IDENTIFICATION OF THE N-TERMINAL DOMAIN OF ENZYME-I OF THE ESCHERICHIA-COLI PHOSPHOENOLPYRUVATE-SUGAR PHOSPHOTRANSFERASE SYSTEM PRODUCED BYPROTEOLYTIC DIGESTION

Citation
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
Citations number
11
Categorie Soggetti
Biology,Biophysics
ISSN journal
00039861
Volume
312
Issue
1
Year of publication
1994
Pages
121 - 124
Database
ISI
SICI code
0003-9861(1994)312:1<121:IOTNDO>2.0.ZU;2-M
Abstract
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.