosphatases (genetics), Adenosine Triphosphatases (metabolism), Arsenite Transporting ATPases (MeSH), Escherichia coli (genetics), Ion Pumps (MeSH), Kinetics (MeSH), Multienzyme Complexes (MeSH), Oxidation-Reduction (MeSH), Plasmids (MeSH), Substrate Specificity (MeSH).
- MESH :
- chemical , antagonists & inhibitors : Adenosine Triphosphatases.
- chemical , genetics : Adenosine Triphosphatases.
- chemical , metabolism : Adenosine Triphosphatases.
- chemical : Arsenite Transporting ATPases, Ion Pumps, Multienzyme Complexes.
- genetics : Escherichia coli.
- Kinetics, Oxidation-Reduction, Plasmids, Substrate Specificity.
Abstract
Resistance to toxic oxyanions in Escherichia coli is conferred by the ars operon carried on plasmid R773. The gene products of this operon catalyze extrusion of antimonials and arsenicals from cells of E. coli, thus providing resistance to those toxic oxyanions. In addition, resistance to arsenate is conferred by the product of the arsC gene. In this report, purified ArsC protein was shown to catalyze reduction of arsenate to arsenite. The enzymatic activity of the ArsC protein required glutaredoxin as a source of reducing equivalents. Other reductants, including glutathione and thioredoxin, were not effective electron donors. A spectrophotometric assay was devised in which arsenate reduction was coupled to NADPH oxidation. The results obtained with the coupled assay corresponded to those found by direct reduction of radioactive arsenate to arsenite. The only substrate of the reaction was arsenate (Km = 8 mM); other oxyanions including phosphate, sulfate, and antimonate were not reduced. Phosphate and sulfate were weak inhibitors, while the product, arsenite, was a stronger inhibitor (Ki = 0.1 mM). Arsenate reductase activity exhibited a pH optimum of 6.3-6.8. These results indicate that the ArsC protein is a novel reductase, and elucidation of its enzymatic mechanism should be of interest.
DOI: 10.1021/bi00189a033
PubMed: 8003492
Affiliations:
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Le document en format XML
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type="state">Michigan</region></placeName><wicri:cityArea>Department of Biochemistry, Wayne State University School of Medicine, Detroit</wicri:cityArea></affiliation></author><author><name sortKey="Oden, K L" sort="Oden, K L" uniqKey="Oden K" first="K L" last="Oden">K L Oden</name></author><author><name sortKey="Rosen, B P" sort="Rosen, B P" uniqKey="Rosen B" first="B P" last="Rosen">B P Rosen</name></author></analytic><series><title level="j">Biochemistry</title><idno type="ISSN">0006-2960</idno><imprint><date when="1994" type="published">1994</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Adenosine Triphosphatases (antagonists & inhibitors)</term><term>Adenosine Triphosphatases (genetics)</term><term>Adenosine Triphosphatases (metabolism)</term><term>Arsenite Transporting ATPases (MeSH)</term><term>Escherichia coli (genetics)</term><term>Ion Pumps (MeSH)</term><term>Kinetics (MeSH)</term><term>Multienzyme Complexes (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Plasmids (MeSH)</term><term>Substrate Specificity (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Adenosine triphosphatases (antagonistes et inhibiteurs)</term><term>Adenosine triphosphatases (génétique)</term><term>Adenosine triphosphatases (métabolisme)</term><term>Arsenite Transporting ATPases (MeSH)</term><term>Cinétique (MeSH)</term><term>Complexes multienzymatiques (MeSH)</term><term>Escherichia coli (génétique)</term><term>Oxydoréduction (MeSH)</term><term>Plasmides (MeSH)</term><term>Pompes ioniques (MeSH)</term><term>Spécificité du substrat (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Adenosine Triphosphatases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Adenosine Triphosphatases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Adenosine Triphosphatases</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Arsenite Transporting ATPases</term><term>Ion Pumps</term><term>Multienzyme Complexes</term></keywords><keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>Adenosine triphosphatases</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Escherichia coli</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Adenosine triphosphatases</term><term>Escherichia coli</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Adenosine triphosphatases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Kinetics</term><term>Oxidation-Reduction</term><term>Plasmids</term><term>Substrate Specificity</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Arsenite Transporting ATPases</term><term>Cinétique</term><term>Complexes multienzymatiques</term><term>Oxydoréduction</term><term>Plasmides</term><term>Pompes ioniques</term><term>Spécificité du substrat</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Resistance to toxic oxyanions in Escherichia coli is conferred by the ars operon carried on plasmid R773. The gene products of this operon catalyze extrusion of antimonials and arsenicals from cells of E. coli, thus providing resistance to those toxic oxyanions. In addition, resistance to arsenate is conferred by the product of the arsC gene. In this report, purified ArsC protein was shown to catalyze reduction of arsenate to arsenite. The enzymatic activity of the ArsC protein required glutaredoxin as a source of reducing equivalents. Other reductants, including glutathione and thioredoxin, were not effective electron donors. A spectrophotometric assay was devised in which arsenate reduction was coupled to NADPH oxidation. The results obtained with the coupled assay corresponded to those found by direct reduction of radioactive arsenate to arsenite. The only substrate of the reaction was arsenate (Km = 8 mM); other oxyanions including phosphate, sulfate, and antimonate were not reduced. Phosphate and sulfate were weak inhibitors, while the product, arsenite, was a stronger inhibitor (Ki = 0.1 mM). Arsenate reductase activity exhibited a pH optimum of 6.3-6.8. These results indicate that the ArsC protein is a novel reductase, and elucidation of its enzymatic mechanism should be of interest.