Cloned (Comment) | Organism |
---|---|
wild-type enzyme and F-G loop deletion mutant enzyme delLL151-E156, overexpression in Escherichia coli | Sulfurisphaera tokodaii |
Crystallization (Comment) | Organism |
---|---|
vapour diffusion method, X-ray crystallography at a resolution of 1.94 A reveals a sufficiently large heme pocket for NAD(P)H binding and a novel contiguous channel from the active site to bulk solvent in the distal heme pocket. The mutant shows a higher affinity for NADH compared with the wild-type because the mutant has a more widely open distal pocket for NAD(P)H binding | Sulfurisphaera tokodaii |
Protein Variants | Comment | Organism |
---|---|---|
delL151-E156 | the Km value of the mutant is about 2times lower than that of the wild-type. | Sulfurisphaera tokodaii |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.29 | - |
Styrene | pH 7, 25°C, wild-type enzyme | Sulfurisphaera tokodaii | |
0.52 | - |
Styrene | pH 7, 25°C, mutant enzyme delLL151-E156 | Sulfurisphaera tokodaii | |
7 | - |
NADH | pH 7, 25°C, mutant enzyme delLL151-E156 | Sulfurisphaera tokodaii | |
13 | - |
NADH | pH 7, 25°C, wild-type enzyme | Sulfurisphaera tokodaii |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
43000 | - |
F-G loop deletion mutant enzyme delLL151-E156 | Sulfurisphaera tokodaii |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Sulfurisphaera tokodaii | Q972I2 | - |
- |
Sulfurisphaera tokodaii 7 | Q972I2 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Sulfurisphaera tokodaii |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
styrene + NADH + H+ + O2 = styrene epoxide + NAD+ + H2O | sequential mechanism. Both styrene and NADH bind to the enzyme before any product is released | Sulfurisphaera tokodaii |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
styrene + NADH + H+ + O2 | the initial rate of catalysis with NADH is slightly higher than with NADPH | Sulfurisphaera tokodaii | styrene epoxide + NAD+ + H2O | - |
? | |
styrene + NADH + H+ + O2 | the initial rate of catalysis with NADH is slightly higher than with NADPH | Sulfurisphaera tokodaii 7 | styrene epoxide + NAD+ + H2O | - |
? | |
styrene + NADPH + H+ + O2 | the initial rate of catalysis with NADH is slightly higher than with NADPH | Sulfurisphaera tokodaii | styrene epoxide + NADP+ + H2O | - |
? | |
styrene + NADPH + H+ + O2 | the initial rate of catalysis with NADH is slightly higher than with NADPH | Sulfurisphaera tokodaii 7 | styrene epoxide + NADP+ + H2O | - |
? |
Synonyms | Comment | Organism |
---|---|---|
P450st | - |
Sulfurisphaera tokodaii |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Sulfurisphaera tokodaii |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.000057 | - |
Styrene | pH 7, 25°C, mutant enzyme delLL151-E156 | Sulfurisphaera tokodaii | |
0.000061 | - |
Styrene | pH 7, 25°C, wild-type enzyme | Sulfurisphaera tokodaii | |
0.000076 | - |
NADH | pH 7, 25°C, wild-type enzyme | Sulfurisphaera tokodaii | |
0.000079 | - |
NADH | pH 7, 25°C, mutant enzyme delLL151-E156 | Sulfurisphaera tokodaii |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
assay at | Sulfurisphaera tokodaii |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADH | the initial rate of catalysis with NADH is slightly higher than with NADPH | Sulfurisphaera tokodaii | |
NADPH | the initial rate of catalysis with NADH is slightly higher than with NADPH | Sulfurisphaera tokodaii |