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show all sequences of 1.20.2.1

The NT-26 cytochrome c552 and its role in arsenite oxidation

Santini, J.; Kappler, U.; Ward, S.; Honeychurch, M.; vanden Hoven, R.; Bernhardt, P.; Biochim. Biophys. Acta 1767, 189-196 (2007)

Data extracted from this reference:

Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
arsenite + cytochrome c552 + H2O
arsenite-oxidising bacterium
physiological electron acceptor
arsenate + reduced cytochrome c552
-
-
?
arsenite + cytochrome c552 + H2O
arsenite-oxidising bacterium NT-26
physiological electron acceptor
arsenate + reduced cytochrome c552
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
arsenite-oxidising bacterium
Q6VAL9
subunit aroB
-
arsenite-oxidising bacterium NT-26
Q6VAL9
subunit aroB
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
arsenite + cytochrome c + H2O
horse heart cytochrome c serves as an in vitro elelctron acceptor
714304
arsenite-oxidising bacterium
arsenate + reduced cytochrome c
-
-
-
?
arsenite + cytochrome c + H2O
horse heart cytochrome c serves as an in vitro elelctron acceptor
714304
arsenite-oxidising bacterium NT-26
arsenate + reduced cytochrome c
-
-
-
?
arsenite + cytochrome c552 + H2O
physiological electron acceptor
714304
arsenite-oxidising bacterium
arsenate + reduced cytochrome c552
-
-
-
?
arsenite + cytochrome c552 + H2O
physiological electron acceptor
714304
arsenite-oxidising bacterium NT-26
arsenate + reduced cytochrome c552
-
-
-
?
Cofactor
Cofactor
Commentary
Organism
Structure
cytochrome c552
physiological electron acceptor to the arsenite oxidase, the gene that encodes this protein is located downstream of the arsenite oxidase genes aroBA. Characterisation reveals the presence of a single heme per protein and that the heme redox potential is similar to that of mitochondrial c-type cytochromes
arsenite-oxidising bacterium
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
cytochrome c552
physiological electron acceptor to the arsenite oxidase, the gene that encodes this protein is located downstream of the arsenite oxidase genes aroBA. Characterisation reveals the presence of a single heme per protein and that the heme redox potential is similar to that of mitochondrial c-type cytochromes
arsenite-oxidising bacterium
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
arsenite + cytochrome c552 + H2O
arsenite-oxidising bacterium
physiological electron acceptor
arsenate + reduced cytochrome c552
-
-
?
arsenite + cytochrome c552 + H2O
arsenite-oxidising bacterium NT-26
physiological electron acceptor
arsenate + reduced cytochrome c552
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
arsenite + cytochrome c + H2O
horse heart cytochrome c serves as an in vitro elelctron acceptor
714304
arsenite-oxidising bacterium
arsenate + reduced cytochrome c
-
-
-
?
arsenite + cytochrome c + H2O
horse heart cytochrome c serves as an in vitro elelctron acceptor
714304
arsenite-oxidising bacterium NT-26
arsenate + reduced cytochrome c
-
-
-
?
arsenite + cytochrome c552 + H2O
physiological electron acceptor
714304
arsenite-oxidising bacterium
arsenate + reduced cytochrome c552
-
-
-
?
arsenite + cytochrome c552 + H2O
physiological electron acceptor
714304
arsenite-oxidising bacterium NT-26
arsenate + reduced cytochrome c552
-
-
-
?
Other publictions for EC 1.20.2.1
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
727089
Kalimuthu
Electrochemically driven catal ...
Rhizobium sp.
Biochim. Biophys. Acta
1837
112-120
2014
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1
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1
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1
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1
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1
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1
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-
713822
Branco
Identification of an aox syste ...
Ochrobactrum tritici, Ochrobactrum tritici SCII24
Appl. Environ. Microbiol.
75
5141-5147
2009
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-
1
-
1
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2
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8
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4
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1
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2
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4
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4
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-
2
-
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-
1
1
2
2
-
-
714842
Duquesne
Arsenite oxidation by a chemoa ...
Thiomonas sp., Thiomonas sp. 3AS
Environ. Microbiol.
10
228-237
2008
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-
-
-
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1
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4
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3
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2
-
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-
-
-
-
1
-
-
2
-
-
714304
Santini
The NT-26 cytochrome c552 and ...
arsenite-oxidising bacterium, arsenite-oxidising bacterium NT-26
Biochim. Biophys. Acta
1767
189-196
2007
-
-
-
-
-
-
-
-
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-
-
2
-
3
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4
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1
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1
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2
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4
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658195
vanden Hoven
Arsenite oxidation by the hete ...
Hydrogenophaga sp., Hydrogenophaga sp. NT-14
Biochim. Biophys. Acta
1656
148-155
2004
-
-
-
-
-
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-
1
1
2
3
2
-
2
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1
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1
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4
1
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1
1
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1
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1
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1
1
2
3
2
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1
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1
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4
1
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1
1
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-
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-
715352
Santini
Molybdenum-containing arsenite ...
arsenite-oxidising bacterium, arsenite-oxidising bacterium NT-26, Rhizobium sp. NT-26
J. Bacteriol.
186
1614-1619
2004
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2
2
2
6
-
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4
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2
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3
2
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2
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2
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2
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2
2
2
6
-
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2
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3
2
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2
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1
1
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