Guanidinoacetate N-methyltransferase

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

S-adenosyl-L-methionine + guanidinoacetate <math>\rightleftharpoons</math> 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.

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.

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.