Inhibition of Escherichia coli fructose-1,6-bisphosphatase by fructose 2,6-bisphosphate |
| |
Authors: | Frank Marcus Ida Edelstein Judith Rittenhouse |
| |
Institution: | Department of Biological Chemistry and Structure University of Health Sciences/The Chicago Medical School 3333 Green Bay Road, North Chicago, IL 60064 USA |
| |
Abstract: | Fructose 2,6-bisphosphate, a potent inhibitor of fructose-1,6-bisphosphatases, was found to be an inhibitor of the Escherichia coli enzyme. The substrate saturation curves in the presence of inhibitor were sigmoidal and the inhibition was much stronger at low than at high substrate concentrations. At a substrate concentration of 20 μM, 50% inhibition was observed at 4.8 μM fructose 2,6-bisphosphate. Escherichia coli fructose-1,6-bisphosphatase was inhibited by AMP (Kj = 16 μM) and phosphoenolpyruvate caused release of AMP inhibition. However, neither AMP inhibition nor its release by phosphoenolpyruvate was affected by the presence of fructose 2,6-bisphosphate. The results obtained, together with previous observations, provide further evidence for the fructose 2,6-bisphosphate-fructose-1,6-bisphosphatase active site interaction. |
| |
Keywords: | |
本文献已被 ScienceDirect 等数据库收录! |
|