EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
2.1.1.231 | 4'-hydroxyflavanone + S-adenosyl-L-methionine |
- |
Dianthus caryophyllus |
4'-methoxyflavanone + S-adenosyl-L-homocysteine |
- |
? |
2.1.1.231 | apigenin + S-adenosyl-L-methionine |
- |
Dianthus caryophyllus |
acacetin + S-adenosyl-L-homocysteine |
- |
? |
2.1.1.231 | genistein + S-adenosyl-L-methionine |
- |
Dianthus caryophyllus |
biochanin A + S-adenosyl-L-homocysteine |
- |
? |
2.1.1.231 | kaempferol + S-adenosyl-L-methionine |
- |
Dianthus caryophyllus |
kaempferide + S-adenosyl-L-homocysteine |
- |
? |
2.1.1.231 | more |
SOMT-2 has a regiospecific methylation activity, resulting in transforming 4'-hydroxyl group of flavonoids B-ring to 4'-methyl group. Caffeic acid, catechol, ferulic acid, and oricinol are biotransformed at less than 1% |
Glycine max |
? |
- |
? |
2.1.1.231 | more |
enzyme specifically methylates the hydroxy substituent in 4'-position of the flavones, flavanones and isoflavones in the presence of S-adenosyl-L-methionine. No activity towards hydroxycinnamic acid derivatives |
Dianthus caryophyllus |
? |
- |
? |
2.1.1.231 | more |
the only substrates found for CrOMT6 are 3'-O-methyl-eriodictyol (homoeriodictyol) and the corresponding flavones and flavonols, substrate specificty, overview. No or poor activity with naringenin, pentahydroxyflavanone, hesperetin, myricetin, 7,3'-O-dimethylquercetin, 7-O-methylquercetin, syringetin, apigenin, luteolin, tricetin, velutin, dihydrokaempferol, dihydroquercetin, dihydromyricetin, and 3'-O-methyl-dihydroquercetin, and also no activity with ferulic acid, coniferyl alcohol, vanillic acid vanillin, eugenol, isoeugenol, and guaicol. Not only the B-ring configuration, but also the size and shape of the A-ring are critical parts of the substrate specificity |
Catharanthus roseus |
? |
- |
? |
2.1.1.231 | more |
among the flavonoids, quercetin is the most favorable substrate, followed by luteolin, myricetin, quercetin glucoside, and fisetin, while only a single product is formed in each case. Product identification by mass-spectrometry and NMR spectrometric analysis. Susbtrate specificity, overview. Mechanistic overview of the regiospecific modification, a double bond between the C2 and the C3 and a single-ring-appended conjugate-hydroxyl group are crucial for the favorable enzymatic conversions of the GerMIII catalysis, modeling and molecular docking. Of all of the anthraquinones that are tested, only alizarin is methylated by the GerMIII at a detectable amount, whereas the methylation of all of the other remaining compounds is not evident. The common feature among the GerMIII substrates is the existence of two neighboring hydroxyl groups in the presence of a double bond between the C2 and the C3, as found in the quercetin, luteolin, myricetin, fisetin, and quercetin glucoside. GerMIII does not methylate many substrates including the close flavonoid relative catechin, which lacks the double bond between the C2 and the C3 |
Streptomyces sp. KCTC 0041BP |
? |
- |
- |
2.1.1.231 | S-adenosyl-L-methionine + 3'-O-methyleriodictyol |
- |
Catharanthus roseus |
S-adenosyl-L-homocysteine + 3',4'-O-dimethyleriodictyol |
- |
? |
2.1.1.231 | S-adenosyl-L-methionine + 3'-O-methyleriodictyol |
- |
Catharanthus roseus |
S-adenosyl-L-homocysteine + 3',4'-O-dimethyleriodictyol |
product identification by mass spectrometry |
? |