Alanine—glyoxylate transaminase

In enzymology, an alanine-glyoxylate transaminase (EC 2.6.1.44) is an enzyme that catalyzes the chemical reaction

L-alanine + glyoxylate pyruvate + glycine

Thus, the two substrates of this enzyme are L-alanine and glyoxylate, whereas its two products are pyruvate and glycine.

This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-alanine:glyoxylate aminotransferase. Other names in common use include AGT, alanine-glyoxylate aminotransferase, alanine-glyoxylic aminotransferase, and L-alanine-glycine transaminase. This enzyme participates in alanine and aspartate metabolism and glycine, serine and threonine metabolism. It employs one cofactor, pyridoxal phosphate.

Structural studies

As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes 1H0C, 1J04, 1VJO, 2BKW, 2HUF, 2HUI, and 2HUU.

References

• Noguchi T, Okuno E, Takada Y, Minatogawa Y, Okai K, Kido R (1978). "Characteristics of hepatic alanine-glyoxylate aminotransferase in different mammalian species". Biochem. J. 169 (1): 113–22. PMC 1184200. PMID 629740. 
• Okuno E, Minatogawa Y, Kido R (1982). "Co-purification of alanine-glyoxylate aminotransferase with 2-aminobutyrate aminotransferase in rat kidney". Biochim. Biophys. Acta 715 (1): 97–104. doi:10.1016/0304-4165(82)90054-x. PMID 6803844. 
• Thompson JS, Richardson KE (1967). "Isolation and characterization of an L-alanine: glyoxylate aminotransferase from human liver". J. Biol. Chem. 242 (16): 3614–9. PMID 6038488.