NMR Analysis of Enzyme-Catalyzed and Free-Equilibrium Mutarotation Kinetics of Monosaccharides
- 10 July 2004
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 126 (30) , 9180-9181
- https://doi.org/10.1021/ja047911j
Abstract
We have exploited the saturation difference (SD) NMR technique to investigate the mutarotations of two sugars, l-fucose and d-ribose, at equilibrium. The KM and kcat values of Escherichia coli FucU-catalyzed mutarotation of l-fucose have been determined by this technique, and the values of KM for α- and β-forms are shown to be the same. Similarly, the spontaneous mutarotation of d-ribose was investigated by using the same method, and it was found that d-ribose has an exceptionally high spontaneous α-to-β conversion rate only between the furan forms.Keywords
This publication has 1 reference indexed in Scilit:
- The effects of aqueous solvent structure on the mutarotation kinetics of glucoseJournal of Solution Chemistry, 1977