Cloned (Comment) | Organism |
---|---|
expression of Thr171Ser mutant enzyme in Escherichia coli | Armoracia rusticana |
Protein Variants | Comment | Organism |
---|---|---|
T171S | loss of a structural restraint in the proximal heme pocket that allows slippage of the proximal heme ligand, but only in the reduced state. This is a remarkably subtle and specific effect that appears to increase the flexibility of the reduced state of the mutant compared to that of the wild-type protein. Significant change in the Fe2+/Fe3+ redox potential of the mutant T171S | Armoracia rusticana |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
607 | - |
reduced 2,2'-azino-bis-(3-ethylbenzthiazole-6-sulfonic acid) | 25°C, pH 5.0, mutant enzyme | Armoracia rusticana |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Armoracia rusticana | P00433 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
reduced 2,2'-azino-bis-(3-ethylbenzthiazole-6-sulfonic acid) + H2O2 | - |
Armoracia rusticana | oxidized 2,2'-azino-bis-(3-ethylbenzthiazole-6-sulfonic acid) + H2O | - |
? |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
heme | loss of a structural restraint in the proximal heme pocket of mutant enzyme T171S allows slippage of the proximal heme ligand, but only in the reduced state. This is a remarkably subtle and specific effect that appears to increase the flexibility of the reduced state of the mutant compared to that of the wild-type protein | Armoracia rusticana |