GlutaredoxinV1, Main, Exploration, bibRecord, 001002

Arsenate reductases in prokaryotes and eukaryotes.

Identifieur interne : 001002 ( Main/Exploration ); précédent : 001001; suivant : 001003

Arsenate reductases in prokaryotes and eukaryotes.

Auteurs : Rita Mukhopadhyay [États-Unis] ; Barry P. Rosen

Source :

Environmental health perspectives [ 0091-6765 ] ; 2002.

RBID : pubmed:12426124

Descripteurs français

KwdFr :
- Arsenate Reductases (MeSH), Arsenic (métabolisme), Arsenite Transporting ATPases (MeSH), Arséniates (pharmacologie), Complexes multienzymatiques (pharmacologie), Escherichia coli (enzymologie), Oxydoréduction (MeSH), Pompes ioniques (pharmacologie), Protéines de Saccharomyces cerevisiae (MeSH), Résistance aux substances (MeSH), Saccharomyces cerevisiae (enzymologie).
MESH :
- enzymologie : Escherichia coli, Saccharomyces cerevisiae.
- métabolisme : Arsenic.
- pharmacologie : Arséniates, Complexes multienzymatiques, Pompes ioniques.
- Arsenate Reductases, Arsenite Transporting ATPases, Oxydoréduction, Protéines de Saccharomyces cerevisiae, Résistance aux substances.

English descriptors

KwdEn :
- Arsenate Reductases (MeSH), Arsenates (pharmacology), Arsenic (metabolism), Arsenite Transporting ATPases (MeSH), Drug Resistance (MeSH), Escherichia coli (enzymology), Ion Pumps (pharmacology), Multienzyme Complexes (pharmacology), Oxidation-Reduction (MeSH), Saccharomyces cerevisiae (enzymology), Saccharomyces cerevisiae Proteins (MeSH).
MESH :
- chemical , metabolism : Arsenic.
- chemical , pharmacology : Arsenates, Ion Pumps, Multienzyme Complexes.
- chemical : Arsenate Reductases, Arsenite Transporting ATPases, Saccharomyces cerevisiae Proteins.
- enzymology : Escherichia coli, Saccharomyces cerevisiae.
- Drug Resistance, Oxidation-Reduction.

Abstract

The ubiquity of arsenic in the environment has led to the evolution of enzymes for arsenic detoxification. An initial step in arsenic metabolism is the enzymatic reduction of arsenate [As(V)] to arsenite [As(III)]. At least three families of arsenate reductase enzymes have arisen, apparently by convergent evolution. The properties of two of these are described here. The first is the prokaryotic ArsC arsenate reductase of Escherichia coli. The second, Acr2p of Saccharomyces cerevisiae, is the only identified eukaryotic arsenate reductase. Although unrelated to each other, both enzymes receive their reducing equivalents from glutaredoxin and reduced glutathione. The structure of the bacterial ArsC has been solved at 1.65 A. As predicted from its biochemical properties, ArsC structures with covalent enzyme-arsenic intermediates that include either As(V) or As(III) were observed. The yeast Acr2p has an active site motif HC(X)(5)R that is conserved in protein phosphotyrosine phosphatases and rhodanases, suggesting that these three groups of enzymes may have evolved from an ancestral oxyanion-binding protein.

DOI: 10.1289/ehp.02110s5745
PubMed: 12426124
PubMed Central: PMC1241237

Affiliations:

