Information on EC 2.1.1.175 - tricin synthase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.1.1.175
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RECOMMENDED NAME
GeneOntology No.
tricin synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 S-adenosyl-L-methionine + tricetin = 2 S-adenosyl-L-homocysteine + 3',5'-O-dimethyltricetin
show the reaction diagram
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S-adenosyl-L-methionine + 3'-O-methyltricetin = S-adenosyl-L-homocysteine + 3',5'-O-dimethyltricetin
show the reaction diagram
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S-adenosyl-L-methionine + tricetin = S-adenosyl-L-homocysteine + 3'-O-methyltricetin
show the reaction diagram
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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].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
cultivar Zhonghua 11
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 S-adenosyl-L-methionine + tricetin
2 S-adenosyl-L-homocysteine + 3',5'-O-dimethyltricetin
show the reaction diagram
S-adenosyl-L-methionine + 3'-O-methyltricetin
S-adenosyl-L-homocysteine + 3',5'-O-dimethyltricetin
show the reaction diagram
S-adenosyl-L-methionine + selgin
S-adenosyl-L-homocysteine + tricin
show the reaction diagram
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-
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-
?
S-adenosyl-L-methionine + tricetin
S-adenosyl-L-homocysteine + 3'-O-methyltricetin
show the reaction diagram
S-adenosyl-L-methionine + tricetin
S-adenosyl-L-homocysteine + selgin
show the reaction diagram
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-
-
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + selgin
S-adenosyl-L-homocysteine + tricin
show the reaction diagram
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-
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?
S-adenosyl-L-methionine + tricetin
S-adenosyl-L-homocysteine + selgin
show the reaction diagram
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-
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
;
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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); 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)
Mg2+
the enzyme is metal-dependent, Mg2+ is the best cation for catalytic activity (with quercetin as substrate); the enzyme is metal-dependent, Mg2+ is the best cation for catalytic activity (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); 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)
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00248 - 0.072
tricetin
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.949 - 2.83
tricetin
2788
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at; assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.48
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calculated from sequence
5.64
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calculated from sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
; expressed in stems only
Manually annotated by BRENDA team
additional information
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, stable when stored in buffer containing 10% (v/v) glycerol for 3-4 weeks
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4C, stable when stored in buffer containing 10% (v/v) glycerol for 34 weeks
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli as glutathione S-transferase fusion protein; expressed in Escherichia coli as glutathione S-transferase fusion protein
expressed in Escherichia coli strain BL21
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expression in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D168L
mutation abolishes activity (with quercetin as substrate)
D194L
mutation abolishes activity (with quercetin as substrate)
D209L
mutation abolishes activity (with quercetin as substrate)
D234L
mutation abolishes activity (with quercetin as substrate)
E112L
mutation results in 40% loss of activity (with quercetin as substrate)
E69L
mutation results in 14% loss of activity (with quercetin as substrate)
N195I
mutation abolishes activity (with quercetin as substrate)
N235I
mutation abolishes activity (with quercetin as substrate)