Serine—glyoxylate transaminase explained

serine-glyoxylate transaminase
Ec Number:	2.6.1.45
Cas Number:	37259-57-7
Go Code:	0050281

In enzymology, a serine-glyoxylate transaminase is an enzyme that catalyzes the chemical reaction

L-serine + glyoxylate

\rightleftharpoons 3-hydroxypyruvate + glycine

Thus, the two substrates of this enzyme are L-serine and glyoxylate, whereas its two products are 3-hydroxypyruvate 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-serine:glyoxylate aminotransferase. This enzyme participates in glycine, serine and threonine metabolism. It employs one cofactor, pyridoxal phosphate.

References

• Ireland RJ, Joy KW . 1983 . Purification and properties of an asparagine aminotransferase from Pisum sativum leaves . Arch. Biochem. Biophys. . 223 . 291 - 6 . 6407397 . 10.1016/0003-9861(83)90594-5 . 1 .
• King J, Waygood ER . 1968 . Glyoxylate aminotranferases from wheat leaves . Can. J. Biochem. . 46 . 771 - 9 . 5672858 . 10.1139/v68-127 . 8 .
• Smith IK . 1973 . Purification and characterization of serine:glyoxylate aminotransferase from kidney bean (Phaseolus vulgaris) . Biochim. Biophys. Acta . 321 . 156 - 64 . 4750762 . 1 . 10.1016/0005-2744(73)90069-7.