Information on EC 1.20.2.1 - arsenate reductase (cytochrome c)

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.20.2.1
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RECOMMENDED NAME
GeneOntology No.
arsenate reductase (cytochrome c)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
arsenite + H2O + 2 oxidized cytochrome c = arsenate + 2 reduced cytochrome c + 2 H+
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
arsenite oxidation I (respiratory)
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SYSTEMATIC NAME
IUBMB Comments
arsenite:cytochrome c oxidoreductase
A molybdoprotein containing iron-sulfur clusters. Isolated from alpha-proteobacteria. Unlike EC 1.20.9.1, arsenate reductase (azurin), it does not use azurin as acceptor.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
arsenite-oxidising bacterium
subunit aroB
UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
arsenite + cytochrome c + H2O
arsenate + reduced cytochrome c
show the reaction diagram
arsenite + cytochrome c-551 + H2O
arsenate + reduced cytochrome c-551
show the reaction diagram
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the bacterium obtains energy from the reaction, required for chemolithoautotrophic growth
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?
arsenite + cytochrome c552 + H2O
arsenate + reduced cytochrome c552
show the reaction diagram
arsenite + H2O + 2,6-dichlorophenolindophenol
arsenate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
additional information
?
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mediated electrocatalytic voltammetry study. In the absence of arsenite, or the enzyme, cytochrome c552 cofactor exhibits a well-defined single electron reversible response at a Au electrode modified with the long chain mercaptoundecanoic acid, which presents a self-assembled monolayer of negatively charged functional groups to the protein surface. In the presence of arsenite and enzyme a variety of CV waveforms are observed depending on sweep rate and substrate concentration. Arsenite binding is very fast
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
arsenite + cytochrome c-551 + H2O
arsenate + reduced cytochrome c-551
show the reaction diagram
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the bacterium obtains energy from the reaction, required for chemolithoautotrophic growth
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?
arsenite + cytochrome c552 + H2O
arsenate + reduced cytochrome c552
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome c-551
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physiological electron acceptor for the arsenite oxidase
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cytochrome c552
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iron-sulfur centre
the large subunit aoxB has the [3Fe-4S] cluster-binding motif as well as the residues proposed to bind arsenite; the small subunit aoxA has a characteristic Tat signal sequence and contains the residues binding the [2Fe-2S] Rieske-type cluster
molybdenum cofactor
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Molybdenum
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protein contains 10.6 mol iron per alpha3beta3 unit and 2.1 mol molybdenum per alpha3beta3 molybdenum
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.035 - 0.061
arsenite
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8.6 - 30.4
arsenite
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.6
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pH 5.5, temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
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assay at
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
16000
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3 * 86000, AroA, + 3 * 16000, AroB, alpha3beta3, SDS-PAGE
86000
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3 * 86000, AroA, + 3 * 16000, AroB, alpha3beta3, SDS-PAGE
219000
306000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
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3 * 86000, AroA, + 3 * 16000, AroB, alpha3beta3, SDS-PAGE
tetramer
additional information
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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functional expression in Ochrobacterium tritici 5bvl1, a non-As(III) oxidizer; functional expression in Ochrobacterium tritici 5bvl1, a non-As(III) oxidizer
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
coexpression of genes aoxA, aoxB and cytC independent of the remaining genes of the operon, aoxS and aoxR; coexpression of genes aoxA, aoxB and cytC independent of the remaining genes of the operon, aoxS and aoxR
induced by growth on arsenite; induced by growth on arsenite
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information