The monovalent cation requirement of rabbit muscle pyruvate kinase is eliminated by substitution of lysine for glutamate 117

Archives of Biochemistry and Biophysics
L T Laughlin, G H Reed

Abstract

The crystal structure of rabbit muscle pyruvate kinase complexed with Mn2+, K+, and pyruvate revealed a binding site of K+ [T. M. Larsen, L. T. Laughlin, H. M. Holden, I. Rayment, and G. H. Reed (1994) Biochemistry 33, 6301-6309]. Sequence comparisons of rabbit muscle pyruvate kinase and pyruvate kinases from Corynebacterium glutamicum and Escherichia coli, which do not exhibit a requirement for activation by monovalent cations, indicate that the only substitutions in the K+ binding site are conservative. Glu 117 in the rabbit muscle enzyme, which is close to the K+ site, is, however, replaced by Lys in these two bacterial pyruvate kinases. The proximity of Glu 117 to K+ in the structure of the rabbit enzyme and conservation of the binding site in the bacterial enzymes which lack a dependence on monovalent cations suggested that a protonated epsilon-amino group of Lys 117 in these bacterial enzymes may provide an "internal monovalent cation." Site-specific mutant forms of the rabbit enzyme corresponding to E117K, E117A, E117D, and E117K/K114Q pyruvate kinase were examined to test this hypothesis. The E117K pyruvate kinase exhibits 12% of the activity of the fully activated wild-type enzyme but is > 200-fold more active than the...Continue Reading

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Citations

Nov 8, 2008·Proceedings of the National Academy of Sciences of the United States of America·John P GrasonGeorge H Lorimer
Jan 26, 2007·Journal of the Royal Society, Interface·Marcella de ChampdoréSabato D'Auria
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Oct 9, 2012·Environmental Microbiology·Lina BarretoJoaquín Ariño
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Sep 9, 2005·The Journal of Biological Chemistry·Jesús Oria-HernándezLeticia Ramírez-Silva
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