PMID: 2502400Jul 15, 1989Paper

Site-directed mutagenesis of yeast phosphoglycerate kinase. The 'basic-patch' residue arginine 168

European Journal of Biochemistry
P A WalkerH C Watson

Abstract

There is evidence, some of it of questionable authenticity, which suggests that phosphoglycerate kinase takes up a more compact form following the binding of substrates. Using this evidence it has been assumed that a conformational rearrangement is required for phosphoryl transfer to occur and that this is brought about by moving the enzyme's two domains towards each other. In order to test this hypothesis we have modified, by site-directed mutagenesis, an arginine residue thought to be involved in stabilising the transition-state intermediate. Although some 1.3 nm away from the site of phosphoryl transfer, as seen in the crystallographically determined structure, the substitution of arginine 168 by lysine (R168K) more than halves the specific activity of the enzyme. Substituting the arginine with a methionine (R168M) reduces activity further, but not completely, thus proving that the charge associated with this residue is not essential for catalytic activity. Both mutations raise the Michaelis constants (Km) for ATP and glycerate 3-phosphate. The largest change is observed with the triose substrate and the methionine mutant, suggesting that the primary function of arginine 168 is to influence the environment of this substrate....Continue Reading

References

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Citations

Oct 1, 1989·European Journal of Biochemistry·H A BoyleR J Williams
Oct 1, 1989·European Journal of Biochemistry·W J FairbrotherR J Williams
May 31, 1990·European Journal of Biochemistry·W J FairbrotherR J Williams
Jul 1, 1992·European Journal of Biochemistry·P A WalkerH C Watson
Aug 15, 1993·European Journal of Biochemistry·H C João, R J Williams
Dec 1, 1994·Biophysical Chemistry·S J HendersonG J Bunick
Jun 19, 1998·Biochemistry·A N Szilágyi, M Vas

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