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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
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)
thiamine pyrophosphate-binding protein similar to Streptomyces clavuligerus N(2)-(2-carboxyethyl)arginine synthase, the first enzyme in the clavulanic acid biosynthesis pathway, and to Pseudomonas fluorescens benzaldehyde lyase, which catalyzes the enantioselective carboligation of two molecules of benzaldehyde to form (R)-benzoin
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