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Article

The W148L substitution in the Escherichia coli ammonium channel AmtB increases flux and indicates that the substrate is an ion.

Proceedings of the National Academy of Sciences of the United States of America - 20 Nov 2007

Fong Rebecca N, Kim Kwang-Seo, Yoshihara Corinne, Inwood William B, Kustu Sydney

Abstract excerpt

The Amt/Mep ammonium channels are trimers in which each monomer contains a long, narrow, hydrophobic pore. Whether the substrate conducted by these pores is NH(3) or NH(4)(+) remains controversial. Substitution of leucine for the highly conserved tryptophan 148 residue at the external opening to Escherichia coli AmtB pores allowed us to address this issue. A strain carrying AmtB(W148L) accumulates much larger...

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PMID: 17998534
DOI: 10.1073/pnas.0709267104
PMCID: PMC2141841

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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