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1-deoxy-D-xylulose-5-phosphate synthase N-terminal domain-containing protein
This family contains 1-deoxyxylulose-5-phosphate synthase (DXP synthase), an enzyme which catalyses the thiamine pyrophosphoate-dependent acyloin condensation reaction between carbon atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate, to yield 1-deoxy-D- xylulose-5-phosphate, a precursor in the biosynthetic pathway to isoprenoids, thiamine (vitamin B1), and pyridoxol (vitamin B6). [1]. 9371765. Identification of a thiamin-dependent synthase in Escherichia coli required for the formation of the 1-deoxy-D-xylulose 5-phosphate precursor to isoprenoids, thiamin, and pyridoxol. Sprenger GA, Schorken U, Wiegert T, Grolle S, de Graaf AA, Taylor SV, Begley TP, Bringer-Meyer S, Sahm H;. Proc Natl Acad Sci U S A. 1997;94:12857-12862. (from Pfam)
thiamine pyrophosphate-dependent enzyme
This family uses thiamine pyrophosphate as a cofactor. This family includes pyruvate dehydrogenase, 2-oxoglutarate dehydrogenase and 2-oxoisovalerate dehydrogenase. (from Pfam)
thiamine pyrophosphate-dependent dehydrogenase E1 component subunit alpha
thiamine pyrophosphate-dependent dehydrogenase E1 component subunit alpha is part of the E1 component of a multi-enzyme dehydrogenase complex such as branched-chain alpha-keto acid dehydrogenase, which catalyzes the multi-step oxidative decarboxylation of alpha-keto acids derived from the branched-chain amino-acids valine, leucine, and isoleucine
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