| Autor: |
Brechtel, C E, Hu, L, King, S C |
| Zdroj: |
Journal of Biological Chemistry; January 1996, Vol. 271 Issue: 2 p783-8, 6p |
| Abstrakt: |
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 alpha-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 microM). 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. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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