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In enzymology, a 1-deoxy-d-xylulose-5-phosphate synthase (EC 2.2.1.7) is an enzyme in the non-mevalonate pathway that catalyzes the chemical reaction. pyruvate + d-glyceraldehyde 3-phosphate 1-deoxy-d-xylulose 5-phosphate + CO 2
The enzyme involved in making 1-deoxy-d-xylulose 5-phosphate (DXP) is DXP synthase. [2] The mechanism follows a catalysis of decarboxylative condensation of pyruvate and d-glyceraldehyde 3-phosphate to produce DXP. [2] [3] In addition, the molecule is involved in making thiamine (vitamin B 1) and pyridoxol (vitamin B 6). [2]
This pathway, called methyl-D-erythritol phosphate (MEP) or non-mevalonate pathway, is responsible for biosynthesis of isoprenoids—molecules required for cell survival in most pathogenic bacteria and hence will be helpful in most usually antibacterial resistant bacteria.
D-Xylulose 5-phosphate (D-xylulose-5-P) is an intermediate in the pentose phosphate pathway. It is a ketose sugar formed from ribulose-5-phosphate by ribulose-5-phosphate epimerase. In the non-oxidative branch of the pentose phosphate pathway, xylulose-5-phosphate acts as a donor of two-carbon ketone groups in transketolase reactions. [1]
In this pathway the enzyme xylose isomerase converts D-xylose directly into D-xylulose. D-xylulose is then phosphorylated to D-xylulose-5-phosphate as in the oxido-reductase pathway. At equilibrium, the isomerase reaction results in a mixture of 83% D-xylose and 17% D-xylulose because the conversion of xylose to xylulose is energetically ...
Thus, the two substrates of this enzyme are D-xylulose 5-phosphate and formaldehyde, whereas its two products are glyceraldehyde 3-phosphate and glycerone. This enzyme belongs to the family of transferases , specifically those transferring aldehyde or ketonic groups (transaldolases and transketolases, respectively).
Thiazole synthase (EC 2.8.1.10, thiG (gene)) is an enzyme with systematic name 1-deoxy-D-xylulose 5-phosphate:thiol sulfurtransferase. [1] [2] [3] ...
In Arabidopsis thaliana 1-deoxy-D-xylulose 5-phosphate reductoisomerase is the first committed enzyme of the MEP pathway for isoprenoid precursor biosynthesis. The enzyme requires Mn 2+, Co 2+ or Mg 2+ for activity, with Mn 2+ being most effective.