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Information on EC 1.1.1.318 - eugenol synthase
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1.1.1.318 eugenol synthaseIUBMB Comments
The enzyme acts in the opposite direction. The enzymes from the plants Ocimum basilicum (sweet basil) [1,3], Clarkia breweri and Petunia hybrida only accept coniferyl acetate and form eugenol. The enzyme from Pimpinella anisum (anise) forms anol (from 4-coumaryl acetate) in vivo, although the recombinant enzyme can form eugenol from coniferyl acetate . The enzyme from Larrea tridentata (creosote bush) also forms chavicol from a coumaryl ester and can use NADH .
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Word Map
- 1.1.1.318
-
volatile
-
phenylpropanoids
- ocimum
-
phenylpropene
-
emit
-
scent
- petunia
- basilicum
- hybrida
- basil
- petals
-
pollinator
-
floral
-
cinnamyl
- isoeugenol
-
ripe
- cinnamate
- estragole
- strawberry
-
benzenoid
-
ammonia-lyase
- methyleugenol
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
eugenol synthase, cbegs1, cbegs2, obegs1, eugenol synthase 1, phegs1, chavicol/eugenol synthase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EGS
EGS1
EGS2
LtCES1
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
eugenol + a carboxylate + NADP+ = a coniferyl ester + NADPH + H+
-
-
-
-
eugenol + a carboxylate + NADP+ = a coniferyl ester + NADPH + H+
reaction mechanism, overview
eugenol + a carboxylate + NADP+ = a coniferyl ester + NADPH + H+
reaction mechanism, detailed overview
-
eugenol + a carboxylate + NADP+ = a coniferyl ester + NADPH + H+
eugenol synthase catalyzes the reductive displacement of acetate from the propenyl side chain of the substrate coniferyl acetate to produce the allyl-phenylpropene eugenol, two-step reaction mechanism involving the formation of a quinone-methide prior to reduction, overview. The formation of this intermediate is promoted by a hydrogen-bonding network that favors deprotonation of the substrate's 4-hydroxyl group and disfavors binding of the acetate moiety, akin to a push-pull catalytic mechanism, involvement of a quinone-methide, a conjugated enone, intermediate in the bond cleavage
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
eugenol:NADP+ oxidoreductase (coniferyl ester reducing)
The enzyme acts in the opposite direction. The enzymes from the plants Ocimum basilicum (sweet basil) [1,3], Clarkia breweri and Petunia hybrida [4] only accept coniferyl acetate and form eugenol. The enzyme from Pimpinella anisum (anise) forms anol (from 4-coumaryl acetate) in vivo, although the recombinant enzyme can form eugenol from coniferyl acetate [5]. The enzyme from Larrea tridentata (creosote bush) also forms chavicol from a coumaryl ester and can use NADH [2].
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-coumaryl acetate + NADPH + H+
chavicol + acetate + NADP+
-
-
GC-MS analysis product analysis
?
4-coumaryl acetate + NADPH + H+
chavicol + acetate + NADP+
-
-
?
4-coumaryl acetate + NADPH + H+
chavicol + acetate + NADP+
-
-
?
4-coumaryl acetate + NADPH + H+
chavicol + acetate + NADP+
-
-
?
coniferyl acetate + NADPH + H+
eugenol + acetate + NADP+
-
CbEGS1 is specific for isoeugenol production
-
?
coniferyl acetate + NADPH + H+
eugenol + acetate + NADP+
-
-
?
coniferyl acetate + NADPH + H+
eugenol + acetate + NADP+
-
-
?
coniferyl acetate + NADPH + H+
eugenol + acetate + NADP+
-
-
GC-MS analysis product analysis
?
coniferyl acetate + NADPH + H+
eugenol + acetate + NADP+
-
-
?
coniferyl acetate + NADPH + H+
eugenol + acetate + NADP+
-
GC-MS analysis product analysis
?
