| EC |
2.1.1.318 |
| Accepted name: |
[trehalose-6-phosphate synthase]-L-cysteine S-methyltransferase |
| Reaction: |
S-adenosyl-L-methionine + [trehalose-6-phosphate synthase]-L-cysteine = S-adenosyl-L-homocysteine + [trehalose-6-phosphate synthase]-S-methyl-L-cysteine
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| Systematic name: |
S-adenosyl-L-methionine:[trehalose-6-phosphate synthase]-L-cysteine S-methyltransferase |
| Comments: |
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. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
| References: |
| 1. |
Sengupta, S., Banerjee, S., Lahiri, S., Dutta, T., Dhar, T.K. and Ghosh, A.K. Purification, characterization, sequencing and molecular cloning of a novel cysteine methyltransferase that regulates trehalose-6-phosphate synthase from Saccharomyces cerevisiae. Biochim. Biophys. Acta 1840 (2014) 1861–1871. [DOI] [PMID: 24412193] |
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| [EC 2.1.1.318 created 2015] |
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