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- W2029853237 abstract "Glu-269, which is located on the hydrophilic face of putative helix VIII in the lactose permease of Escherichia coli, has been replaced with Asp, Gln or Cys by oligonucleotide-directed, site specific mutagenesis. Cells expressing Asp-269 permease exhibit no lactose accumulation or lactose-induced H+ translocation, but retain some ability to mediate lactose influx down a concentration gradient at high substrate concentrations. Furthermore, right-side-out membrane vesicles containing Asp-269 permease do not catalyse active lactose transport, facilitated lactose efflux or equilibrium exchange. Remarkably, however, Asp-269 permease accumulates β,d-galactopyranosyl 1-thio-β,d-galactopyranoside in a partially uncoupled fashion, whereas no transport of methyl-β,d-thiogalactopyranoside, sucrose or maltose is detectable. Mutant permeases containing neutral replacements (Gln or Cys) or Glu-269 are completely devoid of activity, although the proteins are present in the membrane at concentrations comparable with wild-type or Asp-269 permease. The observations demonstrate that a carboxylate at position 269 is essential for transport activity, and Glu-269 is important for substrate binding and/or recognition." @default.
- W2029853237 created "2016-06-24" @default.
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- W2029853237 date "1994-01-01" @default.
- W2029853237 modified "2023-10-17" @default.
- W2029853237 title "Role of glutamate-269 in the lactose permease of<i>Escherichia coli</i>" @default.
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- W2029853237 doi "https://doi.org/10.3109/09687689409161024" @default.
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