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Information on EC 1.20.4.1 - arsenate reductase (glutathione/glutaredoxin) and Organism(s) Staphylococcus aureus and UniProt Accession P0A006

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IUBMB Comments
The enzyme is part of a system for detoxifying arsenate. The substrate binds to a catalytic cysteine residue, forming a covalent thiolate---As(V) intermediate. A tertiary intermediate is then formed between the arsenic, the enzyme's cysteine, and a glutathione cysteine. This intermediate is reduced by glutaredoxin, which forms a dithiol with the glutathione, leading to the dissociation of arsenite. Thus reduction of As(V) is mediated by three cysteine residues: one in ArsC, one in glutathione, and one in glutaredoxin. Although the arsenite formed is more toxic than arsenate, it can be extruded from some bacteria by EC 7.3.2.7, arsenite-transporting ATPase; in other organisms, arsenite can be methylated by EC 2.1.1.137, arsenite methyltransferase, in a pathway that produces non-toxic organoarsenical compounds. cf. EC 1.20.4.4, arsenate reductase (thioredoxin).
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Staphylococcus aureus
UNIPROT: P0A006
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Word Map
The taxonomic range for the selected organisms is: Staphylococcus aureus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
arsenate reductase, asv reductase, acr2p, pvgrx5, slr0946, synarsc, all0195, pcacr2, mxan_0575, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acr2p
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-
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ArsC
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arsenate reductase (glutaredoxin)
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gene arsC proteins
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glutathione:arsenate oxidoreductase
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proteins (specific proteins and subclasses), gene arsC
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reductase, arsenate
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-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
arsenate + glutathione + glutaredoxin = arsenite + a glutaredoxin-glutathione disulfide + H2O
show the reaction diagram
first reaction step is a nucleophilic displacement reaction by C10 on dianionic arsenate. Second step is a preferential nucleophilic attack of C82 on the monoanionic C10-arsenate intermediate stabilized by S17. Thiolate form of C82 is stabilized by an eight-residue alpha helix flanked by C82 and C89 and a hydrogen bond with T11. during the final step, C89 is activated as a nucleophile by structural alterations of the redox helix
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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PATHWAY SOURCE
PATHWAYS
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-, -, -, -
SYSTEMATIC NAME
IUBMB Comments
arsenate:glutathione/glutaredoxin oxidoreductase
The enzyme is part of a system for detoxifying arsenate. The substrate binds to a catalytic cysteine residue, forming a covalent thiolate---As(V) intermediate. A tertiary intermediate is then formed between the arsenic, the enzyme's cysteine, and a glutathione cysteine. This intermediate is reduced by glutaredoxin, which forms a dithiol with the glutathione, leading to the dissociation of arsenite. Thus reduction of As(V) is mediated by three cysteine residues: one in ArsC, one in glutathione, and one in glutaredoxin. Although the arsenite formed is more toxic than arsenate, it can be extruded from some bacteria by EC 7.3.2.7, arsenite-transporting ATPase; in other organisms, arsenite can be methylated by EC 2.1.1.137, arsenite methyltransferase, in a pathway that produces non-toxic organoarsenical compounds. cf. EC 1.20.4.4, arsenate reductase (thioredoxin).
CAS REGISTRY NUMBER
COMMENTARY hide
146907-46-2
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ARSC_STAAU
131
0
14813
Swiss-Prot
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N13A
decrease in activity due to lower local softness, analysis of S-As bond length, Wiberg bond orders, lewaving group energy and nucleofugality
R16A
decrease in activity due to lower local softness, analysis of S-As bond length, Wiberg bond orders, lewaving group energy and nucleofugality
S17A
decrease in activity due to lower local softness, analysis of S-As bond length, Wiberg bond orders, lewaving group energy and nucleofugality
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Roos, G.; Loverix, S.; Brosens, E.; Van Belle, K.; Wyns, L.; Geerlings, P.; Messens, J.
The activation of electrophile, nucleophile and leaving group during the reaction catalysed by pI258 arsenate reductase
Chembiochem
7
981-989
2006
Staphylococcus aureus (P0A006)
Manually annotated by BRENDA team