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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

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(-)-alpha-pinene
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NADH
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H+
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O2
=
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alpha-Pinene oxide
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NAD+
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H2O

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
                EC 1.14.13.1551.14.13.155 alpha-pinene monooxygenase

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Resultsin table
1Cofactor
2Expression
7Inhibitors
3Organism
1pH Optimum
2Protein Variants
1Reaction
3Reference
6Substrates and Products (Substrate)
1Subunits
1Systematic Name
1Temperature Optimum [Ā°C]
All data fields related to EC 1.14.13.155

Engineering

Engineering on EC 1.14.13.155 - alpha-pinene monooxygenase

for references in articles please use BRENDA:EC1.14.13.155

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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