Physical Sciences and Mathematics Commons^™

Mapping Of A Regulatory Site Of The Escherichia Coli Adp-Glucose Pyrophosphorylase, Jaina A. Bhayani, Benjamin L. Hill, Anisha Sharma, Alberto A. Iglesias, Kenneth W. Olsen, Miguel A. Ballicora

Chemistry: Faculty Publications and Other Works

The enzyme ADP-glucose pyrophosphorylase (ADP-Glc PPase) controls the biosynthesis of glycogen in bacteria and starch in plants. It is regulated by various activators in different organisms according to their metabolic characteristics. In Escherichia coli, the major allosteric activator is fructose 1,6-bisphosphate (FBP). Other potent activator analogs include 1,6-hexanediol bisphosphate (HBP) and pyridoxal 5′-phosphate (PLP). Recently, a crystal structure with FBP bound was reported (PDB ID: 5L6S). However, it is possible that the FBP site found is not directly responsible for the activation of the enzyme. We hypothesized FBP activates by binding one of its phosphate groups to …