BRENDA - Enzyme Database
show all sequences of 2.1.1.274

Novel S-adenosyl-L-methionine:salicylic acid carboxyl methyltransferase, an enzyme responsible for biosynthesis of methyl salicylate and methyl benzoate, is not involved in floral scent production in snapdragon flowers

Negre, F.; Kolosova, N.; Knoll, J.; Kish, C.M.; Dudareva, N.; Arch. Biochem. Biophys. 406, 261-270 (2002)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
subcloned into expression vector pET-28a, containing an N-terminal polyhistidine 6-His-tag, and expressed in Escherichia coli
Antirrhinum majus
General Stability
General Stability
Organism
the enzyme is active in both Tris- and phosphate–citrate-based buffers, although its activity in phosphate-citrate buffer is about 20% lower than in Tris-buffer
Antirrhinum majus
Inhibitors
Inhibitors
Commentary
Organism
Structure
Cu2+
5 mM, strong inhibitory effect with more than 95% inhibition
Antirrhinum majus
Fe2+
5 mM, strong inhibitory effect with more than 95% inhibition
Antirrhinum majus
Mn2+
5 mM, inhibits SAMT activity less than 30%
Antirrhinum majus
additional information
presence of 5 mM Mg2+ in the assay reaction and addition of K+, NH4+ and Ca2+ does not affect SAMT activity
Antirrhinum majus
Na+
5 mM, inhibits SAMT activity less than 30%
Antirrhinum majus
Zn2+
5 mM, inhibits SAMT activity less than 30%
Antirrhinum majus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.004
-
S-adenosyl-L-methionine
with salicylic acid, pH 7.5, 20°C
Antirrhinum majus
0.083
-
salicylic acid
pH 7.5, 20°C
Antirrhinum majus
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
49000
-
SDS-PAGE
Antirrhinum majus
107000
-
with a calibrated Sephacryl 200-HR column
Antirrhinum majus
Organism
Organism
UniProt
Commentary
Textmining
Antirrhinum majus
Q8H6N2
snapdragon
-
Purification (Commentary)
Purification (Commentary)
Organism
by nickel-based affinity chromatography
Antirrhinum majus
Source Tissue
Source Tissue
Commentary
Organism
Textmining
petal
200fold higher levels of SAMT mRNA than in the pistil, where lowest level of mRNA expression is observed
Antirrhinum majus
-
sepal
Expression of SAMT mRNA about half the level in petal, where lowest level of mRNA expression is observed
Antirrhinum majus
-
stamen
expression of SAMT only 2fold higher than in pistil, where lowest level of mRNA expression is observed
Antirrhinum majus
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.000126
-
salicylic acid, pH 7.5, 20°C
Antirrhinum majus
Storage Stability
Storage Stability
Organism
the recombinant protein is catalytically stable for more than a year when stored at -80°C
Antirrhinum majus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
additional information
enzyme is also active with benzoic acid resulting in methyl benzoate formation
721415
Antirrhinum majus
?
-
-
-
?
additional information
no activity with 3-hydroxybenzoic acid, 4-hydroxybenzoic acid, trans-cinnamic acid, p-coumaric acid, m-coumaric acid, o-coumaric acid and benzyl alcohol
721415
Antirrhinum majus
?
-
-
-
?
S-adenosyl-L-methionine + salicylic acid
-
721415
Antirrhinum majus
S-adenosyl-L-homocysteine + methyl salicylate
-
-
-
?
Subunits
Subunits
Commentary
Organism
homodimer
2 * 49000, SDS-PAGE
Antirrhinum majus
Synonyms
Synonyms
Commentary
Organism
salicylic acid carboxyl methyltransferase
-
Antirrhinum majus
SAMT
-
Antirrhinum majus
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
42
-
enzyme is stable at temperatures up to 42°C for 30 min but 30-min incubation at 65°C leads to a 70% loss of activity
Antirrhinum majus
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.011
-
salicylic acid
pH 7.5, 20°C
Antirrhinum majus
0.013
-
S-adenosyl-L-methionine
with salicylic acid, pH 7.5, 20°C
Antirrhinum majus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
-
Antirrhinum majus
pH Range
pH Minimum
pH Maximum
Commentary
Organism
additional information
-
at pH 4.0 and 9.5 the enzyme activity falls to about 20% of the maximal activity
Antirrhinum majus
5
8
with 80–90% of maximum activity
Antirrhinum majus
Cloned(Commentary) (protein specific)
Commentary
Organism
subcloned into expression vector pET-28a, containing an N-terminal polyhistidine 6-His-tag, and expressed in Escherichia coli
Antirrhinum majus
General Stability (protein specific)
General Stability
Organism
the enzyme is active in both Tris- and phosphate–citrate-based buffers, although its activity in phosphate-citrate buffer is about 20% lower than in Tris-buffer
Antirrhinum majus
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Cu2+
5 mM, strong inhibitory effect with more than 95% inhibition
Antirrhinum majus
Fe2+
5 mM, strong inhibitory effect with more than 95% inhibition
Antirrhinum majus
Mn2+
5 mM, inhibits SAMT activity less than 30%
Antirrhinum majus
additional information
presence of 5 mM Mg2+ in the assay reaction and addition of K+, NH4+ and Ca2+ does not affect SAMT activity
Antirrhinum majus
Na+
5 mM, inhibits SAMT activity less than 30%
Antirrhinum majus
Zn2+
5 mM, inhibits SAMT activity less than 30%
Antirrhinum majus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.004
-
S-adenosyl-L-methionine
with salicylic acid, pH 7.5, 20°C
Antirrhinum majus
0.083
-
salicylic acid
pH 7.5, 20°C
Antirrhinum majus
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
49000
-
SDS-PAGE
Antirrhinum majus
107000
-
with a calibrated Sephacryl 200-HR column
Antirrhinum majus
Purification (Commentary) (protein specific)
Commentary
Organism
by nickel-based affinity chromatography
Antirrhinum majus
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
