The mechanism of the mouse (m)B0AT1 (slc6a19) transporter was studied in detail using two electrode voltage-clamp techniques and tracer studies in the Xenopus oocyte expression system. All neutral amino acids induced inward currents at physiological potentials, but large neutral non-aromatic amino acids were the preferred substrates of mB0AT1. Substrates were transported with K0.5 values ranging from approx. 1 mM to approx. 10 mM. The transporter mediates Na+–amino acid co-transport with a stoichiometry of 1:1. No other ions were involved in the transport mechanism. An increase in the extracellular Na+ concentration reduced the K0.5 for leucine, and vice versa. Moreover, the K0.5 values and Vmax values of both substrates varied with the membrane potential. As a result, K0.5 and Vmax values are a complex function of the concentration of substrate and co-substrate and the membrane potential. A model is presented assuming random binding order and a positive charge associated with the ternary [Na+–substrate–transporter] complex, which is consistent with the experimental data.
Characterization of mouse amino acid transporter B0AT1 (slc6a19)
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Christoph Böhmer, Angelika Bröer, Michael Munzinger, Sonja Kowalczuk, John E. J. Rasko, Florian Lang, Stefan Bröer; Characterization of mouse amino acid transporter B0AT1 (slc6a19). Biochem J 1 August 2005; 389 (3): 745–751. doi: https://doi.org/10.1042/BJ20050083
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