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

1 Oxidoreductases

1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen

1.14.13 With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor

1.14.13.155 alpha-pinene monooxygenase

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Results	in table
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

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Engineering on EC 1.14.13.155 - alpha-pinene monooxygenase

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Go to Protein Variants Search

Y96F/V247L

Rhodococcus sp. ECU0066

mutant P450cam, shows altered substrate specificity compared to the wild-type enzyme

745560

additional information

Rhodococcus sp. ECU0066

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

745560