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Literature summary for 2.1.1.20 extracted from
- Phosphorylation modulates the activity of glycine N-methyltransferase, a folate binding protein. In vitro phosphorylation is inhibited by the natural folate ligand (1989), J. Biol. Chem., 264, 9638-9642.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| phosphate | in vitro phosphorylation increases activity, about 0.55 mol of phosphate present per mol of N-methyltransferase subunit | Rattus norvegicus |  |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| 5-Methyltetrahydropteroylpentaglutamate | - |
Rattus norvegicus | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| cytosol | - |
Rattus norvegicus | 5829 | - |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Rattus norvegicus | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| liver | - |
Rattus norvegicus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| S-adenosyl-L-methionine + glycine | strict specificity for glycine as methyl acceptor | Rattus norvegicus | S-adenosyl-L-homocysteine + sarcosine | - |
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