Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.1.1.318 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

Cloned(Commentary)

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

Crystallization (Commentary)

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

Inhibitors

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)

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

Organism

Organism UniProt Comment Textmining
Ocimum basilicum Q15GI4
-
-

Reaction

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)

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 ?
-
?

Subunits

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

Synonyms

Synonyms Comment Organism
EGS
-
Ocimum basilicum

Temperature Optimum [°C]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
assay at Ocimum basilicum

Cofactor

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

General Information

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