BRENDA - Enzyme Database show
show all sequences of 2.1.1.270

Blount, J.W.; Huhman, D.; Dixon, R.A.; Noel, J.P.: Structural basis for dual functionality of isoflavonoid O-methyltransferases in the evolution of plant defense responses

Liu, C.J.; Deavours, B.E.; Richard, S.B.; Ferrer, J.L.; Plant Cell 18, 3656-3669 (2006)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli
Medicago truncatula
Crystallization (Commentary)
Crystallization
Organism
crystallized from a polyethylene glycol precipitant containing 2.5 mM of the reaction product S-adenosyl-L-homocysteine, 2.5 A resolution
Medicago truncatula
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.062
-
(+)-6a-hydroxymaackiain
pH 8.0, 30°C
Medicago truncatula
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
S-adenosyl-L-methionine + (+)-6a-hydroxymaackiain
Medicago truncatula
-
S-adenosyl-L-homocysteine + (+)-pisatin
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Medicago truncatula
Q29U70
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
S-adenosyl-L-methionine + (+)-6a-hydroxymaackiain
-
713268
Medicago truncatula
S-adenosyl-L-homocysteine + (+)-pisatin
-
-
-
?
S-adenosyl-L-methionine + (+)-6a-hydroxymaackiain
the bifunctional enzyme also catalyzes the 4'-O-methylation of 2,7,4'-trihydroxyisoflavanonewith slightly higher catalytic efficiency
713268
Medicago truncatula
S-adenosyl-L-homocysteine + (+)-pisatin
-
-
-
?
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Medicago truncatula
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Medicago truncatula
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Medicago truncatula
Crystallization (Commentary) (protein specific)
Crystallization
Organism
crystallized from a polyethylene glycol precipitant containing 2.5 mM of the reaction product S-adenosyl-L-homocysteine, 2.5 A resolution
Medicago truncatula
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.062
-
(+)-6a-hydroxymaackiain
pH 8.0, 30°C
Medicago truncatula
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
S-adenosyl-L-methionine + (+)-6a-hydroxymaackiain
Medicago truncatula
-
S-adenosyl-L-homocysteine + (+)-pisatin
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
S-adenosyl-L-methionine + (+)-6a-hydroxymaackiain
-
713268
Medicago truncatula
S-adenosyl-L-homocysteine + (+)-pisatin
-
-
-
?
S-adenosyl-L-methionine + (+)-6a-hydroxymaackiain
the bifunctional enzyme also catalyzes the 4'-O-methylation of 2,7,4'-trihydroxyisoflavanonewith slightly higher catalytic efficiency
713268
Medicago truncatula
S-adenosyl-L-homocysteine + (+)-pisatin
-
-
-
?
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Medicago truncatula
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Medicago truncatula
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
197
-
(+)-6a-hydroxymaackiain
pH 8.0, 30°C
Medicago truncatula
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
197
-
(+)-6a-hydroxymaackiain
pH 8.0, 30°C
Medicago truncatula
Other publictions for EC 2.1.1.270
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
711599
Fondevilla
Identification of genes differ ...
Pisum sativum, Pisum sativum P665
BMC Genomics
12
28
2011
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-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
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-
-
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-
-
-
-
-
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-
-
-
-
1
-
-
1
-
-
706124
Kaimoyo
Inactivation of pea genes by R ...
Pisum sativum
Phytochemistry
69
76-87
2008
-
-
1
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
1
-
-
3
-
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-
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-
-
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-
1
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-
1
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-
1
-
-
3
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
676377
Akashi
Catalytic specificity of pea O ...
Pisum sativum
Phytochemistry
67
2525-2530
2006
-
-
1
1
-
-
-
2
-
-
-
1
-
5
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-
-
-
-
-
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-
3
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1
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1
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2
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1
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-
-
-
-
3
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-
-
-
-
-
-
-
-
-
-
-
-
-
713268
Liu
Blount, J.W.; Huhman, D.; Dixo ...
Medicago truncatula
Plant Cell
18
3656-3669
2006
-
-
1
1
-
-
-
1
-
-
-
1
-
1
-
-
-
-
-
-
-
-
2
-
1
-
-
-
1
-
-
-
-
-
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-
1
-
1
-
-
-
-
-
1
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-
-
1
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-
-
-
-
-
-
-
2
-
1
-
-
-
1
-
-
-
-
-
-
-
1
1
441447
He
Stress responses in alfalfa (M ...
Medicago sativa
Plant Mol. Biol.
36
43-54
1998
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-
1
-
-
-
-
-
-
-
1
1
-
1
-
-
1
-
-
-
-
-
3
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
1
-
-
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-
3
1
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-
1
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1
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