Information on EC 1.20.9.1 - arsenate reductase (azurin)

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.20.9.1
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RECOMMENDED NAME
GeneOntology No.
arsenate reductase (azurin)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
arsenite + H2O + 2 oxidized azurin = arsenate + 2 reduced azurin + 2 H+
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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-
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
arsenite oxidation II (respiratory)
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SYSTEMATIC NAME
IUBMB Comments
arsenite:azurin oxidoreductase
Contains a molybdopterin centre comprising two molybdopterin guanosine dinucleotide cofactors bound to molybdenum, a [3Fe-4S] cluster and a Rieske-type [2Fe-2S] cluster. Isolated from beta-proteobacteria. Also uses a c-type cytochrome or O2 as acceptors.
CAS REGISTRY NUMBER
COMMENTARY hide
144638-82-4
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain NT10
UniProt
Manually annotated by BRENDA team
strain WA20
UniProt
Manually annotated by BRENDA team
strain WA19
UniProt
Manually annotated by BRENDA team
strain WA19
UniProt
Manually annotated by BRENDA team
strain Ben5
UniProt
Manually annotated by BRENDA team
strain Ben5
UniProt
Manually annotated by BRENDA team
strain 5A
UniProt
Manually annotated by BRENDA team
strain 5A
UniProt
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
Hydrogenophaga sp.
strain NT14
UniProt
Manually annotated by BRENDA team
strain WA13
UniProt
Manually annotated by BRENDA team
strain DM1
UniProt
Manually annotated by BRENDA team
strain DM1
UniProt
Manually annotated by BRENDA team
strain NT-26
-
-
Manually annotated by BRENDA team
strain NT26
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-
Manually annotated by BRENDA team
strain NT4
UniProt
Manually annotated by BRENDA team
strain NT4
UniProt
Manually annotated by BRENDA team
strain HR13
UniProt
Manually annotated by BRENDA team
strain HR13
UniProt
Manually annotated by BRENDA team
strain HB8
UniProt
Manually annotated by BRENDA team
strain RM1
UniProt
Manually annotated by BRENDA team
strain RM1
UniProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
arsenate + azurin(red)
arsenite + H2O + azurin(ox)
show the reaction diagram
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-
-
-
?
arsenite + 2,6-dichlorophenol indophenol
arsenate + reduced 2,6-dichlorophenol indophenol
show the reaction diagram
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-
?
arsenite + H2O + azurin(ox)
arsenate + azurin(red)
show the reaction diagram
arsenite + H2O + azurin(oxidized)
arsenate + azurin(reduced)
show the reaction diagram
additional information
?
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enzyme is expressed during the exponential and stationary phases of growth. Arsenite oxidase, azurin and cytochrome c may form the basis of an electron transport chain
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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
additional information
?
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enzyme is expressed during the exponential and stationary phases of growth. Arsenite oxidase, azurin and cytochrome c may form the basis of an electron transport chain
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
iron-sulfur centre
the large subunit contains a [3Fe-4S] cluster. The small subunit contains a Rieske-type [2Fe-2S] site; the large subunit contains a [3Fe-4S] cluster. The small subunit contains a Rieske-type [2Fe-2S] site
molybdopterin
the large subunit contains a Mo site, consisting of a Mo atom bound to two pterin cofactors
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Iron
the large subunit contains a [3Fe-4S] cluster. The small subunit contains a Rieske-type [2Fe-2S] site; the large subunit contains a [3Fe-4S] cluster. The small subunit contains a Rieske-type [2Fe-2S] site
Molybdenum
the large subunit contains a Mo site, consisting of a Mo atom bound to two pterin cofactors
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Co2+
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1 mM, 1.5% residual activity
diethyldicarbonate
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1 mM, 5% residual activity
Zn2+
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1 mM, 1.8% residual activity
additional information
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not inhibitory: 1 mM of Na+, Ca2+, Fe2+, Mo6+ and EDTA
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
expression of the aroA-like gene in Variovorax sp. strain RM1 is induced by arsenite
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.3
arsenate
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0.026 - 0.07
arsenite
0.008
azurin
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
14400
arsenate
Chrysiogenes arsenatis
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27
azurin
Alcaligenes faecalis
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 35
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more than 92% residual activity
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
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enzyme is expressed during the exponential and stationary phases of growth
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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about 90% of enzyme activity within the membrane fraction
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
85000
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gel filtration
100000
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PAGE
123000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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SDS-PAGE
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; crystal structure of arsenite oxidase to 2.03A in a P21 crystal form with two molecules in the asymmetric unit and to 1.64 A in a P1 crystal form with four molecules in the asymmetric unit. The large subunit contains a Mo site, consisting of a Mo atom bound to two pterin cofactors, and a [3Fe-4S] cluster. The small subunit contains a Rieske-type [2Fe-2S] site; crystal structure of arsenite oxidase to 2.03A in a P21 crystal form with two molecules in the asymmetric unit and to 1.64 A in a P1 crystal form with four molecules in the asymmetric unit. The large subunit contains a Mo site, consisting of a Mo atom bound to two pterin cofactors, and a [3Fe-4S] cluster. The small subunit contains a Rieske-type [2Fe-2S] site
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
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78% residual activity
696599
7
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85% residual activity
696599
8
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82% residual activity
696599
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
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1 h, 70% residual activity
45
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1 h, 55% residual activity
50
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1 h, 15% residual activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, 50 mM MES-buffer, pH 5.5, 100 mM NaCl
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gel filtration
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
environmental protection
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important implications for biomediation of arsenite contaminated soils and groud water
additional information
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