From a comparison of the effects of potential inhibitors it is concluded that the furanose configuration of fructose 1,6-diphosphate is utilized by FDPase. The partial competitive inhibitor methyl d-fructoside 1,6-diphosphate, apparently induces a conformational change that permits acetylation of the active site. The probable importance of the C-2 hydroxyl of the sugar phosphate in the mechanism of FDPase is discussed.
All Science Journal Classification (ASJC) codes
- Molecular Biology