EC Number | Cloned (Comment) | Organism |
---|---|---|
1.11.1.5 | expression in Escherichia coli | Nitrosomonas europaea |
1.11.1.5 | expression in Escherichia coli | Shewanella oneidensis |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.11.1.5 | E123D | distal heme pocket mutant, no detectable electrocatalytic turnover of substrate in the highpotential regime | Shewanella oneidensis |
1.11.1.5 | E123Q | distal heme pocket mutant, no detectable electrocatalytic turnover of substrate in the highpotential regime | Shewanella oneidensis |
1.11.1.5 | F102W | distal heme pocket mutant, 10fold decrease in peroxidase activity and high-potential catalytic turnover of hydrogen peroxide | Shewanella oneidensis |
1.11.1.5 | F81W | modest changes in in vitro peroxidase assays | Nitrosomonas europaea |
1.11.1.5 | H81G | mutant is highly active | Shewanella oneidensis |
1.11.1.5 | Q113N | distal heme pocket mutant, no detectable electrocatalytic turnover of substrate in the highpotential regime | Shewanella oneidensis |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.11.1.5 | L-ascorbate | poising the enzyme in the active state using sodium L-ascorbate, allows for capturing a highly active state that turns over peroxide in a high potential regime | Nitrosomonas europaea | |
1.11.1.5 | L-ascorbate | poising the enzyme in the active state using sodium L-ascorbate, allows for capturing a highly active state that turns over peroxide in a high potential regime | Shewanella oneidensis |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.11.1.5 | 0.00013 | - |
H2O2 | mutant F102W, pH 6.0, 23°C | Nitrosomonas europaea | |
1.11.1.5 | 0.0004 | - |
H2O2 | mutant F81W, pH 6.0, 23°C | Nitrosomonas europaea | |
1.11.1.5 | 0.004 | - |
H2O2 | mutant F102W, pH 6.0, 23°C | Shewanella oneidensis |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.11.1.5 | Nitrosomonas europaea | - |
- |
- |
1.11.1.5 | Shewanella oneidensis | Q8EF24 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.11.1.5 | 2 ferrocytochrome c + H2O2 | - |
Nitrosomonas europaea | 2 ferricytochrome c + 2 H2O | - |
? | |
1.11.1.5 | 2 ferrocytochrome c + H2O2 | - |
Shewanella oneidensis | 2 ferricytochrome c + 2 H2O | - |
? | |
1.11.1.5 | additional information | the rate-limiting step involves a proton-coupled single electron reduction of a high valent iron species centered on the low-potential heme. Reduction shifts the pKa's of at least two amino acids. Loop 1 shifts during the rate-limiting step, changing the environment of residue His81 | Shewanella oneidensis | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.11.1.5 | diheme cytochrome c5 peroxidase CcpA | - |
Nitrosomonas europaea |
1.11.1.5 | diheme cytochrome c5 peroxidase CcpA | - |
Shewanella oneidensis |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.11.1.5 | 1.7 | - |
H2O2 | mutant F81W, pH 6.0, 23°C | Nitrosomonas europaea | |
1.11.1.5 | 4.3 | - |
H2O2 | wild-type, pH 6.0, 23°C | Nitrosomonas europaea | |
1.11.1.5 | 5.5 | - |
H2O2 | mutant F102W, pH 6.0, 23°C | Shewanella oneidensis |