Information on EC 1.14.13.49 - (S)-limonene 7-monooxygenase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
1.14.13.49
-
RECOMMENDED NAME
GeneOntology No.
(S)-limonene 7-monooxygenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(S)-limonene + NADPH + H+ + O2 = (-)-perillyl alcohol + NADP+ + H2O
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
-
Limonene and pinene degradation
-
-
Monoterpenoid biosynthesis
-
-
perillyl aldehyde biosynthesis
-
-
SYSTEMATIC NAME
IUBMB Comments
(S)-limonene,NADPH:oxygen oxidoreductase (7-hydroxylating)
High specificity, but NADH can act instead of NADPH, although more slowly. A heme-thiolate protein (P-450).
CAS REGISTRY NUMBER
COMMENTARY hide
122653-75-2
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
HXN-1500
-
-
Manually annotated by BRENDA team
HXN-1500
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(+)-limonene + NADPH + O2
perillyl alcohol + NADP+ + H2O
show the reaction diagram
-
hydroxylation at the same rate as (-)-limonene
-
?
(-)-(S)-limonene + NADPH + O2
(-)-perillyl alcohol + NADP+ + H2O
show the reaction diagram
(-)-limonene + NADPH + O2
perillyl alcohol + NADP+ + H2O
show the reaction diagram
(S)-limonene + NADPH + H+ + O2
(-)-perillyl alcohol + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(-)-(S)-limonene + NADPH + O2
(-)-perillyl alcohol + NADP+ + H2O
show the reaction diagram
(-)-limonene + NADPH + O2
perillyl alcohol + NADP+ + H2O
show the reaction diagram
-
one of the key reactions of oxygenated monoterpenes, perillyl aldehyde biosynthesis
-
-
?
(S)-limonene + NADPH + H+ + O2
(-)-perillyl alcohol + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome P450
-
heme-thiolate protein, 0.2-0.9 nmol per mg protein
-
NADH
-
5.3% as effective as NADPH
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5,11-Dimethyl-6H-pyrido[4,3-b]carbazole
-
-
clotrimazole
-
i.e. 1-[chloro-alpha,alpha-diphenyl]imidazole, mixed-type, weak
CO
-
CO:O2 ratio of 9:1, photoreversible
cytochrome c
-
strong
Metyrapone
-
i.e. 2-methyl-1,2-di-3-pyridyl-1-propanone, moderate
miconazole
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i.e. 1-[2,4-dichloro-beta-([2,4-di-chlorobenzyl]oxy)phenethyl]-imidazole, mixed-type, weak
NADP+
-
2 mM
SKF 525A
-
i.e. 2-diethyl-aminoethyl-2,2-diphenylvalerate, moderate
additional information
-
no inhibition: ancymidol, imidazole, up to 5 mM
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
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plus FMN, 0.005 mM each, activation
FMN
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plus FAD, 0.005 mM each, activation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.021
(-)-limonene
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0001567
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.6
-
recombinant chimeric mutant enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 8
-
almost no activity at pH 5.5 and pH 8.0, respectively
6.75 - 8.5
-
half-maximal activity at pH 6.75 and 8.5, recombinant chimeric mutant enzyme
7.3 - 8.3
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about half-maximal activity at pH 7.3 and 8.3
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
oil glands on abaxial surface
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
48000
-
x * 48000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0
-
50% loss of activity after 6 h
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate, phenyl Sepharose, Source Q15
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, expression in Escherichia coli as a chimeric protein fused with the N-terminal membrane insertion domain of the limonene-3-hydroxylase
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expression in n-octane grown Pseudomonas putida
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
construction of a chimeric mutant enzyme by fusion of the N-terminal membrane insertion domain of the limonene-3-hydroxylase into limonene 7-hydroxylase. The kinetically competent recombinant protein produces a mixture of C3-, C6- and C7-hydroxylated limonene derivatives with a distribution of 33%, 14% and 53%, respectively