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On the evolutionary origins of the bacterial phosphoenolpyruvate:sugar phosphotransferase system
Author(s) -
Wu L.F.,
Saier M. H.
Publication year - 1990
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.1990.tb00698.x
Subject(s) - biology , pep group translocation , rhodobacter , phosphoenolpyruvate carboxykinase , biochemistry , enzyme , phosphofructokinase 2 , gene , protein superfamily , genetics , mutant
Summary The genes encoding the proteins of the fructose‐specific phosphotransferase system (PTS) of Rhodobacter capsulatus were sequenced, and the deduced amino acyl sequences of the energy‐coupling protein, Enzyme I, and the transport protein, Enzyme II tru , were compared with published sequences. Enzyme I was found to be homologous to pyruvate: phosphate dikinase of plants, while Enzyme II fru was found to be homologous to the insulin‐responsive glucose facilitator of mammals. The evolutionary and functional implications of these findings are discussed.