PHOSPHATE BOUND TO HISTIDINE IN A PROTEIN AS AN INTERMEDIATE IN A NOVEL PHOSPHO-TRANSFERASE SYSTEM

Abstract
A novel phospho-transferase system was isolated from E. coli K235, and was detected in other bacteria. The system involved a sequential transfer of phosphate from phosphoe-nolpyruvate to a heat-stable protein to hexoses; the two reactions were catalyzed by two distinct enzyme fractions. Isolation and characterization of the phosphorylated protein showed that the phosphate group was linked to a histidine residue.