Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • 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 (2006), J. Mol. Biol., 360, 826-838.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.20.4.4 additional information mechanism by which potassium and tetrahedral oxyanions affect catalysis within the Trx-coupled family of arsenate reductases Staphylococcus aureus
1.20.4.4 additional information mechanism by which potassium and tetrahedral oxyanions affect catalysis within the Trx-coupled family of arsenate reductases Bacillus subtilis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.20.4.4 expressed in Escherichia coli Staphylococcus aureus
1.20.4.4 expressed in Escherichia coli Bacillus subtilis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.20.4.4 x-ray structures of the mutants Staphylococcus aureus
1.20.4.4 x-ray structures of the mutants Bacillus subtilis

Protein Variants

EC Number Protein Variants Comment Organism
1.20.4.4 C10S/C15A change of the P-loop geometry Staphylococcus aureus
1.20.4.4 H62Q change of the P-loop geometry Staphylococcus aureus
1.20.4.4 H62Q/N33K site directed mutagenesis Staphylococcus aureus
1.20.4.4 H62Q/N33K/E30D/G31E site directed mutagenesis Staphylococcus aureus
1.20.4.4 K33D site directed mutagenesis Bacillus subtilis
1.20.4.4 K33N site directed mutagenesis Bacillus subtilis
1.20.4.4 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 Staphylococcus aureus
1.20.4.4 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 Bacillus subtilis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.20.4.4 0.009
-
 arsenate wild-type Staphylococcus aureus, condition: 150 mM KCl, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters Staphylococcus aureus
1.20.4.4 0.022
-
 arsenate wild-type Staphylococcus aureus, condition: 150 mM NaCl, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters Staphylococcus aureus
1.20.4.4 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 Bacillus subtilis
1.20.4.4 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 Bacillus subtilis
1.20.4.4 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 Bacillus subtilis
1.20.4.4 0.061
-
 arsenate wild-type Staphylococcus aureus, condition: 50 mM Na2SO4, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters Staphylococcus aureus
1.20.4.4 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 Bacillus subtilis
1.20.4.4 0.08
-
 arsenate H62Q mutant Staphylococcus aureus, condition: 50 mM Na2SO4, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters Staphylococcus aureus
1.20.4.4 0.081
-
 arsenate wild-type Staphylococcus aureus, condition: 50 mM K2SO4, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters Staphylococcus aureus
1.20.4.4 0.087
-
 arsenate H62Q mutant Staphylococcus aureus, condition: 150 mM KCl, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters Staphylococcus aureus
1.20.4.4 0.123
-
 arsenate H62Q mutant Staphylococcus aureus, condition: 150 mM NaCl, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters Staphylococcus aureus
1.20.4.4 0.131
-
 arsenate H62Q mutant Staphylococcus aureus, condition: 50 mM K2SO4, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters Staphylococcus aureus

Organism

EC Number Organism UniProt Comment Textmining
1.20.4.4 Bacillus subtilis P45947
-
-
1.20.4.4 Staphylococcus aureus P0A006
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.20.4.4
-
 Staphylococcus aureus
1.20.4.4
-
 Bacillus subtilis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.20.4.4 arsenate + thioredoxin
-
 Staphylococcus aureus arsenite + thioredoxin disulfide + H2O
-
 ?
1.20.4.4 arsenate + thioredoxin
-
 Bacillus subtilis arsenite + thioredoxin disulfide + H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.20.4.4 Bs_ArsC
-
 Bacillus subtilis
1.20.4.4 Sa_ArsC
-
 Staphylococcus aureus
1.20.4.4 thioredoxin-coupled arsenate reductase detoxification enzyme Staphylococcus aureus
1.20.4.4 thioredoxin-coupled arsenate reductase detoxification enzyme Bacillus subtilis
1.20.4.4 Trx-coupled arsenate reductase
-
 Staphylococcus aureus
1.20.4.4 Trx-coupled arsenate reductase
-
 Bacillus subtilis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.20.4.4 0.58
-
 arsenate wild-type Staphylococcus aureus, condition: 150 mM NaCl, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters Staphylococcus aureus
1.20.4.4 0.7
-
 arsenate H62Q mutant Staphylococcus aureus, condition: 150 mM KCl, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters Staphylococcus aureus
1.20.4.4 0.75
-
 arsenate H62Q mutant Staphylococcus aureus, condition: 150 mM NaCl, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters Staphylococcus aureus
1.20.4.4 0.9
-
 arsenate wild-type Staphylococcus aureus, condition: 150 mM KCl, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters Staphylococcus aureus
1.20.4.4 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 Bacillus subtilis
1.20.4.4 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 Bacillus subtilis
1.20.4.4 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 Bacillus subtilis
1.20.4.4 1.98
-
 arsenate H62Q mutant Staphylococcus aureus, condition: 50 mM Na2SO4, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters Staphylococcus aureus
1.20.4.4 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 Bacillus subtilis
1.20.4.4 2.9
-
 arsenate wild-type Staphylococcus aureus, condition: 50 mM Na2SO4, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters Staphylococcus aureus
1.20.4.4 3.03
-
 arsenate H62Q mutant Staphylococcus aureus, condition: 50 mM K2SO4, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters Staphylococcus aureus
1.20.4.4 3.65
-
 arsenate wild-type Staphylococcus aureus, condition: 50 mM K2SO4, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters Staphylococcus aureus

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.20.4.4 6.1
-
 arsenate H62Q mutant Staphylococcus aureus, condition: 150 mM NaCl, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters Staphylococcus aureus
1.20.4.4 8.1
-
 arsenate H62Q mutant Staphylococcus aureus, condition: 150 mM KCl, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters Staphylococcus aureus
1.20.4.4 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 Bacillus subtilis
1.20.4.4 23.1
-
 arsenate H62Q mutant Staphylococcus aureus, condition: 50 mM K2SO4, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters Staphylococcus aureus
1.20.4.4 24.8
-
 arsenate H62Q mutant Staphylococcus aureus, condition: 50 mM Na2SO4, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters Staphylococcus aureus
1.20.4.4 26.4
-
 arsenate wild-type Staphylococcus aureus, condition: 150 mM NaCl, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters Staphylococcus aureus
1.20.4.4 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 Bacillus subtilis
1.20.4.4 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 Bacillus subtilis
1.20.4.4 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 Bacillus subtilis
1.20.4.4 45.1
-
 arsenate wild-type Staphylococcus aureus, condition: 50 mM K2SO4, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters Staphylococcus aureus
1.20.4.4 47.5
-
 arsenate wild-type Staphylococcus aureus, condition: 50 mM Na2SO4, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters Staphylococcus aureus
1.20.4.4 100
-
 arsenate wild-type Staphylococcus aureus, condition: 150 mM KCl, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters Staphylococcus aureus