glycine N-methyltransferase
Identifiers
EC no.	2.1.1.20
CAS no.	37228-72-1
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / QuickGO
Search PMC articles PubMed articles NCBI proteins

In enzymology, a glycine N-methyltransferase (EC 2.1.1.20) is an enzyme that catalyzes the chemical reaction

S-adenosyl-L-methionine + glycine ${\displaystyle \rightleftharpoons }$ S-adenosyl-L-homocysteine + sarcosine

Thus, the substrates of this enzyme are S-adenosyl methionine and glycine, whereas its two products are S-adenosylhomocysteine and sarcosine.

Glycine N-methyltransferase belongs to the family of methyltransferase enzymes. The systematic name of this enzyme class is S-adenosyl-L-methionine:glycine N-methyltransferase. Other names in common use include glycine methyltransferase, S-adenosyl-L-methionine:glycine methyltransferase, and GNMT. This family of enzymes participates in the metabolism of multiple amino acids.

• J. Blumenstein; G. R. Williams (1963). "Glycine methyltransferase". Can. J. Biochem. Physiol. 41: 201–10. doi:10.1139/o63-025. PMID 13971907.
• Ogawa H, Gomi T, Takusagawa F, Fujioka M (1998). "Structure, function and physiological role of glycine N-methyltransferase". Int. J. Biochem. Cell Biol. 30 (1): 13–26. doi:10.1016/S1357-2725(97)00105-2. PMID 9597750.
• Yeo EJ, Briggs WT, Wagner C (1999). "Inhibition of glycine N-methyltransferase by 5-methyltetrahydrofolate pentaglutamate". J. Biol. Chem. 274 (53): 37559–64. doi:10.1074/jbc.274.53.37559. PMID 10608809.
• FI; Vitvitsky, VM; Mosharov, EV; Banerjee, R; Ataullakhanov, FI (2000). "A substrate switch: a new mode of regulation in the methionine metabolic pathway". J. Theor. Biol. 204 (4): 521–32. Bibcode:2000JThBi.204..521M. doi:10.1006/jtbi.2000.2035. PMID 10833353.
• Fujioka M, Takusagawa F (2003). "Catalytic mechanism of glycine N-methyltransferase". Biochemistry. 42 (28): 8394–402. doi:10.1021/bi034245a. PMID 12859184.
• Pakhomova S, Luka Z, Grohmann S, Wagner C, Newcomer ME (2004). "Glycine N-methyltransferases: a comparison of the crystal structures and kinetic properties of recombinant human, mouse and rat enzymes". Proteins. 57 (2): 331–7. doi:10.1002/prot.20209. PMID 15340920. S2CID 26065465.