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Literature summary extracted from

  • Sengupta, S.; Banerjee, S.; Lahiri, S.; Dutta, T.; Dhar, T.K.; Ghosh, A.K.
    Purification, characterization, sequencing and molecular cloning of a novel cysteine methyltransferase that regulates trehalose-6-phosphate synthase from Saccharomyces cerevisiae (2014), Biochim. Biophys. Acta, 1840, 1861-1871.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.1.1.318 EDTA 2.5 mM, 1.3fold activation Saccharomyces cerevisiae
2.1.1.318 EGTA 2.5 mM, 1.3fold activation Saccharomyces cerevisiae
2.4.1.15 additional information the trehalose-6-phosphate synthase of Saccharomyces cerevisiae shows 1.76fold enhanced activity after specific methylation at a cysteine residue through 14 kDa cysteine methyltransferase from Saccharomyces cerevisiae Saccharomyces cerevisiae

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.1.318 expression in Escherichia coli Saccharomyces cerevisiae

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.1.1.318 Citric acid 2.5 mM, 25% inhibition Saccharomyces cerevisiae
2.1.1.318 S-adenosyl-L-homocysteine competitive Saccharomyces cerevisiae
2.1.1.318 Sodium azide 2.5 mM; 40% inhibition Saccharomyces cerevisiae
2.1.1.318 sulfosalicylic acid 2.5 mM, 35% inhibition Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1.1.318 0.00495
-
 S-adenosyl-L-methionine 37°C, pH not specified in the publication, native and cloned enzyme Saccharomyces cerevisiae

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.1.1.318 ZnCl2 5 mM, enhances activity 1.4fold Saccharomyces cerevisiae

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.1.1.318 14000
-
 non-denaturing PAGE Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.1.318 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

EC Number Organism UniProt Comment Textmining
2.1.1.318 Saccharomyces cerevisiae I6WHP7
-
-
2.4.1.15 Saccharomyces cerevisiae Q00764
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.4.1.15 side-chain modification the trehalose-6-phosphate synthase of Saccharomyces cerevisiae shows 1.76fold enhanced activity after specific methylation at a cysteine residue through 14 kDa cysteine methyltransferase from Saccharomyces cerevisiae Saccharomyces cerevisiae

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.1.318
-
 Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.318 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 Saccharomyces cerevisiae S-adenosyl-L-homocysteine + [albumin]-S-methyl-L-cysteine
-
 ?
2.1.1.318 S-adenosyl-L-methionine + [chymotrypsin]-L-cysteine
-
 Saccharomyces cerevisiae S-adenosyl-L-homocysteine + [chymotrypsin]-S-methyl-L-cysteine
-
 ?
2.1.1.318 S-adenosyl-L-methionine + [lipase]-L-cysteine
-
 Saccharomyces cerevisiae S-adenosyl-L-homocysteine + [lipase]-S-methyl-L-cysteine
-
 ?
2.1.1.318 S-adenosyl-L-methionine + [ovalbumin]-L-cysteine
-
 Saccharomyces cerevisiae S-adenosyl-L-homocysteine + [ovalbumin]-S-methyl-L-cysteine
-
 ?
2.1.1.318 S-adenosyl-L-methionine + [peroxidase]-L-cysteine
-
 Saccharomyces cerevisiae S-adenosyl-L-homocysteine + [peroxidase]-S-methyl-L-cysteine
-
 ?
2.1.1.318 S-adenosyl-L-methionine + [ribonuclease A]-L-cysteine
-
 Saccharomyces cerevisiae S-adenosyl-L-homocysteine + [ribonuclease A]-S-methyl-L-cysteine
-
 ?
2.1.1.318 S-adenosyl-L-methionine + [trehalose-6-phosphate synthase]-L-cysteine
-
 Saccharomyces cerevisiae S-adenosyl-L-homocysteine + [trehalose-6-phosphate synthase]-S-methyl-L-cysteine
-
 ?
2.1.1.318 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 Saccharomyces cerevisiae S-adenosyl-L-homocysteine + [trehalose-6-phosphate synthase]-S-methyl-L-cysteine
-
 ?

Subunits

EC Number Subunits Comment Organism
2.1.1.318 monomer 1 * 14000, SDS-PAGE Saccharomyces cerevisiae

Synonyms

EC Number Synonyms Comment Organism
2.4.1.15 trehalose-6-phosphate synthase
-
 Saccharomyces cerevisiae

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.1.1.318 30
-
-
 Saccharomyces cerevisiae
2.4.1.15 37
-
 assay at Saccharomyces cerevisiae

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.1.1.318 6.4
-
 S-adenosyl-L-methionine 37°C, pH not specified in the publication, native enzyme Saccharomyces cerevisiae
2.1.1.318 7
-
 S-adenosyl-L-methionine 37°C, pH not specified in the publication, cloned enzyme Saccharomyces cerevisiae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.1.1.318 7
-
-
 Saccharomyces cerevisiae

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.1.1.318 0.0109
-
 S-adenosyl-L-homocysteine 37°C, pH not specified in the publication Saccharomyces cerevisiae

pI Value

EC Number Organism Comment pI Value Maximum pI Value
2.1.1.318 Saccharomyces cerevisiae calculated from sequence
-
 6.82

General Information

EC Number General Information Comment Organism
2.1.1.318 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
2.1.1.318 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