Enzymatic Synthesis of Cytidine Diphosphate 3,6-Dideoxyhexoses
Year: 1972
Type: article
Abstract: A procedure is described for the purification of CDP-d-glucose oxidoreductase which catalyzes formation of CDP-4-keto-6-deoxy-d-glucose and for enzymes E1 and E3 which catalyze the further reduction to CDP-4-keto-3,6-dideoxy-d-glucose. All three enzymes have been purified to homogeneity as judged by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. CDP-d-glucose oxidoreductase has been shown to consist of two identical subunits of molecular weight of about 43,000 per subunit. Enzymes E1 and E3 consist of simple polypeptide chains of molecular weight of about 61,000 and 41,000, respectively. Preliminary studies on the mechanism of the reaction suggest that enzyme E1 binds the substrate and that pyridoxamine 5'-phosphate is essential for the binding. Enzyme E3 has been shown to possess NADH oxidase activity and may be the reductase. A mechanism involving participation of the essential cofactor, pyridoxamine-5'-phosphate, is discussed.
Source: Journal of Biological Chemistry
Authors: Pedro Gonzalez-Porque, Jack L. Strominger
Institution: Harvard University
Language: English
Subfield: Organic Chemistry
Field: Chemistry
Domain: Physical Sciences
Open Access status: hybrid
Estimated APC paid: $3,430
OpenAlex ID: W1571432956