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XB-ART-14982
Biochem Biophys Res Commun 1998 May 08;2461:39-44. doi: 10.1006/bbrc.1998.8566.
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Identification of a potential substrate binding domain in the mammalian peptide transporters PEPT1 and PEPT2 using PEPT1-PEPT2 and PEPT2-PEPT1 chimeras.

Fei YJ , Liu JC , Fujita T , Liang R , Ganapathy V , Leibach FH .


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The mammalian peptide transporters PEPT1 and PEPT2 are energized by a transmembrane electrochemical H+ gradient and exhibit similar broad substrate specificity. These transporters however differ in their affinity for substrates, PEPT1 being a low-affinity transporter and PEPT2 being a high-affinity transporter. To identify the substrate binding domain in PEPT1 and PEPT2 which is responsible for the differing affinities, we constructed a series of PEPT1-PEPT2 and PEPT2-PEPT1 chimeras using an in vivo restriction site-independent procedure and determined their substrate affinities. A comparison of these kinetic data for different chimeras with those of the wild-type PEPT1 and PEPT2 in conjunction with the specific structural PEPT1/PEPT2 crossover regions in these chimeras has led to the identification of a putative substrate binding site, which is comprised of the transmembrane domains 7, 8 and 9 of the transporters.

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Species referenced: Xenopus laevis
Genes referenced: slc15a1 slc15a2