IDENTIFICATION OF THE N-TERMINAL DOMAIN OF ENZYME-I OF THE ESCHERICHIA-COLI PHOSPHOENOLPYRUVATE-SUGAR PHOSPHOTRANSFERASE SYSTEM PRODUCED BYPROTEOLYTIC DIGESTION
Br. Lee et al., IDENTIFICATION OF THE N-TERMINAL DOMAIN OF ENZYME-I OF THE ESCHERICHIA-COLI PHOSPHOENOLPYRUVATE-SUGAR PHOSPHOTRANSFERASE SYSTEM PRODUCED BYPROTEOLYTIC DIGESTION, Archives of biochemistry and biophysics, 312(1), 1994, pp. 121-124
The phosphoenolpyruvate:sugar phosphotransferase system of bacteria pl
ays an important role in the concomitant uptake and phosphorylation of
numerous sugars. The first protein in the pathway of phosphotransfer
of the phosphoenolpyruvate:sugar phosphotransferase system is Enzyme I
. It has been shown that a stable N-terminal domain can be produced by
treatment of the purified protein with various proteolytic enzymes. W
e show here that the region from glutamate-252 to leucine-264 is acces
sible to proteolysis resulting in N-terminal cores ranging from M(r) 2
7521 to 28799. (C) 1994 Academic Press, Inc.