کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10765563 | 1050593 | 2009 | 5 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Ligand binding analyses of the putative peptide transporter YjdL from E. coli display a significant selectivity towards dipeptides
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
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چکیده انگلیسی
Proton-dependent oligopeptide transporters (POTs) are secondary active transporters that couple the inwards translocation of di- and tripeptides to inwards proton translocation. Escherichia coli contains four genes encoding the putative POT proteins YhiP, YdgR, YjdL and YbgH. We have over-expressed the previously uncharacterized YjdL and investigated the peptide specificity by means of uptake inhibition. The IC50 value for the dipeptide Ala-Ala was measured to 22Â mM while Ala-Ala-Ala was not able to inhibit uptake. In addition, IC50 values of 0.3Â mM and 1.5Â mM were observed for Ala-Lys and Tyr-Ala, respectively, while the alanyl-extended tripeptides Ala-Lys-Ala, Ala-Ala-Lys, Ala-Tyr-Ala and Tyr-Ala-Ala displayed values of 8, >50, 31 and 31Â mM, respectively. These results clearly indicate that unlike most POT members characterized to date, including YdgR and YhiP, YjdL shows significantly higher specificity towards dipeptides.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 389, Issue 1, 6 November 2009, Pages 112-116
Journal: Biochemical and Biophysical Research Communications - Volume 389, Issue 1, 6 November 2009, Pages 112-116
نویسندگان
Heidi A. Ernst, Antony Pham, Helle Hald, Jette S. Kastrup, Moazur Rahman, Osman Mirza,