Cloned (Comment) | Organism |
---|---|
expression of wild-type and mutant enzymes | Rhodococcus rhodochrous |
Protein Variants | Comment | Organism |
---|---|---|
additional information | quasi random mutation of the large subunit of the epoxygenase component, AmoC alters the enantioselectivity of the enzyme, screening for altered epoxidation abilities | Rhodococcus rhodochrous |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Iron | the enzyme possesses a dinuclear iron center within the large subunit of the epoxygenase component, AmoC, mutagenesis of AmoC alters the enantioselectivity of the enzyme | Rhodococcus rhodochrous |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rhodococcus rhodochrous | - |
- |
- |
Rhodococcus rhodochrous B-276 | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | the enzyme is a three-component system encoded by the 4-gene operon amoABCD, which catalyzes the stereoselective epoxidation of aliphatic alkenes yielding primarily the R enantiomer | Rhodococcus rhodochrous | ? | - |
? | |
additional information | the enzyme is a three-component system encoded by the 4-gene operon amoABCD, which catalyzes the stereoselective epoxidation of aliphatic alkenes yielding primarily the R enantiomer | Rhodococcus rhodochrous B-276 | ? | - |
? | |
propene + NADH + H+ + O2 | - |
Rhodococcus rhodochrous | 1,2-epoxypropane + NAD+ + H2O | - |
? | |
propene + NADH + H+ + O2 | - |
Rhodococcus rhodochrous B-276 | 1,2-epoxypropane + NAD+ + H2O | - |
? |
Synonyms | Comment | Organism |
---|---|---|
AMO | - |
Rhodococcus rhodochrous |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Rhodococcus rhodochrous |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADH | - |
Rhodococcus rhodochrous |