Mechanism and Putative Structure of B0-like Neutral Amino Acid Transporters

Mechanism and Putative Structure of B0-like Neutral Amino Acid Transporters The Na+-dependent transport of neutral amino acids in epithelial cells and neurons is mediated by B0-type neutral amino acid transporters. Two B0-type amino acid transporters have been identified in the neurotransmitter transporter family SLC6, namely B0AT1 (SLC6A19) and B0AT2 (SLC6A15). In contrast to other members of this family, B0-like transporters are chloride-independent. B0AT1 and B0AT2 preferentially bind the substrate prior to the Na+-ion. The Na+-concentration affects the K m of the substrate and vice versa. A kinetic scheme is proposed that is consistent with the experimental data. An overlapping binding site of substrate and cosubstrate has been demonstrated in the bacterial orthologue LeuT Aa from Aquifex aeolicus, which elegantly explains the mutual effect of substrate and cosubstrate on each other’s K m -value. LeuT Aa is sequence-related to transporters of the SLC6 family, allowing homology modeling of B0-like transporters along its structure. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png The Journal of Membrane Biology Springer Journals

Mechanism and Putative Structure of B0-like Neutral Amino Acid Transporters

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Publisher
Springer-Verlag
Copyright
Copyright © 2007 by Springer Science+Business Media, LLC
Subject
Life Sciences; Biochemistry, general; Human Physiology
ISSN
0022-2631
eISSN
1432-1424
D.O.I.
10.1007/s00232-006-0879-3
Publisher site
See Article on Publisher Site

Abstract

The Na+-dependent transport of neutral amino acids in epithelial cells and neurons is mediated by B0-type neutral amino acid transporters. Two B0-type amino acid transporters have been identified in the neurotransmitter transporter family SLC6, namely B0AT1 (SLC6A19) and B0AT2 (SLC6A15). In contrast to other members of this family, B0-like transporters are chloride-independent. B0AT1 and B0AT2 preferentially bind the substrate prior to the Na+-ion. The Na+-concentration affects the K m of the substrate and vice versa. A kinetic scheme is proposed that is consistent with the experimental data. An overlapping binding site of substrate and cosubstrate has been demonstrated in the bacterial orthologue LeuT Aa from Aquifex aeolicus, which elegantly explains the mutual effect of substrate and cosubstrate on each other’s K m -value. LeuT Aa is sequence-related to transporters of the SLC6 family, allowing homology modeling of B0-like transporters along its structure.

Journal

The Journal of Membrane BiologySpringer Journals

Published: Apr 6, 2007

References

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