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Information on EC 2.1.1.175 - tricin synthase
for references in articles please use BRENDA:EC2.1.1.175
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EC Tree 2 Transferases
2.1 Transferring one-carbon groups
2.1.1 Methyltransferases
2.1.1.175 tricin synthase
IUBMB 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 .
The enzyme appears in viruses and cellular organisms
Reaction Schemes
showSynonyms
romt-15, romt9, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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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
-
-
-
-
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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].
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
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
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + tricetin
S-adenosyl-L-homocysteine + selgin
-
Substrates: -
Products: -
Products: -
?
2 S-adenosyl-L-methionine + tricetin
2 S-adenosyl-L-homocysteine + 3',5'-O-dimethyltricetin
-
Substrates: 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
Products: -
Products: -
?
2 S-adenosyl-L-methionine + tricetin
2 S-adenosyl-L-homocysteine + 3',5'-O-dimethyltricetin
Substrates: 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
Products: -
Products: -
?
2 S-adenosyl-L-methionine + tricetin
2 S-adenosyl-L-homocysteine + 3',5'-O-dimethyltricetin
Substrates: 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
Products: -
Products: -
?
2 S-adenosyl-L-methionine + tricetin
2 S-adenosyl-L-homocysteine + 3',5'-O-dimethyltricetin
-
Substrates: 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
Products: -
Products: -
?
S-adenosyl-L-methionine + 3'-O-methyltricetin
S-adenosyl-L-homocysteine + 3',5'-O-dimethyltricetin
-
Substrates: 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
Products: -
Products: -
?
S-adenosyl-L-methionine + 3'-O-methyltricetin
S-adenosyl-L-homocysteine + 3',5'-O-dimethyltricetin
Substrates: 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
Products: -
Products: -
?
S-adenosyl-L-methionine + 3'-O-methyltricetin
S-adenosyl-L-homocysteine + 3',5'-O-dimethyltricetin
-
Substrates: 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
Products: -
Products: -
?
S-adenosyl-L-methionine + tricetin
S-adenosyl-L-homocysteine + 3'-O-methyltricetin
-
Substrates: 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
Products: -
Products: -
?
S-adenosyl-L-methionine + tricetin
S-adenosyl-L-homocysteine + 3'-O-methyltricetin
Substrates: 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
Products: -
Products: -
?
S-adenosyl-L-methionine + tricetin
S-adenosyl-L-homocysteine + 3'-O-methyltricetin
-
Substrates: 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
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + selgin
S-adenosyl-L-homocysteine + tricin
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + tricetin
S-adenosyl-L-homocysteine + selgin
-
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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)
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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
Highest Expressing Human Cell Lines
Cell Line LinksPlease 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
-
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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). OMT17_ORYSJ
292
0
32032
Swiss-Prot
Secretory Pathway (Reliability: 5)
OMT15_ORYSJ
252
0
27772
Swiss-Prot
other Location (Reliability: 2)
A0A0E0A5J2_9ORYZ
260
0
28848
TrEMBL
other Location (Reliability: 4)
A0A0E0AX48_9ORYZ
443
0
48299
TrEMBL
other Location (Reliability: 3)
A0A0E0AX52_9ORYZ
260
0
28418
TrEMBL
other Location (Reliability: 5)
A0A0E0HLM3_ORYNI
303
0
33860
TrEMBL
other Location (Reliability: 1)
A0A0E0IDT5_ORYNI
292
0
31911
TrEMBL
Secretory Pathway (Reliability: 5)
A0A0E0IDT4_ORYNI
290
0
31828
TrEMBL
Secretory Pathway (Reliability: 3)
A0A0E0PTZ4_ORYRU
304
0
34044
TrEMBL
Secretory Pathway (Reliability: 1)
A0A3B6SI45_WHEAT
302
0
33140
TrEMBL
Chloroplast (Reliability: 5)
A0A453QTP6_AEGTS
260
0
28865
TrEMBL
-
A0A453RI94_AEGTS
247
0
27075
TrEMBL
-
A0A6G1C7C7_9ORYZ
252
0
27880
TrEMBL
other Location (Reliability: 3)
A0A6G1C8C1_9ORYZ
253
0
27723
TrEMBL
-
A0A6G1CN54_9ORYZ
303
0
33629
TrEMBL
-
A0A9R0W507_TRITD
296
0
32863
TrEMBL
other Location (Reliability: 2)
A0A9R0Z9D4_TRITD
245
0
26869
TrEMBL
-
A0A9R0ZS57_TRITD
267
0
29511
TrEMBL
-
A0A9R1A0H5_TRITD
302
0
33140
TrEMBL
-
A0A9R1K9U9_WHEAT
246
0
27051
TrEMBL
other Location (Reliability: 1)
A0A9R1M2Z4_WHEAT
267
0
29507
TrEMBL
other Location (Reliability: 2)
A0A9R1N547_WHEAT
302
0
33140
TrEMBL
other Location (Reliability: 2)
A2YWN1_ORYSI
252
0
27772
TrEMBL
other Location (Reliability: 2)
I1QJU5_ORYGL
292
0
31911
TrEMBL
Mitochondrion (Reliability: 5)
J3MBL0_ORYBR
257
0
28614
TrEMBL
Secretory Pathway (Reliability: 2)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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)
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, stable when stored in buffer containing 10% (v/v) glycerol for 3-4 weeks
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli as glutathione S-transferase fusion protein
expression in Escherichia coli
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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
EXTERNAL LINKS (specific for EC-Number 2.1.1.175)
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