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Information on EC 1.20.4.4 - arsenate reductase (thioredoxin) and Organism(s) Bacillus subtilis and UniProt Accession P45947
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1.20.4.4 arsenate reductase (thioredoxin)IUBMB Comments
The enzyme, characterized in bacteria of the Firmicutes phylum, is specific for thioredoxin . It has no activity with glutaredoxin [cf. EC 1.20.4.1, arsenate reductase (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. The enzyme also has the activity of EC 3.1.3.48, protein-tyrosine-phosphatase .
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The taxonomic range for the selected organisms is: Bacillus subtilis
The expected taxonomic range for this enzyme is: Bacteria, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
arsc3, sa_arsc, pi258 arsenate reductase, thioredoxin-coupled arsenate reductase, bs_arsc, arsc1', thioredoxin-arsenate reductase complex, trx-coupled arsenate reductase, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
thioredoxin-coupled arsenate reductase
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
arsenate:thioredoxin oxidoreductase
The enzyme, characterized in bacteria of the Firmicutes phylum, is specific for thioredoxin [1]. It has no activity with glutaredoxin [cf. EC 1.20.4.1, arsenate reductase (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. The enzyme also has the activity of EC 3.1.3.48, protein-tyrosine-phosphatase [3].
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
arsenate + thioredoxin
arsenite + thioredoxin disulfide + H2O
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
mechanism by which potassium and tetrahedral oxyanions affect catalysis within the Trx-coupled family of arsenate reductases
-
additional information
-
mechanism by which potassium and tetrahedral oxyanions affect catalysis within the Trx-coupled family of arsenate reductases
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.047
arsenate
wild-type Bacillus subtilis, condition: 50 mM K2SO4, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters
0.054
arsenate
wild-type Bacillus subtilis, condition: 150 mM KCl, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters
0.058
arsenate
wild-type Bacillus subtilis, condition: 150 mM NaCl, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters
0.064
arsenate
wild-type Bacillus subtilis, condition: 50 mM Na2SO4, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.3
arsenate
wild-type Bacillus subtilis, condition: 150 mM NaCl, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters
1.6
arsenate
wild-type Bacillus subtilis, condition: 150 mM KCl, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters
1.6
arsenate
wild-type Bacillus subtilis, condition: 50 mM K2SO4, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters
2
arsenate
wild-type Bacillus subtilis, condition: 50 mM Na2SO4, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
22.4
arsenate
wild-type Bacillus subtilis, condition: 150 mM NaCl, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters
29.6
arsenate
wild-type Bacillus subtilis, condition: 150 mM KCl, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters
31.3
arsenate
wild-type Bacillus subtilis, condition: 50 mM Na2SO4, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters
34
arsenate
wild-type Bacillus subtilis, condition: 50 mM K2SO4, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C10S/C15A/C82S
mutant in complex with the thioredoxin C32S mutant. Solve the structure of the Trx-ArsC complex by NMR spectroscopy
additional information
additional information
commonly occurring mutation of a histidine (H62), located about 6 A from the potassium-binding site in Sa_ArsC, to a glutamine uncouples the kinetic dependency on potassium. Mutations within the Trx-coupled family of arsenate reductases lead to subtly different ion-dependent kinetic features
additional information
-
commonly occurring mutation of a histidine (H62), located about 6 A from the potassium-binding site in Sa_ArsC, to a glutamine uncouples the kinetic dependency on potassium. Mutations within the Trx-coupled family of arsenate reductases lead to subtly different ion-dependent kinetic features
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Li, Y.; Hu, Y.; Zhang, X.; Xu, H.; Lescop, E.; Xia, B.; Jin, C.
Conformational fluctuations coupled to the thiol-disulfide transfer between thioredoxin and arsenate reductase in Bacillus subtilis
J. Biol. Chem.
282
11078-11083
2007
Bacillus subtilis (P45947), Bacillus subtilis
Roos, G.; Buts, L.; Van Belle, K.; Brosens, E.; Geerlings, P.; Loris, R.; Wyns, L.; Messens, J.
Interplay between ion binding and catalysis in the thioredoxin-coupled arsenate reductase family
J. Mol. Biol.
360
826-838
2006
Bacillus subtilis (P45947), Bacillus subtilis, Staphylococcus aureus (P0A006), Staphylococcus aureus
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