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glyoxylate carboligase
glyoxylate carboligase catalyzes the condensation of two molecules of glyoxylate to form tartronate semialdehyde and carbon dioxide; the reaction requires two cofactors, FAD and thiamine diphosphate
thiamine pyrophosphate-dependent enzyme
thiamine pyrophosphate-binding protein
Thiamine pyrophosphate enzyme, central domain
The central domain of TPP enzymes contains a 2-fold Rossman fold. [1]. 8604141. Crystal structure of the thiamin diphosphate-dependent enzyme pyruvate decarboxylase from the yeast Saccharomyces cerevisiae at 2.3 A resolution. Arjunan P, Umland T, Dyda F, Swaminathan S, Furey W, Sax M, Farrenkopf B, Gao Y, Zhang D, Jordan F;. J Mol Biol 1996;256:590-600. (from Pfam)
Glyoxylate carboligase, also called tartronate-semialdehyde synthase, releases CO2 while synthesizing a single molecule of tartronate semialdehyde from two molecules of glyoxylate. It is a thiamine pyrophosphate-dependent enzyme, closely related in sequence to the large subunit of acetolactate synthase. In the D-glycerate pathway, part of allantoin degradation in the Enterobacteriaceae, tartronate semialdehyde is converted to D-glycerate and then 3-phosphoglycerate, a product of glycolysis and entry point in the general metabolism.
Catalyzes the formation of 2-hydroxy-3-oxopropanoate (tartronate semialdehyde) from two molecules of glyoxylate
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