Cloned (Comment) | Organism |
---|---|
high level and functional expression of P450SMO in Escherichia coli strain BL21, method optimization and evaluation, overview | Rhodococcus sp. |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | heme protein | Rhodococcus sp. |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rhodococcus sp. | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
4-chlorothioanisole + [reduced NADPH-hemoprotein reductase] + O2 | enantioselectivity for the biosulfoxidation catalyzed by the recombinant enzyme expressed from an improved engineered Escherichia coli strain | Rhodococcus sp. | 4-chlorothioanisole sulfoxide + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
4-fluorothioanisole + [reduced NADPH-hemoprotein reductase] + O2 | enantioselectivity for the biosulfoxidation catalyzed by the recombinant enzyme expressed from an improved engineered Escherichia coli strain | Rhodococcus sp. | 4-fluorothioanisole sulfoxide + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
4-methoxythioanisole + [reduced NADPH-hemoprotein reductase] + O2 | enantioselectivity for the biosulfoxidation catalyzed by the recombinant enzyme expressed from an improved engineered Escherichia coli strain | Rhodococcus sp. | 4-methoxythioanisole sulfoxide + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
4-tolylmethylsulfide + [reduced NADPH-hemoprotein reductase] + O2 | enantioselectivity for the biosulfoxidation catalyzed by the recombinant enzyme expressed from an improved engineered Escherichia coli strain | Rhodococcus sp. | 4-tolylmethylsulfoxide + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
ethyl methyl sulfide + [reduced NADPH-hemoprotein reductase] + O2 | enantioselectivity for the biosulfoxidation catalyzed by the recombinant enzyme expressed from an improved engineered Escherichia coli strain | Rhodococcus sp. | ethyl methyl sulfoxide + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
phenyl methyl sulfide + [reduced NADPH-hemoprotein reductase] + O2 | enantioselectivity for the biosulfoxidation catalyzed by the recombinant enzyme expressed from an improved engineered Escherichia coli strain | Rhodococcus sp. | phenyl methyl sulfoxide + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? |
Synonyms | Comment | Organism |
---|---|---|
cytochrome P450 monooxygenase | - |
Rhodococcus sp. |
More | P450SMO belongs to class IV of P450 monooxygenase | Rhodococcus sp. |
P450SMO | - |
Rhodococcus sp. |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
whole cell assay | Rhodococcus sp. |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
20 | 50 | recombinant Escherichia coli cell expressing the enzyme, at higher temperatures over 30°C, the activity decreases significantly, temperature profile, overview | Rhodococcus sp. |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
whole cell assay | Rhodococcus sp. |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
5.5 | 8.5 | recombinant Escherichia coli cell expressing the enzyme, below 7.0 or over 8.0 the enzyme activity decreases drastically, pH profile, overview | Rhodococcus sp. |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
heme | - |
Rhodococcus sp. | |
NADPH | - |
Rhodococcus sp. |