Glycine N-methyltransferase

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glycine N-methyltransferase
2azt.jpg
Identifiers
EC number2.1.1.20
CAS number37228-72-1
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

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[edit]

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[edit]

  • BLUMENSTEIN J, WILLIAMS GR (1963). "Glycine methyltransferase". Can. J. Biochem. Physiol. 41: 201&ndash, 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&ndash, 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&ndash, 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&ndash, 32. doi:10.1006/jtbi.2000.2035. PMID 10833353.
  • Fujioka M, Takusagawa F (2003). "Catalytic mechanism of glycine N-methyltransferase". Biochemistry. 42 (28): 8394&ndash, 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&ndash, 7. doi:10.1002/prot.20209. PMID 15340920.