The enzyme tartronate-semialdehyde synthase (EC 4.1.1.47) catalyzes the chemical reaction
2 glyoxylate ⇌ {\displaystyle \rightleftharpoons } tartronate semialdehyde + CO2 This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is glyoxylate carboxy-lyase (dimerizing tartronate-semialdehyde-forming). Other names in common use include tartronate semialdehyde carboxylase, glyoxylate carbo-ligase, glyoxylic carbo-ligase, hydroxymalonic semialdehyde carboxylase, tartronic semialdehyde carboxylase, glyoxalate carboligase, and glyoxylate carboxy-lyase (dimerizing). This enzyme participates in glyoxylate and dicarboxylate metabolism. It has 2 cofactors: FAD, and Thiamin diphosphate.
References
GUPTA NK, VENNESLAND B (1964). "Glyoxylate Carboligase of Escherichia Coli: A Flavoprotein". J. Biol. Chem. 239 (11): 3787–9. doi:10.1016/S0021-9258(18)91205-6. PMID 14257608. BARKULIS SS, KRAKOW G (1956). "Conversion of glyoxylate to hydroxypyruvate by extracts of Escherichia coli". Biochim. Biophys. Acta. 21 (3): 593–4. doi:10.1016/0006-3002(56)90208-6. PMID 13363977.


