Information on EC 1.1.1.318 - eugenol synthase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.1.1.318
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RECOMMENDED NAME
GeneOntology No.
eugenol synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
eugenol + a carboxylate + NADP+ = a coniferyl ester + NADPH + H+
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
eugenol and isoeugenol biosynthesis
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Phenylpropanoid biosynthesis
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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].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
cv. Mitchell
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
metabolism
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the enzyme is involved in the biosynthesis of phenylpropenes, overview
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-coumaryl acetate + NADPH + H+
chavicol + acetate + NADP+
show the reaction diagram
cinnamyl acetate + NADPH + H+
? + acetate + NADP+
show the reaction diagram
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?
coniferyl acetate + NADPH + H+
eugenol + acetate + NADP+
show the reaction diagram
additional information
?
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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
4-coumaryl acetate + NADPH + H+
chavicol + acetate + NADP+
show the reaction diagram
coniferyl acetate + NADPH + H+
eugenol + acetate + NADP+
show the reaction diagram
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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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.21
4-coumaryl acetate
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pH 7.5, 30C, recombinant enzyme
0.0933 - 0.3105
coniferyl acetate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6.8
4-coumaryl acetate
Larrea tridentata
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pH 7.5, 30C, recombinant enzyme
0.25 - 6.46
coniferyl acetate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
19500
4-coumaryl acetate
Larrea tridentata
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pH 7.5, 30C, recombinant enzyme
15224
0.8 - 22000
coniferyl acetate
4187
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.98
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purified native, wild-type CbEGS, pH 6.5, 28C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
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assay at
30
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assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
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
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 4C, 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
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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 hide
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