coniferyl acetate + NADPH + H+
eugenol + acetate + NADP+
-
ObEGS1 uses a quinone methide intermediate-based mechanism to generate an intermediate to which the reductive transfer of the reducing hydride can then be easily accomplished. the enzyme acts on the substrate via a push-pull mechanism, removing the proton of the para hydroxyl group and promoting the cleavage of the acetyl group. In the resultant quinone-methide intermediate, the C7 atom serves as the acceptor of the hydride ion from NADPH
-
?
coniferyl acetate + NADPH + H+
eugenol + acetate + NADP+
-
-
?
coniferyl acetate + NADPH + H+
eugenol + acetate + NADP+
-
-
?
coniferyl acetate + NADPH + H+
eugenol + acetate + NADP+
-
-
?
coniferyl acetate + NADPH + H+
eugenol + acetate + NADP+
-
-
-
?
coniferyl acetate + NADPH + H+
eugenol + acetate + NADP+
-
reaction via a quinone methide-like intermediate
-
?
coniferyl acetate + NADPH + H+
eugenol + acetate + NADP+
-
PhEGS1 converts coniferyl acetate to eugenol
-
?
additional information
?
-
Gymnadenia odoratissima proteins synthesize eugenol only
-
?
additional information
?
-
Gymnadenia odoratissima proteins synthesize eugenol only
-
?
additional information
?
-
-
Gymnadenia odoratissima proteins synthesize eugenol only
-
?
additional information
?
-
Gymnadenia densiflora proteins synthesize eugenol, as well as a smaller amount of isoeugenol
-
?
additional information
?
-
Gymnadenia densiflora proteins synthesize eugenol, as well as a smaller amount of isoeugenol
-
?
additional information
?
-
-
Gymnadenia densiflora proteins synthesize eugenol, as well as a smaller amount of isoeugenol
-
?
additional information
?
-
specificity of EGS for the production of allyl phenols in heterologically EGS expressing Fragaria x ananassa fruits
-
?
additional information
?
-
determinants of the regioselectivity of the EGS-catalyzed reduction reaction, overview
-
?
additional information
?
-
-
determinants of the regioselectivity of the EGS-catalyzed reduction reaction, overview
-
?
additional information
?
-
no substrate: 4-coumaryl acetate, cinnamyl acetate
-
?
additional information
?
-
no substrate: cinnamyl acetate
-
?
additional information
?
-
no substrate: cinnamyl acetate
-
?
additional information
?
-
no substrate: cinnamyl acetate
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
specificity of EGS for the production of allyl phenols in heterologically EGS expressing Fragaria x ananassa fruits
-
-
?
coniferyl acetate + NADPH + H+
eugenol + acetate + NADP+
-
-
-
?
coniferyl acetate + NADPH + H+
eugenol + acetate + NADP+
-
-
-
-
?
coniferyl acetate + NADPH + H+
eugenol + acetate + NADP+
-
PhEGS1 converts coniferyl acetate to eugenol
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(7S,8S)-ethyl (7,8-methylene)-dihydroferulate
EMDF, a mixed competitive inhibitor, chemical synthesis, and enzyme binding structure, overview. Key interactions between EMDF and the EGS holoenzyme include stacking of the phenyl ring of EMDF against the cofactor's nicotinamide ring and a water-mediated hydrogen-bonding interaction between the EMDF 4-hydroxy group and the side-chain amino moiety of a conserved lysine residue, Lys132
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
28
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.1
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
the highest specific activity levels of eugenol synthase are found in the stamens, followed closely by the pistil and petals
brenda
higher transcript levels especially in young leaves and inflorescence, levels are positively correlated with eugenol contents
brenda
higher transcript levels especially in young leaves and inflorescence, levels are positively correlated with eugenol contents
brenda
higher transcript levels especially in young leaves and inflorescence, levels are positively correlated with eugenol contents
brenda
higher transcript levels especially in young leaves and inflorescence, levels are positively correlated with eugenol contents
brenda
-
PhEGS1 is expressed specifically in the scent-producing parts of the flowers, limbs and tube, but not in other parts of the flowers nor in leaves
brenda
higher transcript levels especially in young leaves and inflorescence, levels are positively correlated with eugenol contents
brenda
higher transcript levels especially in young leaves and inflorescence, levels are positively correlated with eugenol contents
brenda
