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show all sequences of 2.1.1.318

Purification, characterization, sequencing and molecular cloning of a novel cysteine methyltransferase that regulates trehalose-6-phosphate synthase from Saccharomyces cerevisiae

Sengupta, S.; Banerjee, S.; Lahiri, S.; Dutta, T.; Dhar, T.K.; Ghosh, A.K.; Biochim. Biophys. Acta 1840, 1861-1871 (2014)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
EDTA
2.5 mM, 1.3fold activation
Saccharomyces cerevisiae
EGTA
2.5 mM, 1.3fold activation
Saccharomyces cerevisiae
Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli
Saccharomyces cerevisiae
Inhibitors
Inhibitors
Commentary
Organism
Structure
Citric acid
2.5 mM, 25% inhibition
Saccharomyces cerevisiae
S-adenosyl-L-homocysteine
competitive
Saccharomyces cerevisiae
Sodium azide
2.5 mM; 40% inhibition
Saccharomyces cerevisiae
sulfosalicylic acid
2.5 mM, 35% inhibition
Saccharomyces cerevisiae
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.00495
-
S-adenosyl-L-methionine
37°C, pH not specified in the publication, native and cloned enzyme
Saccharomyces cerevisiae
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
ZnCl2
5 mM, enhances activity 1.4fold
Saccharomyces cerevisiae
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
14000
-
non-denaturing PAGE
Saccharomyces cerevisiae
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
S-adenosyl-L-methionine + [trehalose-6-phosphate synthase]-L-cysteine
Saccharomyces cerevisiae
the enzyme performs S-methylation at cysteine residue regulating trehalose-6-phosphate synthase activity by 50%, which results in an increase of the intercellular stress sugar, trehalose. It contributes to stationary phase survival of Saccharomyces cerevisiae by elevating the levels of trehalose in the cell as it enters the stationary phase
S-adenosyl-L-homocysteine + [trehalose-6-phosphate synthase]-S-methyl-L-cysteine
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Saccharomyces cerevisiae
I6WHP7
-
-
Purification (Commentary)
Commentary
Organism
-
Saccharomyces cerevisiae
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
S-adenosyl-L-methionine + [albumin]-L-cysteine
in vitro, the activity of the purified enzyme predominantly corresponds with the cysteine content of the substrates and is not specific for trehalose-6-phosphate synthase
729302
Saccharomyces cerevisiae
S-adenosyl-L-homocysteine + [albumin]-S-methyl-L-cysteine
-
-
-
?
S-adenosyl-L-methionine + [chymotrypsin]-L-cysteine
-
729302
Saccharomyces cerevisiae
S-adenosyl-L-homocysteine + [chymotrypsin]-S-methyl-L-cysteine
-
-
-
?
S-adenosyl-L-methionine + [lipase]-L-cysteine
-
729302
Saccharomyces cerevisiae
S-adenosyl-L-homocysteine + [lipase]-S-methyl-L-cysteine
-
-
-
?
S-adenosyl-L-methionine + [ovalbumin]-L-cysteine
-
729302
Saccharomyces cerevisiae
S-adenosyl-L-homocysteine + [ovalbumin]-S-methyl-L-cysteine
-
-
-
?
S-adenosyl-L-methionine + [peroxidase]-L-cysteine
-
729302
Saccharomyces cerevisiae
S-adenosyl-L-homocysteine + [peroxidase]-S-methyl-L-cysteine
-
-
-
?
S-adenosyl-L-methionine + [ribonuclease A]-L-cysteine
-
729302
Saccharomyces cerevisiae
S-adenosyl-L-homocysteine + [ribonuclease A]-S-methyl-L-cysteine
-
-
-
?
S-adenosyl-L-methionine + [trehalose-6-phosphate synthase]-L-cysteine
-
729302
Saccharomyces cerevisiae
S-adenosyl-L-homocysteine + [trehalose-6-phosphate synthase]-S-methyl-L-cysteine
-
-
-
?
S-adenosyl-L-methionine + [trehalose-6-phosphate synthase]-L-cysteine
the enzyme performs S-methylation at cysteine residue regulating trehalose-6-phosphate synthase activity by 50%, which results in an increase of the intercellular stress sugar, trehalose. It contributes to stationary phase survival of Saccharomyces cerevisiae by elevating the levels of trehalose in the cell as it enters the stationary phase
729302
Saccharomyces cerevisiae
S-adenosyl-L-homocysteine + [trehalose-6-phosphate synthase]-S-methyl-L-cysteine
-
-
-
?
