Study of 1-deoxy-D-xylulose-5-phosphate reductoisomerase: synthesis and evaluation of fluorinated substrate analogues
| Autor: | Hung-wen Liu, Jeffrey W. Munos, Vidusha Devasthali, Kenneth A. Johnson, Alexander W. Wong |
|---|---|
| Rok vydání: | 2004 |
| Předmět: |
chemistry.chemical_classification
Hydrocarbons Fluorinated Chemistry Extramural Stereochemistry Organic Chemistry Substrate (chemistry) chemistry.chemical_element Multienzyme complexes Biochemistry Catalysis Substrate Specificity 1-deoxy-D-xylulose 5-phosphate reductoisomerase Non-competitive inhibition Enzyme Multienzyme Complexes Fluorine Physical and Theoretical Chemistry Oxidoreductases Aldose-Ketose Isomerases |
| Zdroj: | Organic letters. 6(20) |
| ISSN: | 1523-7060 |
| Popis: | [reaction: see text] 1-deoxy-D-xylulose-5-phosphate (DXP) reductoisomerase is a NADPH-dependent enzyme catalyzing the conversion of DXP to methyl-D-erythritol 4-phosphate (MEP). In this study, each of the hydroxyl groups in DXP and one of its C-1 hydrogen atoms, were separately replaced with a fluorine atom and the effect of the substitution on the catalytic turnover was examined. It was found that the 1-fluoro-DXP is a poor substrate, while both 3- and 4-fluoro-DXP behave as noncompetitive inhibitors. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|