Any feedback?
Literature summary for 1.20.4.4 extracted from
- Arsenate reductase of Staphylococcus aureus plasmid pI258 (1994), Biochemistry, 33, 7294-7299.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| overproduced in Escherichia coli | Staphylococcus aureus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| antimonite | SbO2-, pH 7.5, 37°C | Staphylococcus aureus |  |
| arsenite | pH 7.5, 37°C | Staphylococcus aureus | |
| 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 | |
| tellurite | pH 7.5, 37°C | Staphylococcus aureus | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 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 | |
| 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 | |
| 0.0008 | - |
arsenate | high affinity | Staphylococcus aureus | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 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 |
| 14440 | - |
calculated from amino acid sequence | Staphylococcus aureus |
| 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 |
| 14810 | - |
x * 14810, full length enzyme, mass spectral analysis | Staphylococcus aureus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| arsenate + thioredoxin | Staphylococcus aureus | - |
arsenite + thioredoxin disulfide + H2O | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Staphylococcus aureus | P0A006 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Staphylococcus aureus |
| gel filtration, SDS-PAGE | Staphylococcus aureus |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 0.2 | - |
pH 7.5, 37°C | Staphylococcus aureus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| arsenate + thioredoxin | - |
Staphylococcus aureus | arsenite + thioredoxin disulfide + H2O | - |
? | |
| arsenate + thioredoxin | glutaredoxin and reduced glutathione does not stimulate arsenate reduction | Staphylococcus aureus | arsenite + thioredoxin disulfide + H2O | - |
? | |
| additional information | selenate is a poor substrate | Staphylococcus aureus | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | 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 |
| ? | x * 14810, full length enzyme, mass spectral analysis | Staphylococcus aureus |
| monomer | - |
Staphylococcus aureus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ArsC | ambiguous | Staphylococcus aureus |
| ArsC | - |
Staphylococcus aureus |
| arsenate reductase | - |
Staphylococcus aureus |
| plasmid pI258 arsenate reductase | - |
Staphylococcus aureus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Staphylococcus aureus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Staphylococcus aureus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| 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]
| Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.0005 | - |
tellurite | pH 7.5, 37°C | Staphylococcus aureus | |
| 0.01 | - |
antimonite | pH 7.5, 37°C | Staphylococcus aureus | |
| 0.5 | - |
arsenite | pH 7.5, 37°C | Staphylococcus aureus | |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
