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Journal of Bacteriology, July 2002, p. 3756-3758, Vol. 184, No. 13
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.13.3756-3758.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Pyridoxal 5-Phosphate Inhibition of Substrate Selectivity Mutants of UhpT, the Sugar 6-Phosphate Carrier of Escherichia coli

Jason A. Hall and Peter C. Maloney*

Department of Physiology, Johns Hopkins University Medical School, Baltimore, Maryland 21205

Received 4 January 2002/ Accepted 10 April 2002

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-of-function phenotype results from the pairing of the uncompensated lysines in these mutants with the anionic carboxyl group of PEP.

* Corresponding author. Mailing address: Department of Physiology, Johns Hopkins School of Medicine, 725 N. Wolfe St., Baltimore, MD 21205-2185. Phone: (410) 955-8325. Fax: (410) 955-4438. E-mail: pmaloney{at}jhmi.edu.

Journal of Bacteriology, July 2002, p. 3756-3758, Vol. 184, No. 13
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.13.3756-3758.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Hall, J. A., Maloney, P. C. (2005). Altered Oxyanion Selectivity in Mutants of UhpT, the Pi -linked Sugar Phosphate Carrier of Escherichia coli. J. Biol. Chem. 280: 3376-3381 [Abstract] [Full Text]  


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