Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Priestia megaterium |
Protein Variants | Comment | Organism |
---|---|---|
R47E | the mutant enzyme retains significant hydroxylase activity towards saturated fatty acids and shows much increased activity towards C12-C16 alkyl trimethylammonium compounds | Priestia megaterium |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | Km-values of wild-type and mutant enzyme for different fatty acids and alkyl trimethylammonium compounds | Priestia megaterium |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Priestia megaterium | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | enzyme catalyses hydroxylation in the omega-1, omega-2 and omega-3 positions and/or epoxidation of medium- and long-chain fatty acids | Priestia megaterium | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
CYP102 | - |
Priestia megaterium |
cytochrome P-450 BM3 | enzyme contains a P-450 heme domain and an NADPH-cytochrome P-450 reductase flavoprotein domain in a single polypeptide chain | Priestia megaterium |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | Kcat-values of wild-type and mutant enzyme for different fatty acids and alkyl trimethylammonium compounds | Priestia megaterium |