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S-adenosyl-L-methionine + 3,4-dihydroxybenzaldehyde
?
moderate activity
-
-
?
S-adenosyl-L-methionine + 3,4-dihydroxybenzoic acid
S-adenosyl-L-homocysteine + ?
-
activity in presence of Co2+, no activity in presence of Mg2+
-
-
?
S-adenosyl-L-methionine + 4-coumaroyl-CoA
S-adenosyl-L-homocysteine + ?
-
very low activity
-
-
?
S-adenosyl-L-methionine + 5-hydroxy-ferulic acid
S-adenosyl-L-homocysteine + ?
-
activity in presence of Co2+, no activity in presence of Mg2+
-
-
?
S-adenosyl-L-methionine + 5-hydroxy-feruloyl-CoA
S-adenosyl-L-homocysteine + sinapoyl-CoA
S-adenosyl-L-methionine + 5-hydroxyconiferaldehyde
?
S-adenosyl-L-methionine + 5-hydroxyconiferaldehyde
S-adenosyl-L-homocysteine + sinapaldehyde
S-adenosyl-L-methionine + 5-hydroxyferulic acid
?
S-adenosyl-L-methionine + 5-hydroxyferulic acid
S-adenosyl-L-homocysteine + sinapic acid
-
-
-
-
?
S-adenosyl-L-methionine + 5-hydroxyferulic acid ethyl ester
?
high activity
-
-
?
S-adenosyl-L-methionine + 5-hydroxyferuloyl-CoA
?
-
-
-
-
?
S-adenosyl-L-methionine + 5-hydroxyferuoyl-CoA
S-adenosyl-L-homocysteine + sinapoyl-CoA
S-adenosyl-L-methionine + 7,8-dihydroxyflavone
?
-
OMT-15 shows 102% activity and OMT-17 shows 143% activity compared to myricetin
-
-
?
S-adenosyl-L-methionine + baicalein
?
-
-
-
?
S-adenosyl-L-methionine + baicalein
S-adenosyl-L-homocysteine + ?
S-adenosyl-L-methionine + caffeic acid
?
low activity
-
-
?
S-adenosyl-L-methionine + caffeic acid
S-adenosyl-L-homocysteine + ?
S-adenosyl-L-methionine + caffeic acid
S-adenosyl-L-homocysteine + ferulic acid
S-adenosyl-L-methionine + caffeic acid ethyl ester
?
S-adenosyl-L-methionine + caffeic alcohol
S-adenosyl-L-homocysteine + ?
S-adenosyl-L-methionine + caffeoyl alcohol
?
-
-
-
?
S-adenosyl-L-methionine + caffeoyl alcohol
S-adenosyl-L-homocysteine + ?
-
-
-
?
S-adenosyl-L-methionine + caffeoyl alcohol
S-adenosyl-L-homocysteine + coniferyl alcohol
-
-
-
?
S-adenosyl-L-methionine + caffeoyl aldehyde
?
-
-
-
?
S-adenosyl-L-methionine + caffeoyl aldehyde
S-adenosyl-L-homocysteine + ?
S-adenosyl-L-methionine + caffeoyl aldehyde
S-adenosyl-L-homocysteine + coniferaldehyde
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + ?
-
OMT-15 shows 100% activity and OMT-17 shows 58% activity compared to myricetin
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl CoA
33% of the activity with luteolin
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
S-adenosyl-L-methionine + caffeoyl-D-glucose
S-adenosyl-L-homocysteine + feruloyl-D-glucose
-
-
-
-
?
S-adenosyl-L-methionine + caffeoylaldehyde
?
low activity
-
-
?
S-adenosyl-L-methionine + coniferaldehyde
S-adenosyl-L-homocysteine + sinapaldehyde
-
-
-
?
S-adenosyl-L-methionine + coniferyl alcohol
S-adenosyl-L-homocysteine + sinapyl alcohol
-
-
-
?
S-adenosyl-L-methionine + cyanidin 3-O-glucoside
S-adenosyl-L-homocysteine + peonidin 3-O-glucoside
-
-
-
?
S-adenosyl-L-methionine + dihydroquercetin
S-adenosyl-L-homocysteine + ?
2.5% of the activity with luteolin
-
-
?
S-adenosyl-L-methionine + epigallocatechin-3-O-gallate
S-adenosyl-L-homocysteine + ?
-
-
methylation occurs in 3'-, 3''- and 4''-position
-
?
S-adenosyl-L-methionine + eriodictyol
?
-
-
-
?
S-adenosyl-L-methionine + eriodictyol
S-adenosyl-L-homocysteine + ?
S-adenosyl-L-methionine + eriodictyol
S-adenosyl-L-homocysteine + eriodictoyl-3'-O-methylether + eriodictoyl-4'-O-methylether
15% of the activity with luteolin
80% para product versus 20% meta in the wild type
-
?
