EC Number | Cloned (Comment) | Organism |
---|---|---|
1.11.2.4 | expressed in Escherichia coli | Priestia megaterium |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.11.2.4 | F878A | P450 BM-3 heme domain containing the single amino acid substitution F87A is significantly more active than wild type heme domain in reactions driven by H2O2 | Priestia megaterium |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.11.2.4 | additional information | Priestia megaterium | P450 BM-3 peroxygenase 21B3 is a laboratory-evolved variant of the P450 BM-3 heme domain which functions as an H2O2-driven hydroxylase (peroxygenase) and does not require NADPH, O2 , or the reductase | ? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.11.2.4 | Priestia megaterium | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.11.2.4 | - |
Priestia megaterium |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.11.2.4 | 12-4-nitrophenoxycarboxylic acid + H2O2 | - |
Priestia megaterium | 4-nitrophenolate + ? | - |
? | |
1.11.2.4 | additional information | P450 BM-3 peroxygenase 21B3 is a laboratory-evolved variant of the P450 BM-3 heme domain which functions as an H2O2-driven hydroxylase (peroxygenase) and does not require NADPH, O2 , or the reductase | Priestia megaterium | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.11.2.4 | P450 BM-3 peroxygenase 21B3 | - |
Priestia megaterium |