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J Membr Biol. 1998 Sep 1;165(1):65-76.

Characterization of fumarate transport in Helicobacter pylori.

Author information

1
School of Biochemistry and Molecular Genetics, University of New South Wales, Sydney, 2052, Australia.

Abstract

The fumarate transport system of the bacterium Helicobacter pylori was investigated employing radioactive tracer analysis. The transport of fumarate at micromolar concentrations was saturable with a KM of 220 +/- 21 micron and Vmax of 54 +/- 2 nmole/min/mg protein at 20 degrees C, depended on temperature between 4 and 40 degrees C, and was susceptible to inhibitors, suggesting the presence of one or more fumarate carriers. The release of fumarate from cells was also saturable with a KM of 464 +/- 71 micron and Vmax of 22 +/- 2 nmol/min/mg protein at 20 degrees C. The rates of fumarate influx at millomolar concentrations increased linearly with permeant concentration, and depended on the age of the cells. The transport system was specific for dicarboxylic acids suggesting that fumarate is taken up via dicarboxylate transporters. Succinate and fumarate appeared to form an antiport system. The properties of fumarate transport were elucidated by investigating the effects of amino acids, monovalent cations, pH and potential inhibitors. The results provided evidence that influx and efflux of fumarate at low concentrations from H. pylori cells was a carrier-mediated secondary transport with the driving force supplied by the chemical gradient of the anion. The anaerobic C4-dicarboxylate transport protein identified in the genome of the bacterium appeared to be a good candidate for the fumarate transporter.

PMID:
9705983
DOI:
10.1007/s002329900421
[Indexed for MEDLINE]

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