v5.1.0.3
Glycine data from LIS
Type | Domain |
Description | 1-deoxy-D-xylulose 5-phosphate reductoisomerase synthesises 2-C-methyl-D-erythritol 4-phosphate from 1-deoxy-D-xylulose 5-phosphate in a single step by intramolecular rearrangement and reduction and is responsible for terpenoid biosynthesis in some organisms [ , ]. In Arabidopsis thaliana 1-deoxy-D-xylulose 5-phosphate reductoisomerase is the first committed enzyme of the non-mevalonate pathway for isoprenoid biosynthesis. The enzyme requires Mn2+, Co2+ or Mg2+ for activity, with the first being most effective.The structure of this enzyme has been solved, showing the protein forms a dimeric assembly and contains a metal ion in the active site [ ]. This domain is found to the C terminus of domains in bacterial and plant 1-deoxy-D-xylulose 5-phosphate reductoisomerases. This domain has been related to the dimer formation, for providing residues necessary for active site metal binding, and for positioning the substrate [ ]. |
Short Name | DXP_reductoisomerase_C |