S-adenosyl-L-methionine + eriodictyol
S-adenosyl-L-homocysteine + homoeriodictyol
-
single product
-
?
S-adenosyl-L-methionine + eriodictyol
S-adenosyl-L-homocysteine + homoeriodictyol + hesperetin
-
-
-
?
S-adenosyl-L-methionine + esculetin
S-adenosyl-L-homocysteine + ?
S-adenosyl-L-methionine + esculetin
S-adenosyl-L-homocysteine + scopoletin
-
-
-
?
S-adenosyl-L-methionine + ferulic acid
S-adenosyl-L-homocysteine + sinapic acid
-
-
-
?
S-adenosyl-L-methionine + feruloyl-CoA
S-adenosyl-L-homocysteine + ?
-
very low activity
-
-
?
S-adenosyl-L-methionine + luteolin
?
-
-
-
?
S-adenosyl-L-methionine + luteolin
S-adenosyl-L-homocysteine + ?
S-adenosyl-L-methionine + luteolin
S-adenosyl-L-homocysteine + chrysoeriol
-
-
-
?
S-adenosyl-L-methionine + luteolin
S-adenosyl-L-homocysteine + scoparol
S-adenosyl-L-methionine + myricetin
?
high activity
-
-
?
S-adenosyl-L-methionine + quercetagetin
S-adenosyl-L-homocysteine + ?
-
no activity in presence of Co2+, low activity in presence of Mg2+
-
-
?
S-adenosyl-L-methionine + quercetagetin
S-adenosyl-L-homocysteine + quercetagetin 6,3'-di-O-methylether
-
-
-
?
S-adenosyl-L-methionine + quercetin
?
S-adenosyl-L-methionine + quercetin
S-adenosyl-L-homocysteine + ?
S-adenosyl-L-methionine + quercetin
S-adenosyl-L-homocysteine + isorhamnetin
S-adenosyl-L-methionine + scutellarein
?
-
-
-
?
S-adenosyl-L-methionine + scutellarein
S-adenosyl-L-homocysteine + ?
S-adenosyl-L-methionine + sinapoyl-CoA
S-adenosyl-L-homocysteine + ?
-
low activity
-
-
?
S-adenosyl-L-methionine + trans-caffeic acid esters
S-adenosyl-L-homocysteine + ?
-
such as methyl caffeate, chlorogenic acid, trans-5-O-caffeoylshikimate, rosmarinic acid, poor substrates
-
-
?
S-adenosyl-L-methionine + tricetin
S-adenosyl-L-homocysteine + selgin
highest activity
tricin, also identified as product
-
?
additional information
?
-
S-adenosyl-L-methionine + 5-hydroxy-feruloyl-CoA
S-adenosyl-L-homocysteine + sinapoyl-CoA
-
-
-
?
S-adenosyl-L-methionine + 5-hydroxy-feruloyl-CoA
S-adenosyl-L-homocysteine + sinapoyl-CoA
-
-
-
?
S-adenosyl-L-methionine + 5-hydroxy-feruloyl-CoA
S-adenosyl-L-homocysteine + sinapoyl-CoA
3' methylating activity
-
-
?
S-adenosyl-L-methionine + 5-hydroxy-feruloyl-CoA
S-adenosyl-L-homocysteine + sinapoyl-CoA
-
-
-
-
?
S-adenosyl-L-methionine + 5-hydroxy-feruloyl-CoA
S-adenosyl-L-homocysteine + sinapoyl-CoA
-
-
-
?
S-adenosyl-L-methionine + 5-hydroxy-feruloyl-CoA
S-adenosyl-L-homocysteine + sinapoyl-CoA
-
56% activity compared to caffeoyl-CoA
-
-
?
S-adenosyl-L-methionine + 5-hydroxyconiferaldehyde
?
-
-
-
?
S-adenosyl-L-methionine + 5-hydroxyconiferaldehyde
?
low activity
-
-
?
S-adenosyl-L-methionine + 5-hydroxyconiferaldehyde
?
moderate activity
-
-
?
S-adenosyl-L-methionine + 5-hydroxyconiferaldehyde
S-adenosyl-L-homocysteine + sinapaldehyde
-
-
-
-
?
S-adenosyl-L-methionine + 5-hydroxyconiferaldehyde
S-adenosyl-L-homocysteine + sinapaldehyde
-
-
-
?
S-adenosyl-L-methionine + 5-hydroxyferulic acid
?
-
OMT-15 shows 25% activity and OMT-17 shows 18% activity compared to myricetin
-
-
?
S-adenosyl-L-methionine + 5-hydroxyferulic acid
?
high activity
-
-
?
S-adenosyl-L-methionine + 5-hydroxyferuoyl-CoA
S-adenosyl-L-homocysteine + sinapoyl-CoA
-
-
-
-
?
