Substrate specificity of the Escherichia coli 4-aminobutyrate carrier encoded by gabP: Uptake and counterflow of structurally diverse molecules

Casey E. Brechtel, Liaoyuan Hu, Steven C. King

Research output: Contribution to journalArticlepeer-review

19 Scopus citations

Abstract

Transport of 4-aminobutyrate into Escherichia coli is catalyzed by gab permease (GabP). Although published studies show that GabP is relatively specific, recognizing the common α-amino acids with low affinity, recent work from this laboratory indicates that a number of synthetic compounds are high affinity transport inhibitors (50% inhibition at 5-100 μM). Here we present evidence that many of these structurally heterogeneous compounds not only inhibit transport but also function as alternative GabP substrates (i.e. a set of observations inconsistent with the idea that the core of the GabP transport channel exhibits rigid structural specificity for the native substrate, 4-aminobutyrate).

Original languageEnglish (US)
Pages (from-to)783-788
Number of pages6
JournalJournal of Biological Chemistry
Volume271
Issue number2
DOIs
StatePublished - Jan 12 1996

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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