The role of enzyme I in the unmasking of an essential thiol of the membrane-bound enzyme II of the phosphoenolpyruvate-glucose phosphotransferase system of Escherichia coli |
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Authors: | Rosine Haguenauer-Tsapis Adam Kepes |
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Affiliation: | Centre National de la Recherche Scientifique, Institute de Recherche en Biologie Moléculaire, Université Paris VII - Laboratoire des Biomembranes, Tour 43, 2 Place Jusseieu, 75221 - Paris Cédex 05, France |
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Abstract: | The membrane-bound component of the phosphotransferase system of Escherichia coli, responsible for the phosphorylative uptake of methyl-α-d-glucoside has an essential thiol group which becomes available to inactivation by thiol reagents in the presents of the phosphate-accepting sugar or when phosphoenolpyruvate synthesis is inhibited. The form resistant to the thiol reagent requires not only the absence of sugar and an intact phosphoenol-pyruvate generating system, but also an intact system generating phosphorylated Hpr which is impaired by heating of a thermosensitive enzyme I mutant. |
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Keywords: | enzyme I, EC 2.7.3.9 phosphoenzyme I enzyme II, EC 2.7.1.69 phosphohistidinoprotein-hexose phosphotransferase phosphoenzyme II enzyme IIglc enzyme IIbgl enzyme II specific for β-glucosides HPr phospho histidine protein |
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