Premium
Evidence for the phosphorylation of enzyme II glucose of the phospho enol pyruvate—sugar phosphotransferase system of Escherichia coli and Salmonella typhimurium
Author(s) -
Peri Krishna G.,
Hans L Kornberg,
Waygood E.Bruce
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)81367-8
Subject(s) - pep group translocation , biochemistry , phosphoprotein , escherichia coli , enzyme , chemistry , phosphotransferase , salmonella , polyacrylamide gel electrophoresis , phosphorylation , biology , phosphoenolpyruvate carboxykinase , bacteria , gene , genetics
A membrane‐bound phosphoprotein, of subunit Mr 48 000 by sodium dodecyl sulphate‐polyacrylamide gel electrophoresis, has been found in Escherichia coli and Salmonella typhimurium . The phosphorylation of this protein is dependent upon phospho enol pyruvate and the protein of the sugar phosphotransferase (PT) system: enzyme I, HPr, and III glucose . The membrane‐bound phosphoprotein is identified as enzyme II glucose . Other membrane‐bound phosphoproteins, that are also dependent upon the PT system, remain to be identified.