S-adenosyl-L-methionine + 5-hydroxyferuoyl-CoA
S-adenosyl-L-homocysteine + sinapoyl-CoA
-
-
-
?
S-adenosyl-L-methionine + 5-hydroxyferuoyl-CoA
S-adenosyl-L-homocysteine + sinapoyl-CoA
-
-
-
-
?
S-adenosyl-L-methionine + 5-hydroxyferuoyl-CoA
S-adenosyl-L-homocysteine + sinapoyl-CoA
-
-
-
-
?
S-adenosyl-L-methionine + 5-hydroxyferuoyl-CoA
S-adenosyl-L-homocysteine + sinapoyl-CoA
-
-
-
?
S-adenosyl-L-methionine + 5-hydroxyferuoyl-CoA
S-adenosyl-L-homocysteine + sinapoyl-CoA
-
-
-
-
?
S-adenosyl-L-methionine + 5-hydroxyferuoyl-CoA
S-adenosyl-L-homocysteine + sinapoyl-CoA
-
-
-
-
?
S-adenosyl-L-methionine + 5-hydroxyferuoyl-CoA
S-adenosyl-L-homocysteine + sinapoyl-CoA
-
-
-
-
?
S-adenosyl-L-methionine + baicalein
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + baicalein
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + baicalein
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + baicalein
S-adenosyl-L-homocysteine + ?
-
-
-
?
S-adenosyl-L-methionine + caffeic acid
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + caffeic acid
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + caffeic acid
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + caffeic acid
S-adenosyl-L-homocysteine + ferulic acid
-
activity in presence of Co2+, no activity in presence of Mg2+
-
-
?
S-adenosyl-L-methionine + caffeic acid
S-adenosyl-L-homocysteine + ferulic acid
10% of the activity with luteolin
synthesis of a single meta-methylated product
-
?
S-adenosyl-L-methionine + caffeic acid
S-adenosyl-L-homocysteine + ferulic acid
-
-
-
?
S-adenosyl-L-methionine + caffeic acid
S-adenosyl-L-homocysteine + ferulic acid
-
-
-
?
S-adenosyl-L-methionine + caffeic acid
S-adenosyl-L-homocysteine + ferulic acid
-
-
-
?
S-adenosyl-L-methionine + caffeic acid ethyl ester
?
low activity
-
-
?
S-adenosyl-L-methionine + caffeic acid ethyl ester
?
moderate activity
-
-
?
S-adenosyl-L-methionine + caffeic alcohol
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + caffeic alcohol
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + caffeic alcohol
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + caffeic alcohol
S-adenosyl-L-homocysteine + ?
-
-
-
?
S-adenosyl-L-methionine + caffeoyl aldehyde
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + caffeoyl aldehyde
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + caffeoyl aldehyde
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + caffeoyl aldehyde
S-adenosyl-L-homocysteine + ?
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
enzyme predicted to catalyze first methylation step during biosynthesis of monolignols
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
enzyme responsible for the first methylation step during biosynthesis of monolignols
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
possibly involved in biosynthesis of oat avenanthramide phytoalexins
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
preferred substrate, 3' methylating activity
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
bi-functional enzyme, involved in lignin biosynthesis
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
the enzyme is involved in lignin biosynthesis
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
trans-caffeoyl-CoA preferred
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
inducible
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
bi-functional enzyme, involved in lignin biosynthesis
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
reaction of the overall disease resistance response of plants
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
enzyme plays a pivotal role in cell wall reinforcement during the induced disease resistance response
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
if CCoAOMT and cinnamoyl co-enzyme A reductase are coupled together, they can convert caffeoyl-CoA to coniferaldehyde if pH changes from 7.5 to 6.0
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
best substrate
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
moderate activity
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
Zinnia sp.
-
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
Zinnia sp.
-
essential role in the synthesis of guaiacyl lignin units as well as in the supply of substrates for the synthesis of syringyl lignin units
-
-
?
S-adenosyl-L-methionine + eriodictyol
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + eriodictyol
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + eriodictyol
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + eriodictyol
S-adenosyl-L-homocysteine + ?
-
-
-
?
S-adenosyl-L-methionine + esculetin
S-adenosyl-L-homocysteine + ?
20% of the activity with luteolin
-
-
?
S-adenosyl-L-methionine + esculetin
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + esculetin
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + esculetin
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + esculetin
S-adenosyl-L-homocysteine + ?
-
-
-
?
S-adenosyl-L-methionine + luteolin
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + luteolin
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + luteolin
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + luteolin
S-adenosyl-L-homocysteine + ?
-
-
-
?
S-adenosyl-L-methionine + luteolin
S-adenosyl-L-homocysteine + scoparol
-
-
-
?