Subunits
Subunits
Commentary
Organism
monomer
1 * 14000, SDS-PAGE
Saccharomyces cerevisiae
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
-
Saccharomyces cerevisiae
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
6.4
-
S-adenosyl-L-methionine
37°C, pH not specified in the publication, native enzyme
Saccharomyces cerevisiae
7
-
S-adenosyl-L-methionine
37°C, pH not specified in the publication, cloned enzyme
Saccharomyces cerevisiae
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
-
Saccharomyces cerevisiae
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.0109
-
S-adenosyl-L-homocysteine
37°C, pH not specified in the publication
Saccharomyces cerevisiae
pI Value
Organism
Commentary
pI Value Maximum
pI Value
Saccharomyces cerevisiae
calculated from sequence
-
6.82
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
EDTA
2.5 mM, 1.3fold activation
Saccharomyces cerevisiae
EGTA
2.5 mM, 1.3fold activation
Saccharomyces cerevisiae
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Saccharomyces cerevisiae
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Citric acid
2.5 mM, 25% inhibition
Saccharomyces cerevisiae
S-adenosyl-L-homocysteine
competitive
Saccharomyces cerevisiae
Sodium azide
2.5 mM; 40% inhibition
Saccharomyces cerevisiae
sulfosalicylic acid
2.5 mM, 35% inhibition
Saccharomyces cerevisiae
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.0109
-
S-adenosyl-L-homocysteine
37°C, pH not specified in the publication
Saccharomyces cerevisiae
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.00495
-
S-adenosyl-L-methionine
37°C, pH not specified in the publication, native and cloned enzyme
Saccharomyces cerevisiae
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
ZnCl2
5 mM, enhances activity 1.4fold
Saccharomyces cerevisiae
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
14000
-
non-denaturing PAGE
Saccharomyces cerevisiae
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 + [trehalose-6-phosphate synthase]-L-cysteine
Saccharomyces cerevisiae
the enzyme performs S-methylation at cysteine residue regulating trehalose-6-phosphate synthase activity by 50%, which results in an increase of the intercellular stress sugar, trehalose. It contributes to stationary phase survival of Saccharomyces cerevisiae by elevating the levels of trehalose in the cell as it enters the stationary phase
S-adenosyl-L-homocysteine + [trehalose-6-phosphate synthase]-S-methyl-L-cysteine
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
-
Saccharomyces cerevisiae
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
S-adenosyl-L-methionine + [albumin]-L-cysteine
in vitro, the activity of the purified enzyme predominantly corresponds with the cysteine content of the substrates and is not specific for trehalose-6-phosphate synthase
729302
Saccharomyces cerevisiae
S-adenosyl-L-homocysteine + [albumin]-S-methyl-L-cysteine
-
-
-
?
S-adenosyl-L-methionine + [chymotrypsin]-L-cysteine
-
729302
Saccharomyces cerevisiae
S-adenosyl-L-homocysteine + [chymotrypsin]-S-methyl-L-cysteine
-
-
-
?
S-adenosyl-L-methionine + [lipase]-L-cysteine
-
729302
Saccharomyces cerevisiae
S-adenosyl-L-homocysteine + [lipase]-S-methyl-L-cysteine
-
-
-
?
S-adenosyl-L-methionine + [ovalbumin]-L-cysteine
-
729302
Saccharomyces cerevisiae
S-adenosyl-L-homocysteine + [ovalbumin]-S-methyl-L-cysteine
-
-
-
?
S-adenosyl-L-methionine + [peroxidase]-L-cysteine
-
729302
Saccharomyces cerevisiae
S-adenosyl-L-homocysteine + [peroxidase]-S-methyl-L-cysteine
-
-
-
?
S-adenosyl-L-methionine + [ribonuclease A]-L-cysteine
-
729302
Saccharomyces cerevisiae
S-adenosyl-L-homocysteine + [ribonuclease A]-S-methyl-L-cysteine
-
-
-
?
S-adenosyl-L-methionine + [trehalose-6-phosphate synthase]-L-cysteine
-
729302
Saccharomyces cerevisiae
S-adenosyl-L-homocysteine + [trehalose-6-phosphate synthase]-S-methyl-L-cysteine
-
-
-
?
S-adenosyl-L-methionine + [trehalose-6-phosphate synthase]-L-cysteine
the enzyme performs S-methylation at cysteine residue regulating trehalose-6-phosphate synthase activity by 50%, which results in an increase of the intercellular stress sugar, trehalose. It contributes to stationary phase survival of Saccharomyces cerevisiae by elevating the levels of trehalose in the cell as it enters the stationary phase
729302
Saccharomyces cerevisiae
S-adenosyl-L-homocysteine + [trehalose-6-phosphate synthase]-S-methyl-L-cysteine
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
monomer
1 * 14000, SDS-PAGE
Saccharomyces cerevisiae
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
-
Saccharomyces cerevisiae
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
6.4
-
S-adenosyl-L-methionine
37°C, pH not specified in the publication, native enzyme
Saccharomyces cerevisiae
7
-
S-adenosyl-L-methionine
37°C, pH not specified in the publication, cloned enzyme
Saccharomyces cerevisiae
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
-
Saccharomyces cerevisiae
pI Value (protein specific)
Organism
Commentary
pI Value Maximum
pI Value
Saccharomyces cerevisiae
calculated from sequence
-
6.82
General Information
General Information
Commentary
Organism
malfunction
trehalose concentration is 0.93 mM/mg wet weight in the wild type strain as compared to 0.51 mMl/mg wetweight in the knock out mutant strains
Saccharomyces cerevisiae
physiological function
methylation of trehalose-6-phosphate synthase results in enhanced activity and subsequently increased trehalose production in the cell as it enters the stationary phase
Saccharomyces cerevisiae
General Information (protein specific)
General Information
Commentary
Organism
malfunction
trehalose concentration is 0.93 mM/mg wet weight in the wild type strain as compared to 0.51 mMl/mg wetweight in the knock out mutant strains
Saccharomyces cerevisiae
physiological function
methylation of trehalose-6-phosphate synthase results in enhanced activity and subsequently increased trehalose production in the cell as it enters the stationary phase
Saccharomyces cerevisiae
Other publictions for EC 2.1.1.318
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)
729302
Sengupta
Purification, characterization ...
Saccharomyces cerevisiae
Biochim. Biophys. Acta
1840
1861-1871
2014
2
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4
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