| Literature DB >> 9573154 |
C Schaffitzel1, M Berg, P Dimroth, K M Pos.
Abstract
Two membrane proteins encoded by the malonate fermentation gene cluster of Malonomonas rubra, MadL and MadM, have been synthesized in Escherichia coli. MadL and MadM were shown to function together as a malonate transport system, whereas each protein alone was unable to catalyze malonate transport. Malonate transport by MadLM is Na+ dependent, and imposition of a DeltapNa+ markedly enhanced the rate of malonate uptake. The kinetics of malonate uptake into E. coli BL21(DE3) cells synthesizing MadLM at different pH values indicated that Hmalonate- is the transported malonate species. The stimulation of malonate uptake by Na+ ions showed Michaelis-Menten kinetics, and a Km for Na+ of 1.2 mM was determined. These results suggest that MadLM is an electroneutral Na+/Hmalonate- symporter and that it is dependent on two separate genes.Entities:
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Year: 1998 PMID: 9573154 PMCID: PMC107221 DOI: 10.1128/JB.180.10.2689-2693.1998
Source DB: PubMed Journal: J Bacteriol ISSN: 0021-9193 Impact factor: 3.490