S-adenosyl-L-methionine + luteolin
S-adenosyl-L-homocysteine + scoparol
-
synthesis of a single meta-methylated product
-
?
S-adenosyl-L-methionine + luteolin
S-adenosyl-L-homocysteine + scoparol
-
-
-
?
S-adenosyl-L-methionine + quercetin
?
-
-
-
?
S-adenosyl-L-methionine + quercetin
?
moderate activity
-
-
?
S-adenosyl-L-methionine + quercetin
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + quercetin
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + quercetin
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + quercetin
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + quercetin
S-adenosyl-L-homocysteine + ?
-
-
-
?
S-adenosyl-L-methionine + quercetin
S-adenosyl-L-homocysteine + isorhamnetin
60% of the activity with luteolin
synthesis of a single meta-methylated product
-
?
S-adenosyl-L-methionine + quercetin
S-adenosyl-L-homocysteine + isorhamnetin
best substrate
-
-
?
S-adenosyl-L-methionine + scutellarein
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + scutellarein
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + scutellarein
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + scutellarein
S-adenosyl-L-homocysteine + ?
-
-
-
?
additional information
?
-
enzyme shows a strong preference for methylating the para position of flavanones and dihydroflavonols, whereas flavones and flavonols are methylated in the meta-position
-
-
?
additional information
?
-
-
enzyme shows a strong preference for methylating the para position of flavanones and dihydroflavonols, whereas flavones and flavonols are methylated in the meta-position
-
-
?
additional information
?
-
enzyme CCoAOMT7 binds to S-adenosyl-L-homocysteine hydrolase (SAHH) and S-adenosyl-L-methionine synthases (SAMSs) in vivo
-
-
-
additional information
?
-
CCoAOMT7 in Arabidopsis thaliana shows a strong preference to methylate para-position of flavanones and dihydroflavonols, and also a relatively lower activity on caffeoyl-CoA using S-adenosyl-L-methionine (SAM or AdoMet) as methyl donor to produce feruloyl-CoA. CCoAOMT7 also shows methyltransferase activity on caffeoyl CoA, although it shows the highest activity on luteolin, a kind of flavonoids
-
-
-
additional information
?
-
enzyme CCoAOMT7 binds to S-adenosyl-L-homocysteine hydrolase (SAHH) and S-adenosyl-L-methionine synthases (SAMSs) in vivo
-
-
-
additional information
?
-
CCoAOMT7 in Arabidopsis thaliana shows a strong preference to methylate para-position of flavanones and dihydroflavonols, and also a relatively lower activity on caffeoyl-CoA using S-adenosyl-L-methionine (SAM or AdoMet) as methyl donor to produce feruloyl-CoA. CCoAOMT7 also shows methyltransferase activity on caffeoyl CoA, although it shows the highest activity on luteolin, a kind of flavonoids
-
-
-
additional information
?
-
the enzyme is not able to methylate caffeic acid, 5-hydroxyferulic acid, 5-hydroxyconiferyl alcohol, kaempferol and naringenin
-
-
-
additional information
?
-
-
the enzyme is not able to methylate caffeic acid, 5-hydroxyferulic acid, 5-hydroxyconiferyl alcohol, kaempferol and naringenin
-
-
-
additional information
?
-
-
no activity with catechol, kaempferol, coniferyl aldehyde, and coniferyl alcohol
-
-
-
additional information
?
-
CoA and caffeoyl CoA are binding with high affinity to the enzymes in the presence and absence of S-adenosyl-L-methionine, thereby with higher affinity to isozyme CCoAOMT2 than CCoAOMT1, molecular dynamics, simulations, and docking analysis, overview. Conserved active site residues Met58, Thr60, Val63, Glu82, Gly84, Ser90, Asp160, Asp162, Thr169, Asn191 and Arg203 in CCoAOMT1 and CCoAOMT2 enzymes create the positive charge to balance the negatively charged caffeoyl CoA and play an important role in maintaining a functional conformation and are directly involved in donor substrate binding
-
-
?
additional information
?
-
CoA and caffeoyl CoA are binding with high affinity to the enzymes in the presence and absence of S-adenosyl-L-methionine, thereby with higher affinity to isozyme CCoAOMT2 than CCoAOMT1, molecular dynamics, simulations, and docking analysis, overview. Conserved active site residues Met58, Thr60, Val63, Glu82, Gly84, Ser90, Asp160, Asp162, Thr169, Asn191 and Arg203 in CCoAOMT1 and CCoAOMT2 enzymes create the positive charge to balance the negatively charged caffeoyl CoA and play an important role in maintaining a functional conformation and are directly involved in donor substrate binding
-
-
?
additional information
?
-
CCoAOMT down-regulation induces changes in xylem cell-wall structure and the lignin fractions
-
-
?
additional information
?