petal
200fold higher levels of SAMT mRNA than in the pistil, where lowest level of mRNA expression is observed
Antirrhinum majus
-
sepal
Expression of SAMT mRNA about half the level in petal, where lowest level of mRNA expression is observed
Antirrhinum majus
-
stamen
expression of SAMT only 2fold higher than in pistil, where lowest level of mRNA expression is observed
Antirrhinum majus
-
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.000126
-
salicylic acid, pH 7.5, 20°C
Antirrhinum majus
Storage Stability (protein specific)
Storage Stability
Organism
the recombinant protein is catalytically stable for more than a year when stored at -80°C
Antirrhinum majus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
additional information
enzyme is also active with benzoic acid resulting in methyl benzoate formation
721415
Antirrhinum majus
?
-
-
-
?
additional information
no activity with 3-hydroxybenzoic acid, 4-hydroxybenzoic acid, trans-cinnamic acid, p-coumaric acid, m-coumaric acid, o-coumaric acid and benzyl alcohol
721415
Antirrhinum majus
?
-
-
-
?
S-adenosyl-L-methionine + salicylic acid
-
721415
Antirrhinum majus
S-adenosyl-L-homocysteine + methyl salicylate
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
homodimer
2 * 49000, SDS-PAGE
Antirrhinum majus
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
42
-
enzyme is stable at temperatures up to 42°C for 30 min but 30-min incubation at 65°C leads to a 70% loss of activity
Antirrhinum majus
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.011
-
salicylic acid
pH 7.5, 20°C
Antirrhinum majus
0.013
-
S-adenosyl-L-methionine
with salicylic acid, pH 7.5, 20°C
Antirrhinum majus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
-
Antirrhinum majus
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
additional information
-
at pH 4.0 and 9.5 the enzyme activity falls to about 20% of the maximal activity
Antirrhinum majus
5
8
with 80–90% of maximum activity
Antirrhinum majus
Other publictions for EC 2.1.1.274
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
Synonyms
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)
736189
Wang
Cloning and characterization o ...
Lilium hybrid cultivar
Genet. Mol. Res.
14
14510-14521
2015
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2
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736696
Krol
Priming of seeds with methyl j ...
Solanum lycopersicum
J. Plant Physiol.
179
122-132
2015
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1
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1
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1
1
1
1
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736842
Ludwig-Mueller
A novel methyltransferase from ...
Plasmodiophora brassicae
Mol. Plant Pathol.
16
349-364
2015
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1
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1
1
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736841
Zhu
Salicylic acid and jasmonic ac ...
Nicotiana benthamiana
Mol. Plant Microbe Interact.
27
567-577
2014
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1
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1
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6
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1
1
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726129
Lin
Overexpression of a soybean sa ...
Glycine max
Plant Biotechnol. J.
11
1135-1145
2013
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1
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6
1
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2
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5
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5
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1
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1
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1
1
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1
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1
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725781
Yao
QM/MM free energy simulations ...
Clarkia breweri
J. Phys. Chem. B
115
389-396
2011
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726013
Liu
Altering expression of benzoic ...
Arabidopsis thaliana
Mol. Plant Microbe Interact.
23
82-90
2010
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2
2
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726172
Tieman
Functional analysis of a tomat ...
Solanum lycopersicum
Plant J.
62
113-123
2010
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1
1
1
1
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726132
Kwon
-
Biotic and abiotic stresses in ...
Atropa belladonna
Plant Biotechnol.
26
207-215
2009
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723402
Zubieta
Structural basis for substrate ...
Clarkia breweri
Plant Cell
15
1704-1716
2003
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5
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723416
Chen
An Arabidopsis thaliana gene f ...
Arabidopsis lyrata, Arabidopsis thaliana
Plant J.
36
577-588
2003
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721415
Negre
Novel S-adenosyl-L-methionine: ...
Antirrhinum majus
Arch. Biochem. Biophys.
406
261-270
2002
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1
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6
2
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721412
Ross
S-Adenosyl-L-methionine:salicy ...
Clarkia breweri
Arch. Biochem. Biophys.
367
9-16
1999
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