Information on EC 2.1.1.318 - [trehalose-6-phosphate synthase]-L-cysteine S-methyltransferase

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The expected taxonomic range for this enzyme is: Saccharomyces cerevisiae

EC NUMBER
COMMENTARY hide
2.1.1.318
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RECOMMENDED NAME
GeneOntology No.
[trehalose-6-phosphate synthase]-L-cysteine S-methyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + [trehalose-6-phosphate synthase]-L-cysteine = S-adenosyl-L-homocysteine + [trehalose-6-phosphate synthase]-S-methyl-L-cysteine
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:[trehalose-6-phosphate synthase]-L-cysteine S-methyltransferase
The enzyme, characterized from the yeast Saccharomyces cerevisiae, enhances the activity of EC 2.4.1.15, trehalose-6-phosphate synthase, resulting in elevating the levels of trehalose in the cell and contributing to stationary phase survival. In vitro the enzyme performs S-methylation of L-cysteine residues of various protein substrates.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
SUBSTRATE
PRODUCT                       
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 + [albumin]-L-cysteine
S-adenosyl-L-homocysteine + [albumin]-S-methyl-L-cysteine
show the reaction diagram
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
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?
S-adenosyl-L-methionine + [chymotrypsin]-L-cysteine
S-adenosyl-L-homocysteine + [chymotrypsin]-S-methyl-L-cysteine
show the reaction diagram
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-
-
?
S-adenosyl-L-methionine + [lipase]-L-cysteine
S-adenosyl-L-homocysteine + [lipase]-S-methyl-L-cysteine
show the reaction diagram
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-
-
?
S-adenosyl-L-methionine + [ovalbumin]-L-cysteine
S-adenosyl-L-homocysteine + [ovalbumin]-S-methyl-L-cysteine
show the reaction diagram
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-
-
?
S-adenosyl-L-methionine + [peroxidase]-L-cysteine
S-adenosyl-L-homocysteine + [peroxidase]-S-methyl-L-cysteine
show the reaction diagram
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-
-
?
S-adenosyl-L-methionine + [ribonuclease A]-L-cysteine
S-adenosyl-L-homocysteine + [ribonuclease A]-S-methyl-L-cysteine
show the reaction diagram
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-
-
?
S-adenosyl-L-methionine + [trehalose-6-phosphate synthase]-L-cysteine
S-adenosyl-L-homocysteine + [trehalose-6-phosphate synthase]-S-methyl-L-cysteine
show the reaction diagram
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 + [trehalose-6-phosphate synthase]-L-cysteine
S-adenosyl-L-homocysteine + [trehalose-6-phosphate synthase]-S-methyl-L-cysteine
show the reaction diagram
I6WHP7
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
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ZnCl2
5 mM, enhances activity 1.4fold
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Citric acid
2.5 mM, 25% inhibition
S-adenosyl-L-homocysteine
competitive
Sodium azide
2.5 mM; 40% inhibition
sulfosalicylic acid
2.5 mM, 35% inhibition
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
2.5 mM, 1.3fold activation
EGTA
2.5 mM, 1.3fold activation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00495
S-adenosyl-L-methionine
37°C, pH not specified in the publication, native and cloned enzyme
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6.4 - 7
S-adenosyl-L-methionine
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0109
S-adenosyl-L-homocysteine
37°C, pH not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.82
calculated from sequence
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
14000
non-denaturing PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 14000, SDS-PAGE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli