Information on EC 1.14.13.202 - methyl farnesoate epoxidase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.13.202
-
RECOMMENDED NAME
GeneOntology No.
methyl farnesoate epoxidase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
methyl (2E,6E)-farnesoate + NADPH + H+ + O2 = juvenile hormone III + NADP+ + H2O
show the reaction diagram
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Insect hormone biosynthesis
-
-
juvenile hormone III biosynthesis I
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-
SYSTEMATIC NAME
IUBMB Comments
methyl (2E,6E)-farnesoate,NADPH:oxygen oxidoreductase
A heme-thiolate protein (cytochrome P-450). The enzyme, found in insects except for Lepidoptera (moths and butterflies) is specific for methyl farnesoate (cf. EC 1.14.13.203, farnesoate epoxidase) [1,2].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
Uniprot
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
RNAi-mediated knockdown of CYP15A1 in the pre-final larval instar does not result in precocious metamorphosis to pupa. The double knockdown of juvenile hormone acid O-methyltransferase and TcCYP15A1 results in pupae and adults with shorter wings
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2E,6E)-farnesoate + NADPH + H+ + O2
? + NADP+ + H2O
show the reaction diagram
-
-
-
?
methyl (2E,6E)-farnesoate + NADPH + H+ + O2
?
show the reaction diagram
-
epoxidation is 12% compared to epoxidation of methyl (2E,6E)-farnesoate
-
-
?
methyl (2E,6E)-farnesoate + NADPH + H+ + O2
juvenile hormone III + NADP+ + H2O
show the reaction diagram
additional information
?
-
-
no activity with farnesol, farnesal, farnesoic acid, juvenile hormone III, 3,7,11-trimethyl-dodecanol, geranyl geraniol, farnesyl methyl ether, and geraniol and the fatty acids, lauric acid, and arachidonic acid
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-
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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
methyl (2E,6E)-farnesoate + NADPH + H+ + O2
juvenile hormone III + NADP+ + H2O
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome P-450
-
a heme-thiolate protein
-
NADH
-
NADH supports less than 10% of the NADPH rate of epoxidation
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-(2-methylpropyl)-5-[4-([4-[3-(trifluoromethyl)-3H-diaziren-3-yl]benzyl]oxy)phenyl]-1H-imidazole
-
bifunctional compound, inhibits juvenile hormone III synthesis by intact glands as well as methyl farnesoate epoxidation by gland homogenates. Using the compound, a radiolabeled and photoactivatable diazirine or benzophenone group can be introduced to label the hydrophobic substrate binding site of the enzyme
5-(2-(benzyloxy)phenyl)-1-(3,7-dimethyloct-6-en-1-yl)-1H-imidazole
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-
5-(3-[[(2E)-3,7-dimethylocta-2,6-dien-1-yl]oxy]phenyl)-1-(2-methylpropyl)-1H-imidazole
-
-
5-[3-(benzyloxy)phenyl]-1-(2-methylpropyl)-1H-imidazole
-
-
carbon monoxide/oxygen atmosphere
-
half-maximal inhibition at a CO/O ratio of 4.0. Inhibition is reversed by white-light irradiation
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cytochrome c
-
inhibition by oxidized cytochrome c, 20 microM, 52.4% residual activity
methyl (2E,6E)-3,7-dimethyl-8-(3,4-methylenedioxyphenoxy)-octadienoate
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inhibits juvenile hormone biosynthesis in vitro by spontaneously active glands, presumably by direct inhibition of the epoxidase, and also inhibits the production of total methyl ester
NADP+
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2 mM, 57.2% residual activity
[4-([4-[1-(2-methylpropyl)-1H-imidazol-5-yl]phenoxy]methyl)phenyl](phenyl)methanone
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bifunctional compound, inhibits juvenile hormone III synthesis by intact glands as well as methyl farnesoate epoxidation by gland homogenates. Using the compound, a radiolabeled and photoactivatable diazirine or benzophenone group can be introduced to label the hydrophobic substrate binding site of the enzyme
additional information
-
inhibition 1,5-disubstituted imidazoles
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0077 - 0.38
methyl (2E,6E)-farnesoate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.003 - 0.005
methyl (2E,6E)-farnesoate
Diploptera punctata
-
pH 7.7, 30C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0109
1-(2-methylpropyl)-5-[4-([4-[3-(trifluoromethyl)-3H-diaziren-3-yl]benzyl]oxy)phenyl]-1H-imidazole
Diploptera punctata
-
pH 7.3, 30C
0.06
5-(2-(benzyloxy)phenyl)-1-(3,7-dimethyloct-6-en-1-yl)-1H-imidazole
Diploptera punctata
-
pH 7.7, 30C, inhibition of methyl (2E,6E)-farnesoate epoxidation by recombinant CYP15A1 in a reconstituted system
0.0002
5-(3-[[(2E)-3,7-dimethylocta-2,6-dien-1-yl]oxy]phenyl)-1-(2-methylpropyl)-1H-imidazole
Diploptera punctata
-
pH 7.7, 30C, inhibition of methyl (2E,6E)-farnesoate epoxidation by recombinant CYP15A1 in a reconstituted system
0.000025
5-[3-(benzyloxy)phenyl]-1-(2-methylpropyl)-1H-imidazole
Diploptera punctata
-
pH 7.7, 30C, inhibition of methyl (2E,6E)-farnesoate epoxidation by recombinant CYP15A1 in a reconstituted system
0.0003
[4-([4-[1-(2-methylpropyl)-1H-imidazol-5-yl]phenoxy]methyl)phenyl](phenyl)methanone
Diploptera punctata
-
pH 7.3, 30C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.7
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
exclusively microsomal
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55000
-
x * 55000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 55000, SDS-PAGE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Sf9 cells
expression of the His-tagged enzyme in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
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the enzyme may be useful in the design and screening of selective insect control agents