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Le document en format XML

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<term>Arsenates (pharmacology)</term>
<term>Arsenic (metabolism)</term>
<term>Arsenite Transporting ATPases (MeSH)</term>
<term>Drug Resistance (MeSH)</term>
<term>Escherichia coli (enzymology)</term>
<term>Ion Pumps (pharmacology)</term>
<term>Multienzyme Complexes (pharmacology)</term>
<term>Oxidation-Reduction (MeSH)</term>
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<term>Arsenite Transporting ATPases (MeSH)</term>
<term>Arséniates (pharmacologie)</term>
<term>Complexes multienzymatiques (pharmacologie)</term>
<term>Escherichia coli (enzymologie)</term>
<term>Oxydoréduction (MeSH)</term>
<term>Pompes ioniques (pharmacologie)</term>
<term>Protéines de Saccharomyces cerevisiae (MeSH)</term>
<term>Résistance aux substances (MeSH)</term>
<term>Saccharomyces cerevisiae (enzymologie)</term>
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<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Arsenic</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Arsenates</term>
<term>Ion Pumps</term>
<term>Multienzyme Complexes</term>
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<keywords scheme="MESH" type="chemical" xml:lang="en"><term>Arsenate Reductases</term>
<term>Arsenite Transporting ATPases</term>
<term>Saccharomyces cerevisiae Proteins</term>
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<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Escherichia coli</term>
<term>Saccharomyces cerevisiae</term>
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<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Escherichia coli</term>
<term>Saccharomyces cerevisiae</term>
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<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Arsenic</term>
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<term>Oxidation-Reduction</term>
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<term>Arsenite Transporting ATPases</term>
<term>Oxydoréduction</term>
<term>Protéines de Saccharomyces cerevisiae</term>
<term>Résistance aux substances</term>
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<front><div type="abstract" xml:lang="en">The ubiquity of arsenic in the environment has led to the evolution of enzymes for arsenic detoxification. An initial step in arsenic metabolism is the enzymatic reduction of arsenate [As(V)] to arsenite [As(III)]. At least three families of arsenate reductase enzymes have arisen, apparently by convergent evolution. The properties of two of these are described here. The first is the prokaryotic ArsC arsenate reductase of Escherichia coli. The second, Acr2p of Saccharomyces cerevisiae, is the only identified eukaryotic arsenate reductase. Although unrelated to each other, both enzymes receive their reducing equivalents from glutaredoxin and reduced glutathione. The structure of the bacterial ArsC has been solved at 1.65 A. As predicted from its biochemical properties, ArsC structures with covalent enzyme-arsenic intermediates that include either As(V) or As(III) were observed. The yeast Acr2p has an active site motif HC(X)(5)R that is conserved in protein phosphotyrosine phosphatases and rhodanases, suggesting that these three groups of enzymes may have evolved from an ancestral oxyanion-binding protein.</div>
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<ReferenceList><Reference><Citation>Structure. 2001 Nov;9(11):1071-81</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11709171</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 1995 Jun 20;92(13):5910-4</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7597052</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochemistry. 1992 Sep 29;31(38):9288-93</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1390715</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Environ Health Perspect. 1992 Jul;97:259-67</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1396465</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochemistry. 1994 Jun 14;33(23):7288-93</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8003492</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochemistry. 1994 Jun 14;33(23):7294-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8003493</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 1994 Oct 11;91(21):9813-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7937896</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochemistry. 1995 Oct 17;34(41):13472-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7577935</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Yeast. 1997 Jul;13(9):819-28</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9234670</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Cell. 1998 May 15;93(4):617-25</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9604936</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Mol Biol. 1998 Sep 11;282(1):195-208</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9733650</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>FEMS Microbiol Lett. 1998 Nov 1;168(1):127-36</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9812373</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Trends Microbiol. 1999 May;7(5):207-12</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10354596</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1999 Dec 17;274(51):36039-42</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10593884</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Chem Res Toxicol. 2000 Jan;13(1):26-30</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10649963</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2000 Jul 14;275(28):21149-57</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10801893</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2001 Sep 14;276(37):34738-42</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11461905</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 2001 Nov 20;98(24):13577-82</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11698660</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
</PubmedData>
</pubmed>
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Arsenate reductases in prokaryotes and eukaryotes.

Arsenate reductases in prokaryotes and eukaryotes.

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Descripteurs français

English descriptors

Abstract

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