-
-
CCoAOMT down-regulation induces changes in xylem cell-wall structure and the lignin fractions
-
-
?
additional information
?
-
flax CCoAOMT possesses a small, but probably significant 5' methylating activity, in addition to a more usual 3' methylating activity
-
-
?
additional information
?
-
-
flax CCoAOMT possesses a small, but probably significant 5' methylating activity, in addition to a more usual 3' methylating activity
-
-
?
additional information
?
-
-
no activity with catechol, kaempferol, coniferyl aldehyde, and coniferyl alcohol
-
-
-
additional information
?
-
-
no activity with catechol, kaempferol, coniferyl aldehyde, and coniferyl alcohol
-
-
-
additional information
?
-
in silico studies suggest that alcoholic and aldehydic substrates are preferred to those of caffeic, sinapic, and ferulic acid by both caffeic acid-O-methyltransferase, EC 2.1.1.68, and caffeoyl-coenzyme A-O-methyltransferase with a marked preference for CoA ester substrates over free acids, aldehydes, and alcohols
-
-
?
additional information
?
-
-
in silico studies suggest that alcoholic and aldehydic substrates are preferred to those of caffeic, sinapic, and ferulic acid by both caffeic acid-O-methyltransferase, EC 2.1.1.68, and caffeoyl-coenzyme A-O-methyltransferase with a marked preference for CoA ester substrates over free acids, aldehydes, and alcohols
-
-
?
additional information
?
-
a catalytic triad, consisting of Lys157-Asn181-Asp228 residues is required for complete methyl transfer in case of a cation-dependent phenylpropanoid and flavonoid O-methyl transferase. This triad appears essential for efficient methyl transfer to catechol-like hydroxyl group in phenolics. The triad is conserved among all characterized plant caffeoyl coenzyme A O-methyltransferase-like enzymes
-
-
?
additional information
?
-
-
caffeoyl-CoA preferred to 5-hydroxyferuoyl-CoA
-
-
?
additional information
?
-
COMT catalyzes the multi-step methylation reactions of hydroxylated monomeric lignin precursors, and plays a pivotal position in the lignin biosynthetic pathway
-
-
?
additional information
?
-
-
COMT catalyzes the multi-step methylation reactions of hydroxylated monomeric lignin precursors, and plays a pivotal position in the lignin biosynthetic pathway
-
-
?
additional information
?
-
-
OMT-15 and -17 cannot utilize naringenin, apigenin, or kaempferol as substrates, taxifolin and eriodictyol do not serve as methyl acceptors
-
-
?
additional information
?
-
-
no substrates are caffeic acid, bergaptol, xanthotoxol, luteolin, esculetin
-
-
?
additional information
?
-
-
no activity with caffeic acid or 5-hydroxyferulic acid
-
-
-
additional information
?
-
no activity with catechol, kaempferol, caffeoyl aldehyde, caffeoyl acid, coniferyl aldehyde, and coniferyl alcohol
-
-
-
additional information
?
-
-
no activity with catechol, kaempferol, caffeoyl aldehyde, caffeoyl acid, coniferyl aldehyde, and coniferyl alcohol
-
-
-
additional information
?
-
no activity with kaempferol and dihydrokaempferol
-
-
-
additional information
?
-
-
no activity with kaempferol and dihydrokaempferol
-
-
-
additional information
?
-
CCoAOMT2 possesses more affinity toward caffeoyl CoA, feruloyl CoA, 5-hydroxy feruloyl CoA and sinapoyl CoA than CCoAOMT1
-
-
?
additional information
?
-
CCoAOMT2 possesses more affinity toward caffeoyl CoA, feruloyl CoA, 5-hydroxy feruloyl CoA and sinapoyl CoA than CCoAOMT1
-
-
?
additional information
?
-
no activity with caffeic acid, 5-hydroxyferuloyl-CoA, feruloyl-CoA, 4-coumaroyl-CoA, and 5-hydroxyferuloyl-CoA
-
-
-
additional information
?
-
-
no activity with caffeic acid, 5-hydroxyferuloyl-CoA, feruloyl-CoA, 4-coumaroyl-CoA, and 5-hydroxyferuloyl-CoA
-
-
-
additional information
?
-
COMT catalyzes the multi-step methylation reactions of hydroxylated monomeric lignin precursors, and plays a pivotal position in the lignin biosynthetic pathway
-
-
?
additional information
?
-
-
COMT catalyzes the multi-step methylation reactions of hydroxylated monomeric lignin precursors, and plays a pivotal position in the lignin biosynthetic pathway
-
-
?
additional information
?
-
the enzyme is capable of 3'- and 5'-methylating not only acid, aldehyde and alcohol precursors, but also ester precursors, broad substrate specificity, overview
-
-
?
additional information
?
