Literature summary extracted from

Wagner, C.; Decha-Umphai, W.; Corbin, J.
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

EC Number	Activating Compound	Comment	Organism	Structure
2.1.1.20	phosphate	in vitro phosphorylation increases activity, about 0.55 mol of phosphate present per mol of N-methyltransferase subunit	Rattus norvegicus

Inhibitors

EC Number	Inhibitors	Comment	Organism	Structure
2.1.1.20	5-Methyltetrahydropteroylpentaglutamate	-	Rattus norvegicus

Localization

EC Number	Localization	Comment	Organism	GeneOntology No.	Textmining
2.1.1.20	cytosol	-	Rattus norvegicus	5829	-

Organism

EC Number	Organism	UniProt	Comment	Textmining
2.1.1.20	Rattus norvegicus	-	-	-

Source Tissue

EC Number	Source Tissue	Comment	Organism	Textmining
2.1.1.20	liver	-	Rattus norvegicus	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2.1.1.20	S-adenosyl-L-methionine + glycine	strict specificity for glycine as methyl acceptor	Rattus norvegicus	S-adenosyl-L-homocysteine + sarcosine	-	?

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Release 2023.1 (January 2023)