Guanidinoacetate N-methyltransferase

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In enzymology, a guanidinoacetate N-methyltransferase (EC 2.1.1.2) is an enzyme that catalyzes the chemical reaction

S-adenosyl-L-methionine + guanidinoacetate $\rightleftharpoons$ S-adenosyl-L-homocysteine + creatine

Thus, the two substrates of this enzyme are S-adenosyl methionine and guanidinoacetate, whereas its two products are S-adenosylhomocysteine and creatine.

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:N-guanidinoacetate methyltransferase. Other names in common use include GA methylpherase, guanidinoacetate methyltransferase, guanidinoacetate transmethylase, methionine-guanidinoacetic transmethylase, and guanidoacetate methyltransferase. This enzyme participates in glycine, serine and threonine metabolism and arginine and proline metabolism.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes 1KHH, 1P1B, 1P1C, 1XCJ, 1XCL, 1ZX0, and 2BLN.

[edit] References

IUBMB entry for 2.1.1.2
BRENDA references for 2.1.1.2 (Recommended.)
PubMed references for 2.1.1.2
PubMed Central references for 2.1.1.2
Google Scholar references for 2.1.1.2
Cantoni GL and Scarano E (1954). "The formation of S-adenosylhomocysteine in enzymatic transmethylation reactions". J. Am. Chem. Soc. 76: 4744.
CANTONI GL, VIGNOS PJ Jr (1954). "Enzymatic mechanism of creatine synthesis". J. Biol. Chem. 209: 647–59. PMID 13192118.