Biology:Glycine N-methyltransferase
From HandWiki
| 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 / QuickGO | ||||||||
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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 [math]\displaystyle{ \rightleftharpoons }[/math] 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.
References
- J. Blumenstein; G. R. Williams (1963). "Glycine methyltransferase". Can. J. Biochem. Physiol. 41: 201–10. doi:10.1139/o63-025. PMID 13971907.
- "Structure, function and physiological role of glycine N-methyltransferase". Int. J. Biochem. Cell Biol. 30 (1): 13–26. 1998. doi:10.1016/S1357-2725(97)00105-2. PMID 9597750.
- "Inhibition of glycine N-methyltransferase by 5-methyltetrahydrofolate pentaglutamate". J. Biol. Chem. 274 (53): 37559–64. 1999. 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. Bibcode: 2000JThBi.204..521M.
- "Catalytic mechanism of glycine N-methyltransferase". Biochemistry 42 (28): 8394–402. 2003. doi:10.1021/bi034245a. PMID 12859184.
- "Glycine N-methyltransferases: a comparison of the crystal structures and kinetic properties of recombinant human, mouse and rat enzymes". Proteins 57 (2): 331–7. 2004. doi:10.1002/prot.20209. PMID 15340920. https://digitalcommons.lsu.edu/biosci_pubs/2721.
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