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Information on EC 1.1.1.318 - eugenol synthase and Organism(s) Ocimum basilicum and UniProt Accession Q15GI4

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     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.318 eugenol synthase
IUBMB 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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This record set is specific for:
Ocimum basilicum
UNIPROT: Q15GI4
Word Map
The taxonomic range for the selected organisms is: Ocimum basilicum
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
eugenol synthase, obegs1, eugenol synthase 1, cbegs1, cbegs2, phegs1, chavicol/eugenol synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
EGS2
-
-
-
0
eugenol synthase 1
294946
-
LtCES1
-
-
-
0
ObEGS1
891
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
eugenol + a carboxylate + NADP+ = a coniferyl ester + NADPH + H+
show the reaction diagram
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].
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
-
-
-
?
coniferyl acetate + NADPH + H+
eugenol + acetate + NADP+
show the reaction diagram
coniferyl acetate + NADPH + H+
eugenol + acetate + NADP+
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL 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
-
-
-
?
coniferyl acetate + NADPH + H+
eugenol + acetate + NADP+
show the reaction diagram
coniferyl acetate + NADPH + H+
eugenol + acetate + NADP+
show the reaction diagram
-
-
-
-
?
additional information
?
-
specificity of EGS for the production of allyl phenols in heterologically EGS expressing Fragaria x ananassa fruits
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.7
coniferyl acetate
pH 6.5, 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.004
coniferyl acetate
pH 6.5, 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.006
coniferyl acetate
pH 6.5, 25°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
higher transcript levels especially in young leaves and inflorescence, levels are positively correlated with eugenol contents
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
metabolism
the enzyme is involved in the biosynthesis of phenylpropenes, 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
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
EGS1_OCIBA
314
0
35607
Swiss-Prot
other Location (Reliability: 3)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
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
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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