higher transcript levels especially in young leaves and inflorescence, levels are positively correlated with eugenol contents
brenda
higher transcript levels especially in young leaves and inflorescence, levels are positively correlated with eugenol contents
brenda
additional information
no expression in leaf tissue
brenda
additional information
no expression in leaf tissue
brenda
additional information
no expression in leaf tissue
brenda
additional information
no expression in leaf tissue
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
the enzyme is involved in the biosynthesis of phenylpropenes, overview
physiological function
additional information
evolution
EGS is structurally related to the shortchain dehydrogenase/reductases, SDRs, and in particular, enzymes in the isoflavone-reductase-like subfamily
evolution
the phenylpropene-forming eugenol synthase, EGS, belongs to a structural family of NADPH-dependent reductases that also includes isoeugenol synthase, IGS, pinoresinol-lariciresinol reductase, isoflavone reductase, and phenylcoumaran benzylic ether reductase, evolution and function of EGS1 and IGS1, overview
physiological function
catalytic involvement in EGS of the conserved Lys132 in preparing the phenolic substrate for quinone methide formation through the proton-relay network
physiological function
-
plants synthesize the volatile phenylpropene compounds eugenol and isoeugenol to serve in defense against herbivores and pathogens and to attract pollinators. Clarkia breweri flowers emit a mixture of eugenol and isoeugenol. Eugenol and isoeugenol differ in the position of the double bond in the propene side chain
physiological function
-
plants synthesize the volatile phenylpropene compounds eugenol and isoeugenol to serve in defense against herbivores and pathogens and to attract pollinators. Petunia hybrida flowers emit mostly isoeugenol with small amounts of eugenol. Eugenol and isoeugenol differ in the position of the double bond in the propene side chain
physiological function
introduction of petunia coniferyl alcohol acetyltransferase (CFAT) and eugenol synthase (EGS) into hybrid aspen. The overexpression of EGS alone results in a subtle increase in either eugenol or eugenol glycosides, and the overexpression of both CFAT and EGS results in significant increases in the levels of both eugenol and eugenol glycosides which are nonetheless lower than the increases seen with overexpression of CFAT alone
additional information
structure of a ternary complex of EGS bound to the cofactor NADP(H) and a mixed competitive inhibitor (7S,8S)-ethyl (7,8-methylene)-dihydroferulate, binding interactions within the EGS active site, overview
additional information
-
structure of a ternary complex of EGS bound to the cofactor NADP(H) and a mixed competitive inhibitor (7S,8S)-ethyl (7,8-methylene)-dihydroferulate, binding interactions within the EGS active site, overview
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). EGS1_OCIBA
314
0
35607
Swiss-Prot
other Location (Reliability: 3)
A0A0F8DH62_CERFI
296
0
31394
TrEMBL
other Location (Reliability: 2)
A0A2G9G1H8_9LAMI
313
0
35152
TrEMBL
other Location (Reliability: 2)
A0A2P6PYS0_ROSCH
312
0
34278
TrEMBL
other Location (Reliability: 3)
G7IVJ4_MEDTR
317
0
35856
TrEMBL
Mitochondrion (Reliability: 5)
A0A2G9GVK1_9LAMI
313
0
35033
TrEMBL
other Location (Reliability: 2)
A0A2P6PPB1_ROSCH
309
0
34293
TrEMBL
other Location (Reliability: 4)
A0A2P6PYQ4_ROSCH
238
0
26156
TrEMBL
other Location (Reliability: 3)
A0A2P6PYP3_ROSCH
309
0
34049
TrEMBL
other Location (Reliability: 4)
G7IVK6_MEDTR
317
0
35842
TrEMBL
Mitochondrion (Reliability: 5)
A0A396IJI8_MEDTR
223
0
25831
TrEMBL
other Location (Reliability: 4)
A0A072V477_MEDTR
308
0
34192
TrEMBL
other Location (Reliability: 4)
G7J743_MEDTR
312
0
34601
TrEMBL
other Location (Reliability: 4)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
36000
-
x * 38000, recombinant nontagged CbEGS2, SDS-PAGE, x * 36000, recombinant nontagged CbEGS1, SDS-PAGE
36200
38000
-
x * 38000, recombinant nontagged CbEGS2, SDS-PAGE, x * 36000, recombinant nontagged CbEGS1, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
monomer or homodimer, inter-monomer association within the dimer, monomeric EGS is likely the functionally relevant form
monomer
monomer or homodimer, inter-monomer association within the dimer, monomeric EGS is likely the functionally relevant form
?
