Activating Compound | Comment | Organism | Structure |
---|---|---|---|
GSH | required | Escherichia coli |
Protein Variants | Comment | Organism |
---|---|---|
A11W | same Km for arsenate as the wild type with maximal velocity approximately half that of the wild type enzyme | Escherichia coli |
A11W/C12S | catalytic inactive mutation | Escherichia coli |
Y7W | same Km and maximal velocity as the wild type | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
arsenate + reduced glutaredoxin | Escherichia coli | the enzyme is involved in bacterial arsenic resistance | arsenite + oxidized glutaredoxin | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
arsenate + reduced glutaredoxin | the first step of the reaction is the binding of arsenate, followed by the interaction of the enzyme-arsenate complex with GSH. A reaction scheme is hypothesized in which the enzyme forms a mixed disulfide between the Cys-12 thiolate of ArsC and GSH. Glutaredoxin would then be required to resolve the mixed disulfide, regenerating reduced ArsC | Escherichia coli | arsenite + oxidized glutaredoxin | - |
? | |
arsenate + reduced glutaredoxin | the enzyme is involved in bacterial arsenic resistance | Escherichia coli | arsenite + oxidized glutaredoxin | - |
? |