EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
2.1.1.267 | more |
OMT2 performs two sequential methylations at the 3'-and 5'-positions of the B-ring in myricetin (flavonol) and dihydromyricetin (dihydroflavonol) |
Catharanthus roseus |
? |
- |
? |
2.1.1.267 | more |
no activity with kaempferol, dihydrokaempferol, caffeate and caffeate esters |
Catharanthus roseus |
? |
- |
? |
2.1.1.267 | more |
enzyme is a regiospecific flavonoid 3'/5'-O-methyltransferase showing higher binding affinity and catalytic efficiency for quercetin and luteolin than for eriodictyol. No substrates: naringenin, apigenin, tricetin, kaempferol, daidzein, genistein |
Solanum lycopersicum |
? |
- |
? |
2.1.1.267 | more |
anthocyanin O-methyltransferase methylates anthocyanins of both groups, di- and trihydroxylated anthocyanins, quantitative trait locus analyses for the ratios of tri/di-hydroxylated and methylated/non-methylated anthocyanins using a population from an interspecific hybrid cross, relationship between the genotypes of the markers closest to the major quantitative trait loci and the expression levels of anthocyanin biosynthetic genes, overview |
Vitis vinifera |
? |
- |
? |
2.1.1.267 | more |
the enzyme AnthOMT shows a strong affinity for glycosylated anthocyanins, while other flavonoid glycosides and aglycones are much less preferred |
Solanum lycopersicum |
? |
- |
? |
2.1.1.267 | more |
the specificity of AnthOMT is mainly directed towards the 3' and 5' positions of the anthocyanin B-ring, to produce petunidin and malvidin glucosides, and is not active at the 4' position, substrate specificity of enzyme AnthOMT, overview. Poor activity with caffeic acid, no activity with pelargonidin-3-glucoside and delphinidin. AnthOMT is able to methylate the more complex substrates, e.g. an an extract of semi-polar compounds from Ros/Del tomato fruits preparation, resulting in a strong increase in malvidin 3-(4-coumaroyl)-rutinoside-5-glucoside |
Solanum lycopersicum |
? |
- |
? |
2.1.1.267 | more |
substrate specificity study using a number of potential substrates including anthocyanidins, anthocyanins, flavonols, flavones, flavan-3-ols, and phenolic acid as substrates based on optimized conditions, overview. Enzyme PsAOMT uses anthocyanins as methoxyl accepters, and acts to methylate the 3'-hydroxyl group of the B-ring with high affinity and efficiency. Pelargonidin 3-O-glucoside is the only tested anthocyanin compound that is not a substrate for PsAOMT. With delphinidin 3-O-glucoside, a sequential methylation occurs at the 3'- and 5'-hydroxyl group on the B-ring. In comparison with the substrates delphinidin 3-O-glucoside, quercetin 3-O-rutinoside, and quercetin, PsAOMT has a higher affinity for cyanidin 3-O-glucoside and cyanidin 3,5-O-diglucoside. Cyanidin-derived anthocyanins are high-affinity substrates for PsAOMT. No activity with the antocyanin pelargonidin 3-O-glucoside and the cyanidin delphinin. The enzyme also shows no activity with kaempferol 3-O-glucoside, kaempferol, apigenin, naringenin, epicatechin, and caffeic acid |
Paeonia suffruticosa |
? |
- |
- |
2.1.1.267 | more |
substrate specificity study using a number of potential substrates including anthocyanidins, anthocyanins, flavonols, flavones, flavan-3-ols, and phenolic acid as substrates based on optimized conditions, overview. Enzyme PtAOMT uses anthocyanins as methoxyl accepters, and acts to methylate the 3'-hydroxyl group of the B-ring with high affinity and efficiency. Pelargonidin 3-O-glucoside is the only tested anthocyanin compound that is not a substrate for PtAOMT. With delphinidin 3-O-glucoside, a sequential methylation occurs at the 3'- and 5'-hydroxyl group on the B-ring. In comparison with the substrates delphinidin 3-O-glucoside, quercetin 3-O-rutinoside, and quercetin, PtAOMT has a higher affinity for cyanidin 3-O-glucoside and cyanidin 3,5-O-diglucoside. Cyanidin-derived anthocyanins are high-affinity substrates for PtAOMT. No activity with the antocyanin pelargonidin 3-O-glucoside and the cyanidin delphinin. The enzyme also shows no activity with kaempferol 3-O-glucoside, kaempferol, apigenin, naringenin, epicatechin, and caffeic acid |
Paeonia tenuifolia |
? |
- |
- |
2.1.1.267 | more |
the flavonoid-O-methyltransferase from Citrus depressa has a broad substrate specificity and regioselectivity |
Citrus depressa |
? |
- |
- |
2.1.1.267 | more |
the flavonoid-O-methyltransferase from Citrus depressa has a broad substrate specificity and regioselectivity. Isozyme CdFOMT5 exhibits O-methyltransferase activity for quercetin, naringenin, (-)-epicatechin, and equol using S-adenosyl-L-methionine (SAM) as a methyl donor. The recombinant CdFOMT5 CdFOMT5 can catalyze the O-methylation of at least three hydroxyl groups of quercetin, and di- or tri-O-methylated quercetin products are obtained by this enzymatic reaction. CdFMOT5 prefers flavonol (3-hydroxyflavone) to other flavonoid structures. Thus, substrate structure, especially the C-ring in flavonoids, may strongly affect the substrate preference, including regioselectivity, of CdFOMT5 |
Citrus depressa |
? |
- |
- |