Category:Complex:DXP reductoisomerase

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Description (originally from EcoCyc[1]) DXP reductoisomerase

Description (originally from EcoCyc[2]) 1-deoxy-D-xylulose 5-phosphate reductoisomerase

Comments (originally from EcoCyc[2]) Quite a few kinetic values have been determined for Dxr, at various pH values and with varying cofactors. One analysis gives Km values of 250 µM for 1-deoxy-D-xylylose 5-phosphate (DXP) and 7.4 µM for NADPH when Mn2+ is the cofactor. When Mg2+ is the cofactor, these values are 99 µM and 18 µM, respectively. When Co2+ is the cofactor, these values are 60 µM and 8.8 µM, respectively [3][4][5][6].


  1. EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  2. 2.0 2.1 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. Kuzuyama, T et al. (2000) Characterization of 1-deoxy-D-xylulose 5-phosphate reductoisomerase, an enzyme involved in isopentenyl diphosphate biosynthesis, and identification of its catalytic amino acid residues. J. Biol. Chem. 275 19928-32 PubMed
  4. Mac Sweeney, A et al. (2005) The crystal structure of E.coli 1-deoxy-D-xylulose-5-phosphate reductoisomerase in a ternary complex with the antimalarial compound fosmidomycin and NADPH reveals a tight-binding closed enzyme conformation. J. Mol. Biol. 345 115-27 PubMed
  5. Fox, DT & Poulter, CD (2005) Mechanistic studies with 2-C-methyl-D-erythritol 4-phosphate synthase from Escherichia coli. Biochemistry 44 8360-8 PubMed
  6. Hoeffler, JF et al. (2002) Isoprenoid biosynthesis via the methylerythritol phosphate pathway. Mechanistic investigations of the 1-deoxy-D-xylulose 5-phosphate reductoisomerase. Eur. J. Biochem. 269 4446-57 PubMed

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