PMID:2829831
| Citation |
Bradley, SA, Tinsley, CR, Muiry, JA and Henderson, PJ (1987) Proton-linked L-fucose transport in Escherichia coli. Biochem. J. 248:495-500 |
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| Abstract |
1. Addition of L-fucose to energy-depleted anaerobic suspensions of Escherichia coli elicited an uncoupler-sensitive alkaline pH change diagnostic of L-fucose/H+ symport activity. 2. L-Galactose or D-arabinose were also substrates, but not inducers, for the L-fucose/H+ symporter. 3. L-Fucose transport into subcellular vesicles was dependent upon respiration, displayed a pH optimum of about 5.5, and was inhibited by protonophores and ionophores. 4. These results showed that L-fucose transport into E. coli was energized by the transmembrane electrochemical gradient of protons. 5. Neither steady state kinetic measurements nor assays of L-fucose binding to periplasmic proteins revealed the existence of a second L-fucose transport system. |
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| Keywords |
Antimetabolites/pharmacology; Biological Transport/drug effects; Carbohydrate Metabolism; Escherichia coli/drug effects; Escherichia coli/metabolism; Fucose/metabolism; Hydrogen-Ion Concentration; Kinetics; Protons; Subcellular Fractions/metabolism; Substrate Specificity |
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