-
-
the enzyme is capable of 3'- and 5'-methylating not only acid, aldehyde and alcohol precursors, but also ester precursors, broad substrate specificity, overview
-
-
?
additional information
?
-
-
very poor substrates: 4-coumarate, caffeate, ferulate, 5-hydroxyferulate and sinapate, coumarylaldehyde, caffeoyaldehyde, coniferaldehyde, 5-hydroxyconiferaldehyde, sinapaldehyde, 4-coumaryl alcohol, caffeoyl alcohol, coniferyl alcohol, 5-hydroxyconiferyl alcohol and sinapyl alcohol
-
-
?
additional information
?
-
-
recombinant TaCCoAOMT1 protein can only use caffeoyl-CoA and 5-hydroxyferuloyl-CoA as effective substrates and caffeoyl-CoA as the best substrate. No activity with p-coumarate, caffeate, ferulate, 5-hydroxyferulate, sinapate, coumarylaldehyde, caffeoyaldehyde, coniferaldehyde, 5-hydroxyconiferaldehyde, and sinapaldehyde, 4-coumaryl alcohol, caffeoyl alcohol, coniferyl alcohol, 5-hydroxyconiferyl alcohol, and sinapyl alcohol
-
-
-
additional information
?
-
enzyme prefers as a substrate the flavone tricetin. Enzyme shows a lower activity with vanillin precursor, 3,4-dihydroxybenzaldehyde, than with tricetin
-
-
?
additional information
?
-
enzyme prefers as a substrate the flavone tricetin. Enzyme shows a lower activity with vanillin precursor, 3,4-dihydroxybenzaldehyde, than with tricetin
-
-
?
additional information
?
-
-
enzyme prefers as a substrate the flavone tricetin. Enzyme shows a lower activity with vanillin precursor, 3,4-dihydroxybenzaldehyde, than with tricetin
-
-
?
additional information
?
-
-
caffeoyl-CoA preferred to 5-hydroxyferuoyl-CoA
-
-
?
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0.002
-
with 5-hydroxyferulic acid
0.00271
with coniferyl alcohol as substrate, at pH 7.5 and 37°C
0.00273
-
with caffeoyl acid as substrate, at pH 7.5 and 37°C
0.00338
with caffeoyl-CoA as substrate, at pH 7.5 and 37°C
0.00379
isoform CCoAOMT1, with 5-hydroxyconiferaldehyde as substrate, at pH 7.5 and 37°C
0.00443
with esculetin as substrate, at pH 7.5 and 37°C
0.00484
with caffeic alcohol as substrate, at pH 7.5 and 37°C
0.00518
with esculetin as substrate, at pH 7.5 and 37°C
0.00569
with coniferaldehyde as substrate, at pH 7.5 and 37°C
0.00664
isoform CCoAOMT2, with caffeoyl aldehyde as substrate, at pH 7.5 and 37°C
0.00705
with caffeoyl aldehyde as substrate, at pH 7.5 and 37°C
0.008
-
with 5-hydroxyferuloyl-CoA
0.00804
isoform CCoAOMT2, with caffeoyl alcohol as substrate, at pH 7.5 and 37°C
0.00897
with caffeoyl-CoA as substrate, at pH 7.5 and 37°C
0.0107
with eriodictyol as substrate, at pH 7.5 and 37°C
0.01107
isoform CCoAOMT2, with 5-hydroxyconiferaldehyde as substrate, at pH 7.5 and 37°C
0.01195
isoform CCoAOMT2, with baicalein as substrate, at pH 7.5 and 37°C
0.01285
with luteolin as substrate, at pH 7.5 and 37°C
0.01289
-
with caffeoyl aldehyde as substrate, at pH 7.5 and 37°C
0.01332
isoform CCoAOMT1, with caffeoyl aldehyde as substrate, at pH 7.5 and 37°C
0.01339
with quercetin as substrate, at pH 7.5 and 37°C
0.01476
isoform CCoAOMT2, with scutellarein as substrate, at pH 7.5 and 37°C
0.01607
with caffeoyl alcohol as substrate, at pH 7.5 and 37°C
0.018
isoform CCoAOMT1, with eriodictyol as substrate, at pH 7.5 and 37°C
0.01824
-
with caffeoyl-CoA as substrate, at pH 7.5 and 37°C
0.0186
-
with caffeoyl-CoA as substrate, at pH 7.5 and 37°C
0.01923
with ferulic acid as substrate, at pH 7.5 and 37°C
0.02016
with caffeic acid as substrate, at pH 7.5 and 37°C
0.02084
-
with caffeic alcohol as substrate, at pH 7.5 and 37°C
0.021
-
with caffeoyl-CoA
0.02313
isoform CCoAOMT1, with scutellarein as substrate, at pH 7.5 and 37°C
0.02325
-
with caffeoyl-CoA as substrate, at pH 7.5 and 37°C
0.02643
isoform CCoAOMT1, with baicalein as substrate, at pH 7.5 and 37°C
