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.
The expected taxonomic range for this enzyme is: Saccharomyces cerevisiae
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.
Substrates: 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 Products: -
Substrates: 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 Products: -
Substrates: 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 Products: -
methylation of trehalose-6-phosphate synthase results in enhanced activity and subsequently increased trehalose production in the cell as it enters the stationary phase
Purification, characterization, sequencing and molecular cloning of a novel cysteine methyltransferase that regulates trehalose-6-phosphate synthase from Saccharomyces cerevisiae
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