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Literature summary extracted from

  • 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 (2007), PLoS ONE, 2, e993.
    View publication on PubMedView publication on EuropePMC


EC Number Cloned (Comment) Organism DNA and amino acid sequence determination and analysis Ocimum basilicum

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism 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 Ocimum basilicum


EC Number Inhibitors Comment Organism Structure (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 Ocimum basilicum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac. coniferyl acetate + NADPH + H+ Ocimum basilicum
eugenol + acetate + NADP+


EC Number Organism UniProt Comment Textmining Ocimum basilicum Q15GI4


EC Number Reaction Comment Organism Reaction ID 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 Ocimum basilicum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac. cinnamyl acetate + NADPH + H+
Ocimum basilicum ? + acetate + NADP+
? coniferyl acetate + NADPH + H+
Ocimum basilicum eugenol + acetate + NADP+
? additional information determinants of the regioselectivity of the EGS-catalyzed reduction reaction, overview Ocimum basilicum ?


EC Number Subunits Comment Organism homodimer monomer or homodimer, inter-monomer association within the dimer, monomeric EGS is likely the functionally relevant form Ocimum basilicum monomer monomer or homodimer, inter-monomer association within the dimer, monomeric EGS is likely the functionally relevant form Ocimum basilicum


EC Number Synonyms Comment Organism EGS
Ocimum basilicum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism 25
assay at Ocimum basilicum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism 6.5
assay at Ocimum basilicum


EC Number Cofactor Comment Organism Structure NADPH enzyme binding structure, overview Ocimum basilicum

General Information

EC Number General Information Comment Organism evolution EGS is structurally related to the shortchain dehydrogenase/reductases, SDRs, and in particular, enzymes in the isoflavone-reductase-like subfamily Ocimum basilicum metabolism the enzyme is involved in the biosynthesis of phenylpropenes, overview Ocimum basilicum 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 Ocimum basilicum physiological function catalytic involvement in EGS of the conserved Lys132 in preparing the phenolic substrate for quinone methide formation through the proton-relay network Ocimum basilicum