Any feedback?
Information on EC 2.1.1.175 - tricin synthase
for references in articles please use BRENDA:EC2.1.1.175Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.1.1.175 tricin synthaseIUBMB Comments
The enzymes from Oryza sativa (ROMT-15 and ROMT-17) catalyses the stepwise methylation of tricetin to its 3'-mono- and 3',5'-dimethyl ethers. In contrast with the wheat enzyme (EC 2.1.1.169, tricetin 3',4',5'-O-trimethyltransferase), tricetin dimethyl ether is not converted to its 3',4',5'-trimethylated ether derivative . The enzymes from Hordeum vulgare (HvOMT1) and from Zea mays (ZmOMT1) form the 3',5'-dimethyl derivative as the major product .
Specify your search results
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
romt-15, romt9, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 S-adenosyl-L-methionine + tricetin = 2 S-adenosyl-L-homocysteine + 3',5'-O-dimethyltricetin
-
-
-
-
S-adenosyl-L-methionine + 3'-O-methyltricetin = S-adenosyl-L-homocysteine + 3',5'-O-dimethyltricetin
-
-
-
-
S-adenosyl-L-methionine + tricetin = S-adenosyl-L-homocysteine + 3'-O-methyltricetin
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:tricetin 3',5'-O-dimethyltransferase
The enzymes from Oryza sativa (ROMT-15 and ROMT-17) catalyses the stepwise methylation of tricetin to its 3'-mono- and 3',5'-dimethyl ethers. In contrast with the wheat enzyme (EC 2.1.1.169, tricetin 3',4',5'-O-trimethyltransferase), tricetin dimethyl ether is not converted to its 3',4',5'-trimethylated ether derivative [1]. The enzymes from Hordeum vulgare (HvOMT1) and from Zea mays (ZmOMT1) form the 3',5'-dimethyl derivative as the major product [2].
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 S-adenosyl-L-methionine + tricetin
2 S-adenosyl-L-homocysteine + 3',5'-O-dimethyltricetin
S-adenosyl-L-methionine + 3'-O-methyltricetin
S-adenosyl-L-homocysteine + 3',5'-O-dimethyltricetin
S-adenosyl-L-methionine + selgin
S-adenosyl-L-homocysteine + tricin
-
-
-
-
?
S-adenosyl-L-methionine + tricetin
S-adenosyl-L-homocysteine + selgin
-
-
-
-
?
2 S-adenosyl-L-methionine + tricetin
2 S-adenosyl-L-homocysteine + 3',5'-O-dimethyltricetin
-
stepwise methylation of tricetin to its 3'-mono- and 3',5'-dimethyl ethers (major product). The enzyme also catalyzes the 3'-O-methylation of luteolin (EC 2.1.1.42) and the methylation of 5-hydroxyferulic acid and quercetin, prefers tricetin over luteolin
-
-
?
2 S-adenosyl-L-methionine + tricetin
2 S-adenosyl-L-homocysteine + 3',5'-O-dimethyltricetin
the enzyme catalyzes the stepwise methylation of tricetin to its 3'-mono- and 3',5'-dimethyl ethers. In contrast with the wheat enzyme, tricetin dimethyl ether is not converted to its 3',4',5'-trimethylated ester derivatives. The enzyme also catalyzes the methylation of luteolin, myricetin (formation of the 3',5'-dimethyl ether of myricetin, EC 2.1.1.149) and caffeoyl-CoA. ROMT-15 exhibits similar Kcat/Km values for the four substrates. ROMT-15 can not utilize naringenin, apigenin, or kaempferol. The 2,3-double bond and the O-dihydroxyl group are both required for catalytic activity
-
-
?
2 S-adenosyl-L-methionine + tricetin
2 S-adenosyl-L-homocysteine + 3',5'-O-dimethyltricetin
the enzyme catalyzes the stepwise methylation of tricetin to its 3'-mono- and 3',5'-dimethyl ethers. In contrast with the wheat enzyme, tricetin dimethyl ether is not converted to its 3',4',5'-trimethylated ester derivatives. The enzyme also catalyzes the methylation of luteolin, myricetin (formation of the 3',5'-dimethyl ether of myricetin, EC 2.1.1.149) and caffeoyl-CoA. ROMT-17 prefers tricetin. ROMT-15 can not utilize naringenin, apigenin, or kaempferol. The 2,3-double bond and the O-dihydroxyl group are both required for catalytic activity
-
-
?
2 S-adenosyl-L-methionine + tricetin
2 S-adenosyl-L-homocysteine + 3',5'-O-dimethyltricetin
-
the enzyme also catalyzes the 3'-O-methylation of luteolin (EC 2.1.1.42) and the methylation of 5-hydroxyferulic acid and quercetin, prefers tricetin over luteolin
-
-
?
S-adenosyl-L-methionine + 3'-O-methyltricetin
S-adenosyl-L-homocysteine + 3',5'-O-dimethyltricetin
-
the enzyme catalyzes the stepwise methylation of tricetin to its 3'-mono- and 3',5'-dimethyl ethers (major product). In contrast with the wheat enzyme, tricetin dimethyl ether is not converted to its 3',4',5'-trimethylated ester derivatives
-
-
?
S-adenosyl-L-methionine + 3'-O-methyltricetin
S-adenosyl-L-homocysteine + 3',5'-O-dimethyltricetin
the enzyme catalyzes the stepwise methylation of tricetin to its 3'-mono- and 3',5'-dimethyl ethers. In contrast with the wheat enzyme, tricetin dimethyl ether is not converted to its 3',4',5'-trimethylated ester derivatives
-
-
?