0.02719
isoform CCoAOMT2, with caffeoyl-CoA as substrate, at pH 7.5 and 37°C
0.0313
-
unreliable, great loss during purification
0.03412
-
with scutellarein as substrate, at pH 7.5 and 37°C
0.03484
isoform CCoAOMT1, with caffeoyl-CoA as substrate, at pH 7.5 and 37°C
0.03572
with baicalein as substrate, at pH 7.5 and 37°C
0.03592
-
with luteolin as substrate, at pH 7.5 and 37°C
0.03742
isoform CCoAOMT2, with luteolin as substrate, at pH 7.5 and 37°C
0.04291
-
with caffeic alcohol as substrate, at pH 7.5 and 37°C
0.04316
isoform CCoAOMT2, with quercetin as substrate, at pH 7.5 and 37°C
0.044
-
with eriodictyol as substrate, at pH 7.5 and 37°C
0.04714
with eriodictyol as substrate, at pH 7.5 and 37°C
0.04726
-
with caffeic alcohol as substrate, at pH 7.5 and 37°C
0.04848
isoform CCoAOMT2, with eriodictyol as substrate, at pH 7.5 and 37°C
0.04961
-
with baicalein as substrate, at pH 7.5 and 37°C
0.05067
with scutellarein as substrate, at pH 7.5 and 37°C
0.05571
isoform CCoAOMT1, with luteolin as substrate, at pH 7.5 and 37°C
0.05666
with luteolin as substrate, at pH 7.5 and 37°C
0.05677
isoform CCoAOMT1, with quercetin as substrate, at pH 7.5 and 37°C
0.06077
-
with quercetin as substrate, at pH 7.5 and 37°C
0.06396
-
with quercetin as substrate, at pH 7.5 and 37°C
0.06852
-
with luteolin as substrate, at pH 7.5 and 37°C
0.07092
-
with scutellarein as substrate, at pH 7.5 and 37°C
0.07201
-
with eriodictyol as substrate, at pH 7.5 and 37°C
0.07343
-
with baicalein as substrate, at pH 7.5 and 37°C
0.07787
-
with eriodictyol as substrate, at pH 7.5 and 37°C
0.07834
-
with luteolin as substrate, at pH 7.5 and 37°C
0.08656
-
with quercetin as substrate, at pH 7.5 and 37°C
0.08675
-
with scutellarein as substrate, at pH 7.5 and 37°C
0.08976
-
with baicalein as substrate, at pH 7.5 and 37°C
0.10781
-
with esculetin as substrate, at pH 7.5 and 37°C
0.12782
with quercetin as substrate, at pH 7.5 and 37°C
0.19117
-
with esculetin as substrate, at pH 7.5 and 37°C
0.22432
-
with esculetin as substrate, at pH 7.5 and 37°C
0.00143
-
with caffeoyl acid as substrate, at pH 7.5 and 37°C
0.00143
-
with caffeoyl acid as substrate, at pH 7.5 and 37°C
0.0174
-
with caffeoyl aldehyde as substrate, at pH 7.5 and 37°C
0.0174
-
with caffeoyl aldehyde as substrate, at pH 7.5 and 37°C
additional information
T-DNA null mutant indicates collapsed xylem elements under short-day conditions, lignin composition of p-hydroxyphenyl units and inability of sinapoyl malate synthesis in double mutants impaired in caffeoyl CoA 3-O-methyltransferase (CCoAOMT 1) and caffeic acid O-methyltransferase (COMT 1), C3 methylation of the phenolic ring of monolignols in Arabidopsis mediated by both, caffeoyl CoA 3-O-methyltransferase (CCoAOMT 1) and caffeic acid O-methyltransferase (COMT 1), both enzymes also involved in formation of sinapoyl malate and isorhamnetin
additional information
-
T-DNA null mutant indicates collapsed xylem elements under short-day conditions, lignin composition of p-hydroxyphenyl units and inability of sinapoyl malate synthesis in double mutants impaired in caffeoyl CoA 3-O-methyltransferase (CCoAOMT 1) and caffeic acid O-methyltransferase (COMT 1), C3 methylation of the phenolic ring of monolignols in Arabidopsis mediated by both, caffeoyl CoA 3-O-methyltransferase (CCoAOMT 1) and caffeic acid O-methyltransferase (COMT 1), both enzymes also involved in formation of sinapoyl malate and isorhamnetin
additional information
determination of lignin content in transgenic plants, overview
additional information
-
determination of lignin content in transgenic plants, overview
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Marita, J.M.; Ralph, J.; Hatfield, R.D.; Guo, D.; Chen, F.; Dixon, R.A.
