Kinetic characterization of Synechocystis sp. PCC6803 1-deoxy-d-xylulose 5-phosphate reductoisomerase mutants
β Scribed by Roberta P.M. Fernandes; Philip J. Proteau
- Publisher
- Elsevier Science
- Year
- 2006
- Tongue
- English
- Weight
- 268 KB
- Volume
- 1764
- Category
- Article
- ISSN
- 1570-9639
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1-Deoxy-D-xylulose-5-phosphate reductoisomerase (DXR) is the second enzyme in the non-mevalonate pathway of isoprenoid biosynthesis. The structure of the apo-form of this enzyme from Zymomonas mobilis has been solved and refined to 1.9-A Λresolution, and that of a binary complex with the co-substrat
1-Deoxy-D-xyluiose 5-phosphate is biotransformed to 2-C-methyl-D-erythritol 4-phosphate in a single step in the presence of NADPH by a new recombinant enzyme named l-deoxy-D-xylulose 5-phosphate reductoisomerase purified from Escherichia coli.
1-deoxy-D-xylulose 5-phosphate reductoisomerase catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose 5-phosphate to form 2-C-methyl-D-erythritol 4-phosphate, as the second step of the deoxyxylulose 5-phosphate/methylerythritol 4-phosphate pathway found in many bacteria and