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">8003492</PMID><DateCompleted><Year>1994</Year><Month>07</Month><Day>21</Day></DateCompleted><DateRevised><Year>2019</Year><Month>06</Month><Day>13</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0006-2960</ISSN><JournalIssue CitedMedium="Print"><Volume>33</Volume><Issue>23</Issue><PubDate><Year>1994</Year><Month>Jun</Month><Day>14</Day></PubDate></JournalIssue><Title>Biochemistry</Title><ISOAbbreviation>Biochemistry</ISOAbbreviation></Journal><ArticleTitle>Properties of the arsenate reductase of plasmid R773.</ArticleTitle><Pagination><MedlinePgn>7288-93</MedlinePgn></Pagination><Abstract><AbstractText>Resistance to toxic oxyanions in Escherichia coli is conferred by the ars operon carried on plasmid R773. The gene products of this operon catalyze extrusion of antimonials and arsenicals from cells of E. coli, thus providing resistance to those toxic oxyanions. In addition, resistance to arsenate is conferred by the product of the arsC gene. In this report, purified ArsC protein was shown to catalyze reduction of arsenate to arsenite. The enzymatic activity of the ArsC protein required glutaredoxin as a source of reducing equivalents. Other reductants, including glutathione and thioredoxin, were not effective electron donors. A spectrophotometric assay was devised in which arsenate reduction was coupled to NADPH oxidation. The results obtained with the coupled assay corresponded to those found by direct reduction of radioactive arsenate to arsenite. The only substrate of the reaction was arsenate (Km = 8 mM); other oxyanions including phosphate, sulfate, and antimonate were not reduced. Phosphate and sulfate were weak inhibitors, while the product, arsenite, was a stronger inhibitor (Ki = 0.1 mM). Arsenate reductase activity exhibited a pH optimum of 6.3-6.8. These results indicate that the ArsC protein is a novel reductase, and elucidation of its enzymatic mechanism should be of interest.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Gladysheva</LastName><ForeName>T B</ForeName><Initials>TB</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, Wayne State University School of Medicine, Detroit, Michigan 48201.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Oden</LastName><ForeName>K L</ForeName><Initials>KL</Initials></Author><Author ValidYN="Y"><LastName>Rosen</LastName><ForeName>B P</ForeName><Initials>BP</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>CA54141</GrantID><Acronym>CA</Acronym><Agency>NCI NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013487">Research Support, U.S. Gov't, P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Biochemistry</MedlineTA><NlmUniqueID>0370623</NlmUniqueID><ISSNLinking>0006-2960</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D016623">Ion Pumps</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D009097">Multienzyme Complexes</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.6.1.-</RegistryNumber><NameOfSubstance UI="D000251">Adenosine Triphosphatases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.6.3.16</RegistryNumber><NameOfSubstance UI="D053501">Arsenite Transporting ATPases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><GeneSymbolList><GeneSymbol>arsC</GeneSymbol></GeneSymbolList><MeshHeadingList><MeshHeading><DescriptorName UI="D000251" MajorTopicYN="N">Adenosine Triphosphatases</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D053501" MajorTopicYN="N">Arsenite Transporting ATPases</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016623" MajorTopicYN="Y">Ion Pumps</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009097" MajorTopicYN="Y">Multienzyme Complexes</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010957" MajorTopicYN="Y">Plasmids</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1994</Year><Month>6</Month><Day>14</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1994</Year><Month>6</Month><Day>14</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1994</Year><Month>6</Month><Day>14</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">8003492</ArticleId><ArticleId IdType="doi">10.1021/bi00189a033</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>Michigan</li></region></list><tree><noCountry><name sortKey="Oden, K L" sort="Oden, K L" uniqKey="Oden K" first="K L" last="Oden">K L Oden</name><name sortKey="Rosen, B P" sort="Rosen, B P" uniqKey="Rosen B" first="B P" last="Rosen">B P Rosen</name></noCountry><country name="États-Unis"><region name="Michigan"><name sortKey="Gladysheva, T B" sort="Gladysheva, T B" uniqKey="Gladysheva T" first="T B" last="Gladysheva">T B Gladysheva</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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