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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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
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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UniProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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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
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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 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
14000
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1* 85000, subunit LSU, plus 1 * 14000, subunit SSU, SDS-PAGE
29000
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1 * 87000 + 1 * 29000, SDS-PAGE
85000
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gel filtration
87000
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1 * 87000 + 1 * 29000, SDS-PAGE
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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