Three Pyruvate Kinase Variants with Increased Affinity for PEP

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Abstract
Three variants of pyruvate kinase are described which have marked reduction of activity associated with severe non-spherocytic hemolytic anemia. Each variant shows a reduced K0.5 for phosphoenolpyruvate (the value of the intercept of the abscissa on the Hill plot) and reduced Hill coefficient; FDP [fructose diphosphate] activation and ATP inhibition are less than normal and utilization of GDP is increased. The variants are slightly less inhibited by 2,3-DPG [2,3-diphosphoglycerate] than controls but require more FDP to relieve this inhibition. Two cases had decreased thermostability but the 3rd case was normal. The mutant enzymes are further distinguished by their affinity for FDP. Their kinetic and physicochemical properties are compared with other known cases with high affinity for PEP and discussed in terms of a R .dblarw. T model for allosteric enzymes.

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