DXP synthase is a thiamine diphosphate-dependent enzyme related to transketolase and
the pyruvate dehydrogenase E1-beta subunit. DXP synthase is found in bacteria (gene dxs)
and plants (gene CLA1) which catalyzes 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 (dxp), a
precursor in the biosynthetic pathway to isoprenoids, thiamine (vitamin B1), and pyridoxol (vitamin B6). DXP synthase is
evolutionary related to TK. The N-terminal section, contains a histidine residue which appears to function in proton transfer
during catalysis [1]. In the central section there are conserved acidic residues that are part of the active cleft
and may participate in substrate-binding [1]. This family includes transketolase enzymes EC:2.2.1.1. and also
partially matches to 2-oxoisovalerate dehydrogenase beta subunit 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.
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