-
x * 38000, recombinant nontagged CbEGS2, SDS-PAGE, x * 36000, recombinant nontagged CbEGS1, SDS-PAGE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
wild-type native apo-EGS, EGS as binary complex with cofactor NADPH or mixed competitive inhibitor (7S,8S)-ethyl (7,8-methylene)-dihydroferulate, or holo-EGS as ternary complex of bound to NADPH and inhibitor, from 0.1 M sodium succinate, pH 5.5, 5 mM NADP+, 0.3 M KCl, 2 mM DTT and 21% w/v PEG 3350, or from 0.1 M MOPSO, pH 6.5-7.0, 5 mM NADP+, 0.3 M KNO3, 2 mM DTT, and 28% w/v PEG monomethylether 5000, at 4°C, X-ray diffraction structure determination and analysis at 1.6-1.8 A resolution, modeling
homology modeling of structure
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F84V/I87Y
-
site-directed mutagenesis, the CbEGS1 mutant plants show increased isoeugenol production and an altered eugenol/isoeugenol ratio compared to the wild-type enzyme
F86V/I89Y
-
site-directed mutagenesis, the CbEGS2 mutant plants show increased isoeugenol production and an altered eugenol/isoeugenol ratio compared to the wild-type enzyme
Q86V/L89Y
-
site-directed mutagenesis, the mutant plants show increased isoeugenol production and an altered eugenol/isoeugenol ratio compared to the wild-type enzyme
additional information
recombinant Ocimum basilicum EGS transient overexpression in agroinfiltrated fruits leads to a substantial increase in the accumulation of chavicol and eugenol the endogenous phenylpropene pathway and the EGS protein compete for common substrates, specificity of EGS for the production of allyl phenols
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native EGS 118fold from petals by alternating steps of anion exchange and hydrophobic interaction chromatography, co-purification with isoeugenol synthase, EC 1.1.1.319. Recombinant His-tagged CbEGS1 and CbEGS2 from Escherichia coli by nickel affinity chromatography
-
recombinant GST-taged enzyme from Escherichia coli strain BL21 by glutathione affinity chromatography and dialysis
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression in GST-tagged Escherichia coli strain BL21
-
DNA and amino acid sequence determination and analysis, sequence comparison, quantitative expression analysis
-
DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis
-
DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, expression of nontagged and of His-tagged CbEGS1 and CbEGS2 in Escherichia coli
-
DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, quantitative expression analysis
EGS1 expression in Fragaria x ananassa cv. Elsanta via transfection with Agrobacterium tumefaciens strain AGL0, downregulation of chalcone synthase via antisense construct in parallel
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
in ripe strawberry receptacles, the expression of cinnamyl alcohol dehydrogenase 1 and eugenol synthase EGS2, structural genes involved in eugenol production, is down-regulated. The expression of transcription factor EOBII is silenced in ripe receptacles, and correlates with eugenol content in both fruit receptacle and petals. The expression of EOBII is repressed by auxins and activated by abscisic acid, in parallel to the ripening process
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Vassao, D.; Kim, S.; Milhollan, J.; Eichinger, D.; Davin, L.; Lewis, N.
A pinoresinol-lariciresinol reductase homologue from the creosote bush (Larrea tridentata) catalyzes the efficient in vitro conversion of p-coumaryl/coniferyl alcohol esters into the allylphenols chavicol/eugenol, but not the propenylphenols p-anol/isoeug
Arch. Biochem. Biophys.
465
209-218
2007
Larrea tridentata
brenda
Hoffmann, T.; Kurtzer, R.; Skowranek, K.; Kiessling, P.; Fridman, E.; Pichersky, E.; Schwab, W.
