Protein Variants | Comment | Organism |
---|---|---|
additional information | construction of an artificial self-sufficient P450-type monoterpene hydroxylase by fusing the wild-type P450SMO reductase domain and the P450cam(Y96F/V247L) domain to a linker region (G4S)4. The resultant chimeric P450 enzyme, chimeric P450cam (Y96F/V247L)-P450SMO red F1-F4, catalyzes the hydroxylation of (-)-limonene and (-)-alpha-pinene as well as camphor, which are all inactive for the wild-type enzyme P450SMO | Rhodococcus sp. ECU0066 |
Y96F/V247L | mutant P450cam, shows altered substrate specificity compared to the wild-type enzyme | Rhodococcus sp. ECU0066 |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
(1R,4S,6S)-1-methyl-4-(prop-1-en-2-yl)-7-oxabicyclo[4.1.0]heptane | - |
Rhodococcus sp. ECU0066 | |
(1S,5R)-2-methyl-5-(prop-1-en-2-yl)cyclohex-2-en-1-ol | - |
Rhodococcus sp. ECU0066 | |
(1S,6R)-3-methyl-6-(prop-1-en-2-yl)cyclohex-2-en-1-ol | - |
Rhodococcus sp. ECU0066 | |
1,7,7-trimethylbicyclo[2.2.1]heptane-2,5-dione | - |
Rhodococcus sp. ECU0066 | |
4,6,6-trimethylbicyclo[3.1.1]hept-3-en-2-ol | - |
Rhodococcus sp. ECU0066 | |
4,6,6-trimethylbicyclo[3.1.1]hept-3-en-2-one | - |
Rhodococcus sp. ECU0066 | |
5-hydroxy-1,7,7-trimethylbicyclo[2.2.1]heptan-2-one | - |
Rhodococcus sp. ECU0066 |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rhodococcus sp. ECU0066 | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(-)-alpha-pinene + NADH + H+ + O2 | substrate enzyme mutant chimeric P450cam (Y96F/V247L)-P450SMO red F1-F4 | Rhodococcus sp. ECU0066 | alpha-pinene oxide + NAD+ + H2O | - |
? | |
(-)-limonene + NADH + H+ + O2 | substrate of enzyme mutant chimeric P450cam (Y96F/V247L)-P450SMO red F1-F4 | Rhodococcus sp. ECU0066 | (1S,6R)-isopiperitenol + (4R,6S)-carveol + (R)-1,2-epoxy-limonene | - |
? | |
camphor + NADH + H+ + O2 | substrate of enzyme mutant P450Cam (Y96F/V247L) and enzyme mutant chimeric P450cam (Y96F/V247L)-P450SMO red F1-F4 | Rhodococcus sp. ECU0066 | 5-exo-hydroxycamphor + NAD+ + H2O | - |
? | |
additional information | usage of artificial substrates by chimeric P450 mutants, the wild-type P450SMO reductase shows no activity with substrates camphor, (-)-alpha-pinene, and (-)-limonene | Rhodococcus sp. ECU0066 | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | the cytochrome P450 enzyme consists of a heme domain, a flavin-reductase domain containing FMN and NADPH binding sites, and a[Fe2S2] ferredoxin domain | Rhodococcus sp. ECU0066 |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | 30 | assay at | Rhodococcus sp. ECU0066 |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Rhodococcus sp. ECU0066 |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
cytochrome P450 | - |
Rhodococcus sp. ECU0066 |