Glycine N-methyltransferase
| Glycine N-methyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 | |||||||||
| Identifiers | |||||||||
| EC no. | 2.1.1.20 | ||||||||
| CAS no. | 37228-72-1 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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Glycine N-methyltransferase (EC 2.1.1.20) is an enzyme that catalyzes the chemical reaction
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The enzyme catalyses a methylation reaction in which the amino acid glycine is converted to sarcosine. The methyl group comes from the cofactor, S-adenosyl methionine (SAM), which loses its methyl group and becomes S-adenosyl-L-homocysteine (SAH).[1][2][3]
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.[4] It regulates methyl group metabolism in the liver and pancreas by alterating the ratio between SAM and SAH. It is inhibited by 5-methyltetrahydrofolate pentaglutamate.[5][6] The product, sarcosine is converted back into glycine by the enzyme sarcosine dehydrogenase.
Structural studies
The crystal structure of three variants of the mammalian enzyme have been compared.[7]
References
- ↑ 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.
- ↑ Fujioka M, Takusagawa F (2003). "Catalytic mechanism of glycine N-methyltransferase". Biochemistry. 42 (28): 8394–402. doi:10.1021/bi034245a. PMID 12859184.
- ↑ Enzyme 2.1.1.20 at KEGG Pathway Database.
- ↑ 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.
- ↑ 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.
- ↑ 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.
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