Glycine N-methyltransferase
| glycine N-methyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
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| Identifiers | |||||||||
| EC number | 2.1.1.20 | ||||||||
| CAS number | 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 / EGO | ||||||||
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In enzymology, a glycine N-methyltransferase (EC 2.1.1.20) is an enzyme that catalyzes the chemical reaction
- S-adenosyl-L-methionine + glycine S-adenosyl-L-homocysteine + sarcosine
Thus, the two substrates of this enzyme are S-adenosyl methionine and glycine, whereas its two products are S-adenosylhomocysteine and sarcosine.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. 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 enzyme participates in glycine, serine and threonine metabolism.
Structural studies
As of late 2007, 12 structures have been solved for this class of enzymes, with PDB accession codes 1BHJ, 1D2C, 1D2G, 1D2H, 1KIA, 1NBH, 1NBI, 1R74, 1XVA, 2AZT, 2IDJ, and 2IDK.
References
- BLUMENSTEIN J, WILLIAMS GR (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. 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.