Ligand binding analyses of the putative peptide transporter YjdL from E. coli display a significant selectivity towards dipeptides

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Ligand binding analyses of the putative peptide transporter YjdL from E. coli display a significant selectivity towards dipeptides. / Ernst, Heidi Asschenfeldt; Pham, Antony; Hald, Helle; Kastrup, Jette Sandholm; Rahman, Moazur; Mirza, Osman Asghar.

In: Biochemical and Biophysical Research Communications, Vol. 389, No. 1, 2009, p. 112-116.

Research output: Contribution to journalJournal articlepeer-review

Harvard

Ernst, HA, Pham, A, Hald, H, Kastrup, JS, Rahman, M & Mirza, OA 2009, 'Ligand binding analyses of the putative peptide transporter YjdL from E. coli display a significant selectivity towards dipeptides', Biochemical and Biophysical Research Communications, vol. 389, no. 1, pp. 112-116. https://doi.org/10.1016/j.bbrc.2009.08.098

APA

Ernst, H. A., Pham, A., Hald, H., Kastrup, J. S., Rahman, M., & Mirza, O. A. (2009). Ligand binding analyses of the putative peptide transporter YjdL from E. coli display a significant selectivity towards dipeptides. Biochemical and Biophysical Research Communications, 389(1), 112-116. https://doi.org/10.1016/j.bbrc.2009.08.098

Vancouver

Ernst HA, Pham A, Hald H, Kastrup JS, Rahman M, Mirza OA. Ligand binding analyses of the putative peptide transporter YjdL from E. coli display a significant selectivity towards dipeptides. Biochemical and Biophysical Research Communications. 2009;389(1):112-116. https://doi.org/10.1016/j.bbrc.2009.08.098

Author

Ernst, Heidi Asschenfeldt ; Pham, Antony ; Hald, Helle ; Kastrup, Jette Sandholm ; Rahman, Moazur ; Mirza, Osman Asghar. / Ligand binding analyses of the putative peptide transporter YjdL from E. coli display a significant selectivity towards dipeptides. In: Biochemical and Biophysical Research Communications. 2009 ; Vol. 389, No. 1. pp. 112-116.

Bibtex

@article{f1f62650a10611debc73000ea68e967b,
title = "Ligand binding analyses of the putative peptide transporter YjdL from E. coli display a significant selectivity towards dipeptides",
abstract = "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 IC(50) value for the dipeptide Ala-Ala was measured to 22mM while Ala-Ala-Ala was not able to inhibit uptake. In addition, IC(50) values of 0.3mM and 1.5mM 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 31mM, respectively. These results clearly indicate that unlike most POT members characterized to date, including YdgR and YhiP, YjdL shows significantly higher specificity towards dipeptides.",
keywords = "Former Faculty of Pharmaceutical Sciences",
author = "Ernst, {Heidi Asschenfeldt} and Antony Pham and Helle Hald and Kastrup, {Jette Sandholm} and Moazur Rahman and Mirza, {Osman Asghar}",
note = "Keywords: E. coli; POTs; Transport; Peptides; Ligand specificity; YjdL",
year = "2009",
doi = "10.1016/j.bbrc.2009.08.098",
language = "English",
volume = "389",
pages = "112--116",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Elsevier",
number = "1",

}

RIS

TY - JOUR

T1 - Ligand binding analyses of the putative peptide transporter YjdL from E. coli display a significant selectivity towards dipeptides

AU - Ernst, Heidi Asschenfeldt

AU - Pham, Antony

AU - Hald, Helle

AU - Kastrup, Jette Sandholm

AU - Rahman, Moazur

AU - Mirza, Osman Asghar

N1 - Keywords: E. coli; POTs; Transport; Peptides; Ligand specificity; YjdL

PY - 2009

Y1 - 2009

N2 - 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 IC(50) value for the dipeptide Ala-Ala was measured to 22mM while Ala-Ala-Ala was not able to inhibit uptake. In addition, IC(50) values of 0.3mM and 1.5mM 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 31mM, respectively. These results clearly indicate that unlike most POT members characterized to date, including YdgR and YhiP, YjdL shows significantly higher specificity towards dipeptides.

AB - 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 IC(50) value for the dipeptide Ala-Ala was measured to 22mM while Ala-Ala-Ala was not able to inhibit uptake. In addition, IC(50) values of 0.3mM and 1.5mM 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 31mM, respectively. These results clearly indicate that unlike most POT members characterized to date, including YdgR and YhiP, YjdL shows significantly higher specificity towards dipeptides.

KW - Former Faculty of Pharmaceutical Sciences

U2 - 10.1016/j.bbrc.2009.08.098

DO - 10.1016/j.bbrc.2009.08.098

M3 - Journal article

C2 - 19703419

VL - 389

SP - 112

EP - 116

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 1

ER -

ID: 14411038