EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.14.15.1 | Y75F | the mutant shows an altered active site structure influencing catalysis | Pseudomonas putida |
1.14.15.1 | Y96F | the mutant shows an altered active site structure influencing catalysis | Pseudomonas putida |
1.14.15.1 | Y96F/Y75F | the mutant shows an altered active site structure influencing catalysis | Pseudomonas putida |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.14.15.1 | additional information | - |
additional information | stopped-flow kinetic analysis of the peracid oxidation of the wild-type enzyme and substrate-free ferric mutant enzymes overview | Pseudomonas putida |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.14.15.1 | Pseudomonas putida | P00183 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.15.1 | 3-chloroperbenzoic acid + O2 + reduced putidaredoxin | compound I, ferryl iron plus a porphyrin pi-cation radical (Fe(IV)=O/Por(+)), and compound ES, Fe(IV)=O/Tyr(), in reactions of substrate-free ferric enzyme with 3-chloroperbenzoic acid, compound ES arises by intramolecular electron transfer from nearby tyrosines to the porphyrin pi-cation radical of compound I, active site changes influence electron transfer from nearby tyrosines and affect formation of intermediates, the tyrosyl radical is assigned to Tyr96 for wild type or to Tyr75 for the Y96F variant, overview | Pseudomonas putida | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.14.15.1 | cytochrome p450cam | - |
Pseudomonas putida |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.14.15.1 | putidaredoxin | - |
Pseudomonas putida |