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Two membrane proteins encoded by the malonate fermentation gene cluster ofMalonomonas rubra , MadL and MadM, have been synthesized inEscherichia 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 ΔpNa+ markedly enhanced the rate of malonate uptake. The kinetics of malonate uptake intoE. 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 aKm 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.

Identification of an Na + -Dependent Malonate Transporter of Malonomonas rubra and Its Dependence on Two Separate Genes

Identification of an Na ⁺ -Dependent Malonate Transporter of Malonomonas rubra and Its Dependence on Two Separate Genes