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

BRENDA support

Literature summary extracted from

  • Ji, G.; Garber, E.A.E.; Armes, L.G.; Chen, C.M.; Fuchs, J.A.; Silver, S.
    Arsenate reductase of Staphylococcus aureus plasmid pI258 (1994), Biochemistry, 33, 7294-7299.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.20.4.4 overproduced in Escherichia coli Staphylococcus aureus

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.20.4.4 antimonite SbO2-, pH 7.5, 37°C Staphylococcus aureus
1.20.4.4 arsenite pH 7.5, 37°C Staphylococcus aureus
1.20.4.4 additional information arsenite, tellurite, and antimonite [Sb(III)] are inhibitors for NADPH oxidation; the substrate, arsenate, is not inhibitory at concentrations up to 40 mM Staphylococcus aureus
1.20.4.4 tellurite pH 7.5, 37°C Staphylococcus aureus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.20.4.4 additional information
-
 additional information NADPH oxidation shows Michaelis-Menten kinetics with a Km of 1 microM AsO43- and an apparent Vmax of 200 nmol/min per mg of protein. At high substrate concentration (above 1 mM AsO43-), a secondary rise in the reaction rate is observed, with a Km of 2 mM and an apparent Vmax of 450 nmol/min per mg of protein Staphylococcus aureus
1.20.4.4 additional information
-
 arsenate pH 7.5, 37°C, at low substrate concentrations the Km-value for arsenate is 0.0008 mM. Above 1 mM arsenate, a second increase in rate with increasing substrate is observed, with an apparent Km of 2 mM arsenate Staphylococcus aureus
1.20.4.4 0.0008
-
 arsenate high affinity Staphylococcus aureus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.20.4.4 14436
-
 x * 14436, protein with a loss of the first three amino acid residues from part of the arsenate reductase may have occurred intracellularly or extracellularly during the purification process, mass spectral analysis Staphylococcus aureus
1.20.4.4 14440
-
 calculated from amino acid sequence Staphylococcus aureus
1.20.4.4 14500
-
 electrospray mass spectrometry shows two molecular masses of 14810.5 and 14436.0 Da, suggesting that 70% of the purified protein lacks the N-terminal three amino acids Staphylococcus aureus
1.20.4.4 14810
-
 x * 14810, full length enzyme, mass spectral analysis Staphylococcus aureus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.20.4.4 arsenate + thioredoxin Staphylococcus aureus
-
 arsenite + thioredoxin disulfide + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.20.4.4 Staphylococcus aureus P0A006
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.20.4.4
-
 Staphylococcus aureus
1.20.4.4 gel filtration, SDS-PAGE Staphylococcus aureus

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.20.4.4 0.2
-
 pH 7.5, 37°C Staphylococcus aureus

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 glutaredoxin and reduced glutathione does not stimulate arsenate reduction Staphylococcus aureus arsenite + thioredoxin disulfide + H2O
-
 ?
1.20.4.4 additional information selenate is a poor substrate Staphylococcus aureus ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.20.4.4 ? x * 14436, protein with a loss of the first three amino acid residues from part of the arsenate reductase may have occurred intracellularly or extracellularly during the purification process, mass spectral analysis Staphylococcus aureus
1.20.4.4 ? x * 14810, full length enzyme, mass spectral analysis Staphylococcus aureus
1.20.4.4 monomer
-
 Staphylococcus aureus

Synonyms

EC Number Synonyms Comment Organism
1.20.4.4 ArsC ambiguous Staphylococcus aureus
1.20.4.4 ArsC
-
 Staphylococcus aureus
1.20.4.4 arsenate reductase
-
 Staphylococcus aureus
1.20.4.4 plasmid pI258 arsenate reductase
-
 Staphylococcus aureus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.20.4.4 37
-
 assay at Staphylococcus aureus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.20.4.4 7.5
-
 assay at Staphylococcus aureus

Cofactor

EC Number Cofactor Comment Organism Structure
1.20.4.4 additional information purified enzyme reduces radioactive arsenate to arsenite when coupled to thioredoxin, thioredoxin reductase, and NADPH. All three protein components, arsenate reductase, thioredoxin, and thioredoxin reductase, are required for arsenate reduction. Glutaredoxin and reduced glutathione do not stimulate arsenate reduction Staphylococcus aureus

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.20.4.4 0.0005
-
 tellurite pH 7.5, 37°C Staphylococcus aureus
1.20.4.4 0.01
-
 antimonite pH 7.5, 37°C Staphylococcus aureus
1.20.4.4 0.5
-
 arsenite pH 7.5, 37°C Staphylococcus aureus