Structural and compositional modifications in lignin of transgenic alfalfa down-regulated in caffeic acid 3-O-methyltransferase and caffeoyl coenzyme A 3-O-methyltransferase
Phytochemistry
62
53-65
2003
Medicago sativa
brenda
Day, A.; Dehorter, B.; Neutelings, G.; Czeszak, X.; Chabbert, B.; Belingheri, L.; David, H.
Caffeoyl-coenzyme A 3-O-methyltransferase enzyme activity, protein and transcript accumulation in flax (Linum usitatissimum) stem during development
Physiol. Plant.
113
275-284
2001
Linum usitatissimum
brenda
Hoffmann, L.; Maury, S.; Bergdoll, M.; Thion, L.; Erard, M.; Legrand, M.
Identification of the enzymatic active site of tobacco caffeoyl-coenzyme A O-methyltransferase by site-directed mutagenesis
J. Biol. Chem.
276
36831-36838
2001
Nicotiana tabacum
brenda
Parvathi, K.; Chen, F.; Guo, D.; Blount, J.W.; Dixon, R.A.
Substrate preferences of O-methyltransferases in alfalfa suggest new pathways for 3-O-methylation of monolignols
Plant J.
25
193-202
2001
Medicago sativa
brenda
Zhong, R.; Morrison, W.H.; Himmelsbach, D.S.; Poole, F.L.; Ye, Z.H.
Essential role of caffeoyl coenzyme A O-methyltransferase in lignin biosynthesis in woody poplar plants
Plant Physiol.
124
563-578
2000
Populus tremula x Populus alba (Q43095)
brenda
Chen, C.; Meyermans, H.; Burggraeve, B.; De Rycke, R.M.; Inoue, K.; De Vleesschauwer, V.; Steenackers, M.; Van Montagu, M.C.; Engler, G.J.; Boerjan, W.A.
Cell-specific and conditional expression of caffeoyl-coenzyme A-3-O-methyltransferase in poplar
Plant Physiol.
123
853-867
2000
Populus tremula x Populus alba, Populus trichocarpa
brenda
Maury, S.; Geoffroy, P.; Legrand, M.
Tobacco O-methyltransferases involved in phenylpropanoid metabolism. The different caffeoyl-coenzyme A/5-hydroxyferuloyl-coenzyme A 3/5-O-methyltransferase and caffeic acid/5-hydroxyferulic acid 3/5-O-methyltransferase classes have distinct substrate specificities and expression patterns
Plant Physiol.
121
215-224
1999
Nicotiana tabacum
brenda
Grimmig, B.; Kneusel, R.E.; Junghanns, K.T.; Matern, U.
Expression of bifunctional caffeoyl-CoA 3-O-methyltransferase in stress compensation and lignification
Plant Biol.
1
299-310
1999
Nicotiana tabacum, Petroselinum crispum
-
brenda
Martz, F.; Maury, S.; Pincon, G.; Legrand, M.
cDNA cloning, substrate specificity and expression study of tobacco caffeoyl-CoA 3-O-methyltransferase, a lignin biosynthetic enzyme
Plant Mol. Biol.
36
427-437
1998
Nicotiana tabacum
brenda
Meng, H.; Campbell, W.H.
Substrate profiles and expression of caffeoyl coenzyme A and caffeic acid O-methyltransferases in secondary xylem of aspen during seasonal development
Plant Mol. Biol.
38
513-520
1998
Populus tremuloides
brenda
Inoue, K.; Sewalt, V.J.H.; Ballance, G.M.; Ni, W.; Sturzer, C.; Dixon, R.A.
Developmental expression and substrate specificities of alfalfa caffeic acid 3-O-methyltransferase and caffeoyl coenzyme A 3-O-methyltransferase in relation to lignification
Plant Physiol.
117
761-770
1998
Medicago sativa (Q40313), Medicago sativa
brenda
Busam, G.; Junghanns, K.T.; Kneusel, R.E.; Kassemeyer, H.H.; Matern, U.
Characterization and expression of caffeoyl-coenzyme A 3-O-methyltransferase proposed for the induced resistance response of Vitis vinifera L
Plant Physiol.
115
1039-1048
1997
Vitis vinifera
brenda
Ni, W.; Sewalt, V.J.H.; Korth, K.L.; Blount, J.W.; Ballance, G.M.; Dixon, R.A.
Stress responses in alfalfa. XXI. Activation of caffeic acid 3-O-methyltransferase and caffeoyl coenzyme A 3-O-methyltransferase genes does not contribute to changes in metabolite accumulation in elicitor-treated cell-suspension cultures
Plant Physiol.
112
717-726
1996
Medicago sativa
brenda
Pakusch, A.E.; Matern, U.; Schiltz, E.
Elicitor-inducible caffeoyl-coenzyme A 3-O-methyltransferase from Petroselinum crispum cell suspensions
Plant Physiol.
95
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