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Enzyme Nomenclature
Information on EC 1.1.1.318 - eugenol synthase
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.1.1.318
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RECOMMENDED NAME
GeneOntology No.
eugenol synthase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
eugenol + a carboxylate + NADP+ = a coniferyl ester + NADPH + H+
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eugenol + a carboxylate + NADP+ = a coniferyl ester + NADPH + H+
reaction mechanism, detailed overview
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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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eugenol + a carboxylate + NADP+ = a coniferyl ester + NADPH + H+
reaction mechanism, overview
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
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the enzyme is involved in the biosynthesis of phenylpropenes, overview
physiological function
additional information
evolution
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EGS is structurally related to the shortchain dehydrogenase/reductases, SDRs, and in particular, enzymes in the isoflavone-reductase-like subfamily
evolution
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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
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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
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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
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catalytic involvement in EGS of the conserved Lys132 in preparing the phenolic substrate for quinone methide formation through the proton-relay network
additional information
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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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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+
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GC-MS analysis product analysis
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?
coniferyl acetate + NADPH + H+
eugenol + acetate + NADP+
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CbEGS1 is specific for isoeugenol production
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?
coniferyl acetate + NADPH + H+
eugenol + acetate + NADP+
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GC-MS analysis product analysis
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?
coniferyl acetate + NADPH + H+
eugenol + acetate + NADP+
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GC-MS analysis product analysis
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?
coniferyl acetate + NADPH + H+
eugenol + acetate + NADP+
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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
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-
?
coniferyl acetate + NADPH + H+
eugenol + acetate + NADP+
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?
coniferyl acetate + NADPH + H+
eugenol + acetate + NADP+
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reaction via a quinone methide-like intermediate
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coniferyl acetate + NADPH + H+
eugenol + acetate + NADP+
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PhEGS1 converts coniferyl acetate to eugenol
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-
?
additional information
?
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specificity of EGS for the production of allyl phenols in heterologically EGS expressing Fragaria x ananassa fruits
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additional information
?
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determinants of the regioselectivity of the EGS-catalyzed reduction reaction, overview
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
?
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Q15GI4
specificity of EGS for the production of allyl phenols in heterologically EGS expressing Fragaria x ananassa fruits
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coniferyl acetate + NADPH + H+
eugenol + acetate + NADP+
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?
coniferyl acetate + NADPH + H+
eugenol + acetate + NADP+
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PhEGS1 converts coniferyl acetate to eugenol
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?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(7S,8S)-ethyl (7,8-methylene)-dihydroferulate
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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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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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the highest specific activity levels of eugenol synthase are found in the stamens, followed closely by the pistil and petals
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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
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
36000
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x * 38000, recombinant nontagged CbEGS2, SDS-PAGE, x * 36000, recombinant nontagged CbEGS1, SDS-PAGE
38000
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x * 38000, recombinant nontagged CbEGS2, SDS-PAGE, x * 36000, recombinant nontagged CbEGS1, SDS-PAGE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
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x * 38000, recombinant nontagged CbEGS2, SDS-PAGE, x * 36000, recombinant nontagged CbEGS1, SDS-PAGE
homodimer
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monomer or homodimer, inter-monomer association within the dimer, monomeric EGS is likely the functionally relevant form
monomer
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monomer or homodimer, inter-monomer association within the dimer, monomeric EGS is likely the functionally relevant form
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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
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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
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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
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DNA and amino acid sequence determination and analysis, sequence comparison, quantitative expression analysis
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DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis
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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
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DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, quantitative expression analysis
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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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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F84V/I87Y
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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
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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
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site-directed mutagenesis, the mutant plants show increased isoeugenol production and an altered eugenol/isoeugenol ratio compared to the wild-type enzyme
additional information
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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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LINKS TO OTHER DATABASES (specific for EC-Number 1.1.1.318)
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