S-adenosyl-L-methionine + 3'-O-methyltricetin
S-adenosyl-L-homocysteine + 3',5'-O-dimethyltricetin
-
the enzyme catalyzes the stepwise methylation of tricetin to its 3'-mono- and 3',5'-dimethyl ethers (major product). In contrast with the wheat enzyme, tricetin dimethyl ether is not converted to its 3',4',5'-trimethylated ester derivatives
-
-
?
S-adenosyl-L-methionine + tricetin
S-adenosyl-L-homocysteine + 3'-O-methyltricetin
-
the enzyme catalyzes the stepwise methylation of tricetin to its 3'-mono- and 3',5'-dimethyl ethers (major product). In contrast with the wheat enzyme, tricetin dimethyl ether is not converted to its 3',4',5'-trimethylated ester derivatives
-
-
?
S-adenosyl-L-methionine + tricetin
S-adenosyl-L-homocysteine + 3'-O-methyltricetin
the enzyme catalyzes the stepwise methylation of tricetin to its 3'-mono- and 3',5'-dimethyl ethers. In contrast with the wheat enzyme, tricetin dimethyl ether is not converted to its 3',4',5'-trimethylated ester derivatives
-
-
?
S-adenosyl-L-methionine + tricetin
S-adenosyl-L-homocysteine + 3'-O-methyltricetin
-
the enzyme catalyzes the stepwise methylation of tricetin to its 3'-mono- and 3',5'-dimethyl ethers (major product). In contrast with the wheat enzyme, tricetin dimethyl ether is not converted to its 3',4',5'-trimethylated ester derivatives
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + selgin
S-adenosyl-L-homocysteine + tricin
-
-
-
-
?
S-adenosyl-L-methionine + tricetin
S-adenosyl-L-homocysteine + selgin
-
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Mg2+
the enzyme is metal-dependent, Mg2+ is the best cation for catalytic activity (with quercetin as substrate)
Mn2+
additional information
Co2+
the enzyme is metal-dependent, Mg2+ is the best cation for catalytic activity, Co2+ shows 41% of the activity with Mg2+ (with quercetin as substrate)
Co2+
the enzyme is metal-dependent, Mg2+ is the best cation for catalytic activity, Co2+ shows 82% of the activity with Mg2+ (with quercetin as substrate)
Mn2+
the enzyme is metal-dependent, Mg2+ is the best cation for catalytic activity, Mn2+ shows 69% of the activity with Mg2+ (with quercetin as substrate)
Mn2+
the enzyme is metal-dependent, Mg2+ is the best cation for catalytic activity, Mn2+ shows 74% of the activity with Mg2+ (with quercetin as substrate)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
-
Oryza sativa variety Njavara contains a high content of tricin
brenda
additional information
-
Oryza sativa variety Njavara contains a high content of tricin
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
Oryza sativa variety Njavara contains a high content of tricin, it is used as therpeutic in ajurvedal medical treatment, overview. Tricin mediated reduction of LPS induced COX-2 activity and PGE2 production, inhibits LPS-induced TNF-alpha and IL-6 production, and attenuates LPS induced production of matrix metalloproteinases by hPBMCs. Tricin is highly inhibitory for inflammatory enzymes, overview
additional information
-
Oryza sativa variety Njavara contains a high content of tricin, it is used as therpeutic in ajurvedal medical treatment, overview. Tricin mediated reduction of LPS induced COX-2 activity and PGE2 production, inhibits LPS-induced TNF-alpha and IL-6 production, and attenuates LPS induced production of matrix metalloproteinases by hPBMCs. Tricin is highly inhibitory for inflammatory enzymes, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). OMT15_ORYSJ
252
0
27772
Swiss-Prot
other Location (Reliability: 1)
OMT17_ORYSJ
292
0
32032
Swiss-Prot
Mitochondrion (Reliability: 2)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E112L
mutation results in 40% loss of activity (with quercetin as substrate)
E69L
mutation results in 14% loss of activity (with quercetin as substrate)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, stable when stored in buffer containing 10% (v/v) glycerol for 3-4 weeks
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli as glutathione S-transferase fusion protein
expression in Escherichia coli
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lee, Y.; Kim, B.; Chong, Y.; Lim, Y.; Ahn, J.
Cation dependent O-methyltransferases from rice
Planta
227
641-647
2008
Oryza sativa, Oryza sativa (Q9XGP7)
brenda
Zhou, J.-M.; Fukushi, Y.; Wollenweber, E.; Ibrahim, R.K.
Characterization of two O-methyltransferase-like genes in barley and maize
Pharm. Biol.
46
26-34
2008
Hordeum vulgare, Zea mays
-
brenda
Shalini, V.; Bhaskar, S.; Kumar, K.S.; Mohanlal, S.; Jayalekshmy, A.; Helen, A.
Molecular mechanisms of anti-inflammatory action of the flavonoid, tricin from Njavara rice (Oryza sativa L.) in human peripheral blood mononuclear cells: possible role in the inflammatory signaling
Int. Immunopharmacol.
14
32-38
2012
Oryza sativa, Oryza sativa njavara
brenda
Lam, P.Y.; Liu, H.; Lo, C.
Completion of tricin biosynthesis pathway in rice: cytochrome P450 75B4 is a unique chrysoeriol 5'-hydroxylase
Plant Physiol.
168
1527-1536
2015
Oryza sativa Japonica Group
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 2.1.1.175)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
