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Physical mechanism for regulation of phosphoenolpyruvate-dependent glucose transport activity in Escherichia coli.

Abstract：

:The activity of the phosphoenolpyruvate-dependent glucose phosphotransferase system (PTS) in Escherichia coli is coupled to the oxidation-reduction potential. It is inhibited when the redox potential is increased above -300 mV either via substrate oxidation or via direct addition of oxidizing agents. Depending on the point of addition, dithiothreitol either blocks or reverses these effects. Inhibition occurs at the level of sugar binding to EII. A sulfhydryl group associated with EII activity undergoes reversible oxidation to, presumably, a disulfide, resulting in the conversion of EII from a reduced, high-affinity form to an oxidized, low-affinity form which has a 10(2)-10(3) times lower affinity for the sugar. An identical change in affinity occurs as the result of the generation of a delta mu H+ during the oxidation of reduced N-methylphenazonium methosulfate or nicotinamide adenine dinucleotide. In this case, uncouplers and ionophores reverse the change. A mechanism is proposed in which the electrical potential difference across the membrane regulates the glucose PTS by shifting the midpoint potential of the EII-associated redox transition to more negative values. As a result, EII is converted to the oxidized, low-affinity state in the presence of a delta mu H+.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Robillard GT,Konings WN

doi

10.1021/bi00520a032

subject

Has Abstract

pub_date

1981-08-18 00:00:00

pages

5025-32

issue

17

eissn

0006-2960

issn

1520-4995

journal_volume

20

pub_type

杂志文章

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