EC 2.1.1.20 - Glycine N-methyltransferase

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IntEnz Enzyme Nomenclature
EC 2.1.1.20

Names

Accepted name:
glycine N-methyltransferase
Other names:
S-adenosyl-L-methionine:glycine methyltransferase
GNMT
glycine methyltransferase
Systematic name:
S-adenosyl-L-methionine:glycine N-methyltransferase

Reaction

Comments:

This enzyme is thought to play an important role in the regulation of methyl group metabolism in the liver and pancreas by regulating the ratio between S-adenosyl-L-methionine and S-adenosyl-L-homocysteine. It is inhibited by 5-methyltetrahydrofolate pentaglutamate [4]. Sarcosine, which has no physiological role, is converted back into glycine by the action of EC 1.5.8.3, sarcosine dehydrogenase.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0017174
CAS Registry Number: 37228-72-1
UniProtKB/Swiss-Prot: (409) [show] [UniProt]

References

  1. Blumenstein, J. and Williams, G.R.
    Glycine methyltransferase.
    Can. J. Biochem. Physiol. 41: 201-210 (1963). [PMID: 13971907]
  2. Ogawa, H., Gomi, T., Takusagawa, F. and Fujioka, M.
    Structure, function and physiological role of glycine N-methyltransferase.
    Int. J. Biochem. Cell Biol. 30: 13-26 (1998). [PMID: 9597750]
  3. Yeo, E.-J., Briggs, W.T. and Wagner, C.
    Inhibition of glycine N-methyltransferase by 5-methyltetrahydrofolate pentaglutamate.
    J. Biol. Chem. 274: 37559-37564 (2000). [PMID: 10608809]
  4. Martinov, M.V., Vitvitsky, V.M., Mosharov, E.V., Banerjee, R. and Ataullakhanov, F.I.
    A substrate switch: a new mode of regulation in the methionine metabolic pathway.
    J. Theor. Biol. 204: 521-532 (2000). [PMID: 10833353]
  5. Takata, Y., Huang, Y., Komoto, J., Yamada, T., Konishi, K., Ogawa, H., Gomi, T., Fujioka, M. and Takusagawa, F.
    Catalytic mechanism of glycine N-methyltransferase.
    Biochemistry 42: 8394-8402 (2003). [PMID: 12859184]
  6. Pakhomova, S., Luka, Z., Grohmann, S., Wagner, C. and Newcomer, M.E.
    Glycine N-methyltransferases: a comparison of the crystal structures and kinetic properties of recombinant human, mouse and rat enzymes.
    Proteins 57: 331-337 (2004). [PMID: 15340920]

[EC 2.1.1.20 created 1972, modified 2005]