EC Number | Cloned (Comment) | Organism |
---|---|---|
1.14.14.1 | expression in Escherichia coli | Priestia megaterium |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.14.14.1 | 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 |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.14.14.1 | additional information | - |
additional information | Km-values of wild-type and mutant enzyme for different fatty acids and alkyl trimethylammonium compounds | Priestia megaterium |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.14.14.1 | Priestia megaterium | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.14.1 | 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 | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.14.14.1 | CYP102 | - |
Priestia megaterium |
1.14.14.1 | 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 |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.14.14.1 | additional information | - |
additional information | Kcat-values of wild-type and mutant enzyme for different fatty acids and alkyl trimethylammonium compounds | Priestia megaterium |