Resolution of the phosphoenolpyruvate: fructose phosphotransferase system of Escherichia coli into two components; enzyme IIfructose and fructose-induced HPr-like protein (FPr)

Abstract

A protein that substitutes for histidine-containing protein (HPr) in the phosphoenolpyruvate: fructose phosphotransferase system has been found in E. coli grown on fructose. The impure preparation of the fructose-induced HPr-like protein (FPr) appears to be an extrinsic membrane protein which differs from HPr on the basis of its appeparent MW (45,000 vs. 9600, respectively), its affinity for DEAE-cellulose and its ability to promote sugar phosphorylation which is specific for fructose, rather than for glucose.