EC Number | Application | Comment | Organism |
---|---|---|---|
1.14.14.1 | biotechnology | enzymatic activity of P450SMO makes it an attractive biocatalyst for asymmetric synthesis of enantiopure sulfoxides | Rhodococcus sp. |
EC Number | Cloned (Comment) | Organism |
---|---|---|
1.14.14.1 | into the pET28a (+) vector and expressed in Escherichia coli BL21 (DE3) | Rhodococcus sp. |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.14.14.1 | imidazole | at 20 mM, only half of P450SMO activity remains | Rhodococcus sp. |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.14.14.1 | Fe2+ | the C-terminal reductase portion of P450SMO comprises a [2Fe2S] ferredoxin center | Rhodococcus sp. |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
1.14.14.1 | 87190 | - |
sequence analysis | Rhodococcus sp. |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.14.14.1 | Rhodococcus sp. | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.14.14.1 | gel filtration | Rhodococcus sp. |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.14.1 | 7-ethoxycoumarin + NADPH + H+ + O2 | mediates the O-dealkylation | Rhodococcus sp. | 7-hydroxycoumarin + NADP+ + H2O + ? | - |
? | |
1.14.14.1 | additional information | no hydroxylation activity towards naphthalene, indene, ethyl benzene, and m-xylene | Rhodococcus sp. | ? | - |
? | |
1.14.14.1 | p-chlorothioanisole + [reduced NADPH-hemoprotein reductase] + O2 | - |
Rhodococcus sp. | ? | - |
? | |
1.14.14.1 | p-fluorothioanisole + [reduced NADPH-hemoprotein reductase] + O2 | - |
Rhodococcus sp. | ? | - |
? | |
1.14.14.1 | p-methoxythioanisole + [reduced NADPH-hemoprotein reductase] + O2 | - |
Rhodococcus sp. | ? | - |
? | |
1.14.14.1 | p-tolyl methyl sulfide + [reduced NADPH-hemoprotein reductase] + O2 | - |
Rhodococcus sp. | ? | - |
? | |
1.14.14.1 | phenyl ethyl sulfide + [reduced NADPH-hemoprotein reductase] + O2 | - |
Rhodococcus sp. | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.14.14.1 | cytochrome P450 monooxygenase | - |
Rhodococcus sp. |
1.14.14.1 | P450SMO | - |
Rhodococcus sp. |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.14.14.1 | 30 | - |
toward p-chlorothioanisole | Rhodococcus sp. |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.14.14.1 | 7 | - |
toward p-chlorothioanisole | Rhodococcus sp. |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.14.14.1 | FMN | the C-terminal reductase portion of P450SMO comprises an FMN-binding | Rhodococcus sp. | |
1.14.14.1 | NADH | the C-terminal reductase portion of P450SMO comprises an NADH-binding | Rhodococcus sp. | |
1.14.14.1 | NADPH | - |
Rhodococcus sp. |
EC Number | Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|---|
1.14.14.1 | Rhodococcus sp. | - |
- |
5.17 |