Information on EC 1.14.13.155 - alpha-pinene monooxygenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.13.155
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RECOMMENDED NAME
GeneOntology No.
alpha-pinene monooxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(-)-alpha-pinene + NADH + H+ + O2 = alpha-pinene oxide + NAD+ + H2O
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
(-)-alpha-pinene,NADH:oxygen oxidoreductase
Involved in the catabolism of alpha-pinene.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(-)-alpha-pinene + NADH + H+ + O2
alpha-pinene oxide + NAD+ + H2O
show the reaction diagram
(?)-limonene + NADH + H+ + O2
(S)-3-hydroxy-limonene + (S)-6-hydroxy-limonene + (R)-1,2-epoxy-limonene
show the reaction diagram
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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
show the reaction diagram
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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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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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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome P450
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(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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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 30
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assay at
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
alpha-pinene monooxygenase is expressed at a low constitutive level and induced in presence of alpha-pinene
ENGINEERING
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