DXP_synthase_N

• PFAM accession number: PF13292
• Interpro abstract (IPR005477):

  1-Deoxy-D-xylulose-5-phosphate synthase (DXP synthase) is a regulatory enzyme of the mevalonate-independent pathway involved in terpenoid biosynthesis. Terpeniods are plant natural products with important pharmaceutical activity. 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 [ (PUBMED:1628611) ]. In the central section there are conserved acidic residues that are part of the active cleft and may participate in substrate-binding [ (PUBMED:1628611) ]. 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.

• GO process: terpenoid biosynthetic process (GO:0016114)
• GO function: 1-deoxy-D-xylulose-5-phosphate synthase activity (GO:0008661)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry DXP_synthase_N