Changes in accessibility of the membrane bound transport enzyme glucose phosphotransferase of E. coli to protein group reagents in presence of substrate or absence of energy source
Biochemical and Biophysical Research CommunicationsPublished 1 October 1973
Rosine Haguenauer‐Tsapis, Adam Képès
Citations24
SJR quartileQ2
SJR score0.75
SNIP0.56
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TL;DR
It is demonstrated in the case of N-ethylmaleimide that the target of the inhibition is the membrane bound component of the phosphoenol pyruvate glucose phospho-transferase system: enzyme II.
Abstract
The inactivation of α-methyl-D-glucoside transport in E. coli by N-ethyl-maleimide and 1-fluoro-2,4-dinitrobenzene is strongly enhanced by the presence of substrate or of an inhibitor of phosphoenol pyruvate synthesis. It is demonstrated in the case of N-ethylmaleimide that the target of the inhibition is the membrane bound component of the phosphoenol pyruvate glucose phospho-transferase system: enzyme II. Enzyme II could exist, in course of the transport, in two alternate conformational states: an energized and a deenergized state, the energized one being protected against inactivation by N-ethylmaleimide.
Keywords
Biochemistry, Genetics and Molecular Biology
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