Abstract
Abstract An unlinked suppressor mutation, pfkB1, was reported to restore fructose 6-phosphate kinase activity to fructose 6-phosphate kinase mutants (e.g. pfkA1; Morrissey, A. T. E., and Fraenkel, D. G. (1972) J. Bacteriol. 112, 183). We show here that a strain wild type at the pfkA locus and also carrying the suppressor mutation contains two readily separable enzyme activities. Activity 1 resembles the known allosteric wild type enzyme, and activity 2 does not show allosteric characteristics.
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