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(-)-alpha-pinene + NADH + H+ + O2 = alpha-pinene oxide + NAD+ + H2O
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(-)-alpha-pinene,NADH:oxygen oxidoreductase
Involved in the catabolism of alpha-pinene.
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(-)-alpha-pinene + NADH + H+ + O2
alpha-pinene oxide + NAD+ + H2O
(-)-limonene + NADH + H+ + O2
(1S,6R)-isopiperitenol + (4R,6S)-carveol + (R)-1,2-epoxy-limonene
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Substrates: substrate of enzyme mutant chimeric P450cam (Y96F/V247L)-P450SMO red F1-F4
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camphor + NADH + H+ + O2
5-exo-hydroxycamphor + NAD+ + H2O
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Substrates: substrate of enzyme mutant P450Cam (Y96F/V247L) and enzyme mutant chimeric P450cam (Y96F/V247L)-P450SMO red F1-F4
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additional information
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Substrates: usage of artificial substrates by chimeric P450 mutants, the wild-type P450SMO reductase shows no activity with substrates camphor, (-)-alpha-pinene, and (-)-limonene
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(-)-alpha-pinene + NADH + H+ + O2
alpha-pinene oxide + NAD+ + H2O
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Substrates: -
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(-)-alpha-pinene + NADH + H+ + O2
alpha-pinene oxide + NAD+ + H2O
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Substrates: -
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(-)-alpha-pinene + NADH + H+ + O2
alpha-pinene oxide + NAD+ + H2O
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Substrates: substrate enzyme mutant chimeric P450cam (Y96F/V247L)-P450SMO red F1-F4
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(1R,4S,6S)-1-methyl-4-(prop-1-en-2-yl)-7-oxabicyclo[4.1.0]heptane
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(1S,5R)-2-methyl-5-(prop-1-en-2-yl)cyclohex-2-en-1-ol
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(1S,6R)-3-methyl-6-(prop-1-en-2-yl)cyclohex-2-en-1-ol
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1,7,7-trimethylbicyclo[2.2.1]heptane-2,5-dione
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4,6,6-trimethylbicyclo[3.1.1]hept-3-en-2-ol
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4,6,6-trimethylbicyclo[3.1.1]hept-3-en-2-one
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5-hydroxy-1,7,7-trimethylbicyclo[2.2.1]heptan-2-one
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Highest Expressing Human Cell Lines
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additional information
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the cytochrome P450 enzyme consists of a heme domain, a flavin-reductase domain containing FMN and NADPH binding sites, and a[Fe2S2] ferredoxin domain
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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
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alpha-pinene monooxygenase is expressed at a low constitutive level and induced in presence of alpha-pinene
alpha-pinene monooxygenase is expressed at a low constitutive level and induced in presence of alpha-pinene
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alpha-pinene monooxygenase is expressed at a low constitutive level and induced in presence of alpha-pinene
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Colocousi, A.; Saqib, K.M.; Leak, D.J.
Mutants of Pseudomonas fluorescens NCIMB 11671 defective in the catabolism of alpha-pinene
Appl. Microbiol. Biotechnol.
45
822-830
1996
Pseudomonas fluorescens, Pseudomonas fluorescens NCIMB 11671
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Luan, Z.; Yin, Y.; Li, A.; Yu, H.; Xu, J.
Monoterpene hydroxylation with an artificial self-sufficient P450 utilizing a P450SMO reductase domain for the electron transfer
J. Mol. Catal. B
116
78-82
2015
Rhodococcus sp. ECU0066
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