1.14.13.155: alpha-pinene monooxygenase
This is an abbreviated version!
For detailed information about alpha-pinene monooxygenase, go to the full flat file.
Reaction
ECTree
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1 | Cofactor |
2 | Expression |
7 | Inhibitors |
3 | Organism |
1 | pH Optimum |
2 | Protein Variants |
1 | Reaction |
3 | Reference |
6 | Substrates and Products (Substrate) |
1 | Subunits |
1 | Systematic Name |
1 | Temperature Optimum [°C] |
Engineering
Engineering on EC 1.14.13.155 - alpha-pinene monooxygenase
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Y96F/V247L
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mutant P450cam, shows altered substrate specificity compared to the wild-type enzyme
additional information
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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