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 language | English (US) |
---|---|
Pages (from-to) | 3756-3758 |
Number of pages | 3 |
Journal | Journal of bacteriology |
Volume | 184 |
Issue number | 13 |
DOIs | |
State | Published - 2002 |
Externally published | Yes |
ASJC Scopus subject areas
- Microbiology
- Molecular Biology