Enzymatic Synthesis of Cytidine Diphosphate 3,6-Dideoxyhexoses
Year: 1974
Type: article
Abstract: Enzyme E3, one of the two enzymes required to promote the formation of CDP-4-keto-3,6-dideoxyglucose from CDP-4-keto-6-deoxyglucose, is thought to catalyze the NADPH requiring reduction in which the 3-deoxy group is actually formed from the intermediate discussed in the preceding paper. One mole of NAD(P)H was oxidized for every mole of sugar reduced when the reaction was carried out in an argon atmosphere. Experiments with both A- and B-[4-3H]NADPH have shown that there is no direct hydride transfer from NADPH to either the sugar being reduced or to pyridoxamine 5'-phosphate, a participant in the reaction. On the other hand, using tritiated water 1 atom of hydrogen is incorporated into the CDP-4-keto-3,6-dideoxyglucose formed. E3 alone also catalyzes the oxidation of NAD(P)H although there is no chromophoric group such as a flavin associated with the enzyme. However, added FMN or 2,6-dichlorophenolindophenol greatly enhances the rate of NAD(P)H oxidation by E3.
Source: Journal of Biological Chemistry
Authors: Peter A. Rubenstein, 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: W1518575349