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

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


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
perillyl aldehyde biosynthesis
-
-
Monoterpenoid biosynthesis
-
-
Limonene and pinene degradation
-
-
Biosynthesis of secondary metabolites
-
-
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
-
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
-
plus FMN, 0.005 mM each, activation
FMN
-
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
-
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
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
-
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
-
expression in n-octane grown Pseudomonas putida
-
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