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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)
Transketolase, thiamine diphosphate binding domain
This family includes transketolase enzymes EC:2.2.1.1. and also partially matches to 2-oxoisovalerate dehydrogenase beta subunit Swiss:P37941 EC:1.2.4.4. Both these enzymes utilise thiamine pyrophosphate as a cofactor, suggesting there may be common aspects in their mechanism of catalysis. [1]. 8176731. Refined structure of transketolase from Saccharomyces cerevisiae. at 2.0 A resolution.. Nikkola M, Lindqvist Y, Schneider G;. J Mol Biol 1994;238:387-404.. [2]. 1628611. Three-dimensional structure of transketolase, a thiamine. diphosphate dependent enzyme, at 2.5 A resolution.. Lindqvist Y, Schneider G, Ermler U, Sundstrom M;. EMBO J 1992;11:2373-2379. (from Pfam)
transketolase
transketolase with the TPP di-phosphate residue-binding domain but lacking the TPP pyrimidine-binding domain and the C-terminal domain; transketolase catalyzes the transfer of a two-carbon unit from ketose phosphates to aldose phosphates
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