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- W2016408814 abstract "The Na+/dicarboxylate cotransporters (NaDC1) from mouse (m) and rabbit (rb) differ in their ability to handle glutarate. Substrate-dependent inward currents, measured using two-electrode voltage clamp, were similar for glutarate and succinate in Xenopus oocytes expressing mNaDC1. In contrast, currents evoked by glutarate in rbNaDC1 were only about 5% of the succinate-dependent currents. To identify domains involved in glutarate transport, we constructed a series of chimeric transporters between mouse and rabbit NaDC1. Although residues found in multiple transmembrane helices (TM) participate in glutarate transport, the most important contribution is made by TM 3 and 4 and the associated loops. The R(M3−4) chimera, consisting of rbNaDC1 with substitution of TM 3−4 from mNaDC1, had a decreased K0.5glutarate of 4 mM compared with 15 mM in wild-type rbNaDC1 without any effect on K0.5succinate. The chimeras were also characterized using dual-label competitive uptakes with 14C-glutarate and 3H-succinate to calculate the transport specificity ratio (TSR), a measure of relative catalytic efficiency with the two substrates. The TSR analysis provides evidence for functional coupling in the transition state between TM 3 and 4. We conclude that TM 3 and 4 contain amino acid residues that are important determinants of substrate specificity and catalytic efficiency in NaDC1." @default.
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- W2016408814 date "2006-01-25" @default.
- W2016408814 modified "2023-09-26" @default.
- W2016408814 title "Transmembrane Helices 3 and 4 Are Involved in Substrate Recognition by the Na<sup>+</sup>/Dicarboxylate Cotransporter, NaDC1" @default.
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- W2016408814 doi "https://doi.org/10.1021/bi052328g" @default.
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