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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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1.1.1.318 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 taxonomic range for the selected organisms is: Ocimum basilicum
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
eugenol synthase, obegs1, eugenol synthase 1, cbegs1, cbegs2, phegs1, chavicol/eugenol synthase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EGS
EGS1
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
eugenol + a carboxylate + NADP+ = a coniferyl ester + NADPH + H+
reaction mechanism, 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
PATHWAY SOURCE
PATHWAYS
BRENDA
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)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
?
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
-
-
?
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+
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
higher transcript levels especially in young leaves and inflorescence, levels are positively correlated with eugenol contents
higher transcript levels especially in young leaves and inflorescence, levels are positively correlated with eugenol contents
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
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
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
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
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)
PDB
SCOP
CATH
UNIPROT
ORGANISM
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
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
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, 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)
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
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
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)
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)
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