{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["11"],"submitter":["Hao DL"],"pubmed_abstract":["AtAMT1;3 is a major contributor to high-affinity ammonium uptake in <i>Arabidopsis</i> roots. Using a stable electrophysiological recording strategy, we demonstrate in <i>Xenopus laevis</i> oocytes that AtAMT1;3 functions as a typical high-affinity NH<sub>4</sub> <sup>+</sup> uniporter independent of protons and Ca<sup>2+</sup>. The findings that AtAMT1;3 transports methylammonium (MeA<sup>+</sup>, a chemical analog of NH<sub>4</sub> <sup>+</sup>) with extremely low affinity (<i>K</i> <sub>m</sub> in the range of 2.9-6.1 mM) led to investigate the mechanisms underlying substrate binding. Homologous modeling and substrate docking analyses predicted that the deduced substrate binding motif of AtAMT1;3 facilitates the binding of NH<sub>4</sub> <sup>+</sup> ions but loosely accommodates the bi"],"journal":["Frontiers in plant science"],"pagination":["571"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7256485"],"repository":["biostudies-literature"],"pubmed_title":["Functional Characterization of the <i>Arabidopsis</i> Ammonium Transporter AtAMT1;3 With the Emphasis on Structural Determinants of Substrate Binding and Permeation Properties."],"pmcid":["PMC7256485"],"pubmed_authors":["Liu SX","Zhou JY","Sentenac H","Hao DL","Very AA","Huang YN","Su YH","Yang SY"],"additional_accession":[]},"is_claimable":false,"name":"Functional Characterization of the <i>Arabidopsis</i> Ammonium Transporter AtAMT1;3 With the Emphasis on Structural Determinants of Substrate Binding and Permeation Properties.","description":"AtAMT1;3 is a major contributor to high-affinity ammonium uptake in <i>Arabidopsis</i> roots. Using a stable electrophysiological recording strategy, we demonstrate in <i>Xenopus laevis</i> oocytes that AtAMT1;3 functions as a typical high-affinity NH<sub>4</sub> <sup>+</sup> uniporter independent of protons and Ca<sup>2+</sup>. The findings that AtAMT1;3 transports methylammonium (MeA<sup>+</sup>, a chemical analog of NH<sub>4</sub> <sup>+</sup>) with extremely low affinity (<i>K</i> <sub>m</sub> in the range of 2.9-6.1 mM) led to investigate the mechanisms underlying substrate binding. Homologous modeling and substrate docking analyses predicted that the deduced substrate binding motif of AtAMT1;3 facilitates the binding of NH<sub>4</sub> <sup>+</sup> ions but loosely accommodates the bi","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020","modification":"2026-05-04T12:44:21.435Z","creation":"2020-06-14T07:07:04Z"},"accession":"S-EPMC7256485","cross_references":{"pubmed":["32528489"],"doi":["10.3389/fpls.2020.00571"]}}