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J. Biol. Chem., Vol. 276, Issue 45, 41588-41593, November 9, 2001

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Substitution of Aspartate and Glutamate for Active Center Histidines in the Escherichia coli Phosphoenolpyruvate:Sugar Phosphotransferase System Maintain Phosphotransfer Potential^*

Scott Napper^§, Stephen J. Brokx^¶, Elliott Pally^¶, Jason Kindrachuk^¶, Louis T. J. Delbaere^¶, and E. Bruce Waygood^¶

From the ^¶ Department of Biochemistry, Health Sciences Building, University of Saskatchewan, 107 Wiggins Road, Saskatoon, SK S7N 5E5 Canada and the  Department of Biochemistry/Veterinary Infectious Disease Organization, University of Saskatchewan, 120 Veterinary Road, Saskatoon, SK S7N 5E3 Canada

The active center histidines of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system proteins; histidine-containing protein, enzyme I, and enzyme IIA^Glc were substituted with a series of amino acids (serine, threonine, tyrosine, cysteine, aspartate, and glutamate) with the potential to undergo phosphorylation. The mutants [H189E]enzyme I, [H15D]HPr, and [H90E]enzyme IIA^Glc retained ability for phosphorylation as indicated by [³²P]phosphoenolpyruvate labeling. As the active center histidines of both enzyme I and enzyme IIA^Glc undergo phosphorylation of the N² atom, while HPr is phosphorylated at the N¹ atom, a pattern of successful substitution of glutamates for N² phosphorylations and aspartates for N¹ phosphorylations emerges. Furthermore, phosphotransfer between acyl residues: P-aspartyl to glutamyl and P-glutamyl to aspartyl was demonstrated with these mutant proteins and enzymes.

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