Pyridoxal 5-phosphate inhibition of substrate selectivity mutants of Uhpt, the sugar 6-phosphate carrier of Escherichia coli

Jason A. Hall, Peter C. Maloney

Research output: Contribution to journalArticlepeer-review

Abstract

In the sugar phosphate transporter UhpT, gain-of-function derivatives that prefer phosphoenolpyruvate (PEP) as substrate have an uncompensated lysine residue on transmembrane segment 11. We show here that these variants are also highly susceptible to substrate-protectable inhibition by covalent modification of lysine with pyridoxal 5-phosphate. The chemical requirements of this interaction provide evidence that the gain-offunction phenotype results from the pairing of the uncompensated lysines in these mutants with the anionic carboxyl group of PEP.

Original languageEnglish (US)
Pages (from-to)3756-3758
Number of pages3
JournalJournal of bacteriology
Volume184
Issue number13
DOIs
StatePublished - 2002

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology

Fingerprint Dive into the research topics of 'Pyridoxal 5-phosphate inhibition of substrate selectivity mutants of Uhpt, the sugar 6-phosphate carrier of Escherichia coli'. Together they form a unique fingerprint.

Cite this