Cloned (Comment) | Organism |
---|---|
DNA and amino acid sequence determination and analysis | Ocimum basilicum |
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 | 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 | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
coniferyl acetate + NADPH + H+ | Ocimum basilicum | - |
eugenol + acetate + NADP+ | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Ocimum basilicum | Q15GI4 | - |
- |
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 | 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 | 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 | Comment | Organism |
---|---|---|
EGS | - |
Ocimum basilicum |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Ocimum basilicum |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6.5 | - |
assay at | Ocimum basilicum |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADPH | enzyme binding structure, overview | Ocimum basilicum |
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 |