Reference: Fairbrother WJ, et al. (1989) Site-directed mutagenesis of histidine 62 in the 'basic patch' region of yeast phosphoglycerate kinase. FEBS Lett 258(2):247-50

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Abstract


Site-directed mutagenesis has been used to produce a mutant form of yeast phosphoglycerate kinase (PGK) in which the 'basic patch' residue His 62 has been replaced by a glutamine residue. Using 1H-NMR spectroscopy, it was found that 3-phosphoglycerate (3-PG) binding to the mutant protein induces the same conformational effects as for wild-type PGK, although the affinity was reduced by 2- to 3-fold. Kinetic studies show both Km for 3-PG and Vmax to be increased by approximately 2-fold relative to the wild-type enzyme. These data are consistent with the suggestion that His 62 assists in the binding of the substrate to the enzyme.

Reference Type
Journal Article | Research Support, Non-U.S. Gov't
Authors
Fairbrother WJ, Hall L, Littlechild JA, Walker PA, Watson HC, Williams RJ
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