Metabolic engineering in strawberry fruit uncovers a dormant biosynthetic pathway
Metab. Eng.
13
527-531
2011
Ocimum basilicum (Q15GI4)
brenda
Koeduka, T.; Louie, G.V.; Orlova, I.; Kish, C.M.; Ibdah, M.; Wilkerson, C.G.; Bowman, M.E.; Baiga, T.J.; Noel, J.P.; Dudareva, N.; Pichersky, E.
The multiple phenylpropene synthases in both Clarkia breweri and Petunia hybrida represent two distinct protein lineages
Plant J.
54
362-374
2008
Clarkia breweri, Ocimum basilicum, Petunia x hybrida
brenda
Koeduka, T.; Orlova, I.; Baiga, T.J.; Noel, J.P.; Dudareva, N.; Pichersky, E.
The lack of floral synthesis and emission of isoeugenol in Petunia axillaris subsp. parodii is due to a mutation in the isoeugenol synthase gene
Plant J.
58
961-969
2009
Petunia axillaris subsp. parodii
brenda
Louie, G.V.; Baiga, T.J.; Bowman, M.E.; Koeduka, T.; Taylor, J.H.; Spassova, S.M.; Pichersky, E.; Noel, J.P.
Structure and reaction mechanism of basil eugenol synthase
PLoS ONE
2
e993
2007
Ocimum basilicum (Q15GI4), Ocimum basilicum
brenda
Koeduka, T.; Fridman, E.; Gang, D.; Vassao, D.; Jackson, B.; Kish, C.; Orlova, I.; Spassova, S.; Lewis, N.; Noel, J.; Baiga, T.; Dudareva, N.; Pichersky, E.
Eugenol and isoeugenol, characteristic aromatic constituents of spices, are biosynthesized via reduction of a coniferyl alcohol ester
Proc. Natl. Acad. Sci. USA
103
10128-10133
2006
Ocimum basilicum (Q15GI4)
brenda
Koeduka, T.; Suzuki, S.; Iijima, Y.; Ohnishi, T.; Suzuki, H.; Watanabe, B.; Shibata, D.; Umezawa, T.; Pichersky, E.; Hiratake, J.
Enhancement of production of eugenol and its glycosides in transgenic aspen plants via genetic engineering
Biochem. Biophys. Res. Commun.
436
73-78
2013
Petunia x hybrida (B2WSN1)
brenda
Anand, A.; Jayaramaiah, R.H.; Beedkar, S.D.; Singh, P.A.; Joshi, R.S.; Mulani, F.A.; Dholakia, B.B.; Punekar, S.A.; Gade, W.N.; Thulasiram, H.V.; Giri, A.P.
Comparative functional characterization of eugenol synthase from four different Ocimum species: Implications on eugenol accumulation
Biochim. Biophys. Acta
1864
1539-1547
2016
Ocimum basilicum (A0A1B2U6R8), Ocimum tenuiflorum (A0A1B2U6S6), Ocimum tenuiflorum, Ocimum gratissimum (A0A1B2U6S7), Ocimum kilimandscharicum (A0A1B2U6T4)
brenda
Gupta, A.K.; Schauvinhold, I.; Pichersky, E.; Schiestl, F.P.
Eugenol synthase genes in floral scent variation in Gymnadenia species
Funct. Integr. Genomics
14
779-788
2014
Gymnadenia x densiflora (A0A0E3H852), Gymnadenia x densiflora (A0A0E3KNP5), Gymnadenia x densiflora, Gymnadenia odoratissima (A0A0E3NBN0), Gymnadenia odoratissima (A0A0E3NCN9), Gymnadenia odoratissima
brenda
Medina-Puche, L.; Molina-Hidalgo, F.J.; Boersma, M.; Schuurink, R.C.; Lopez-Vidriero, I.; Solano, R.; Franco-Zorrilla, J.M.; Caballero, J.L.; Blanco-Portales, R.; Munoz-Blanco, J.
An R2R3-MYB transcription factor regulates eugenol production in ripe strawberry fruit receptacles
Plant Physiol.
168
598-614
2015
Fragaria x ananassa (T2AZ69), Fragaria x ananassa
brenda
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