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• W1916573076 abstract "Abstract The pyruvate kinase (ATP: pyruvate phosphotransferase, EC 2.7.1.40) from the spore-forming bacterium Bacillus licheniformis was investigated. Pyruvate kinase was found to be rapidly inactivated by dilution at 30° or incubation at 0°. Divalent cations, P-enolpyruvate, and either AMP or Pi acted in concert to protect the enzyme against both the inactivation accompanying dilution and that caused by low temperatures. Pyruvate kinase was stabilized by Mg(II), P-enolpyruvate, and Pi during the 370-fold purification of the enzyme. Stability studies revealed that NAD+, NADH, ATP, and P-enolpyruvate partially stabilized pyruvate kinase in the presence of Mg(II). AMP and Pi decreased the apparent stability of the enzyme in the absence of Penolpyruvate. These studies also showed that the inactivation could be reversed under certain conditions. Three kinetically differentiable states of pyruvate kinase were shown, i.e. one active and two inactive. The first state, obtained when the enzyme was inactivated by dilution in the absence of metabolite ligands, was converted to the second inactive state by a time-dependent process mediated by AMP or Pi. The second inactive state, stabilized by AMP or Pi, was converted to the active, third state in a time-dependent process mediated by Mg(II) and P-enolpyruvate. This last conversion appeared to involve an aggregation process, since the rate of reactivation manifested a second order dependence on the concentration of inactive enzyme. The specific activity of pyruvate kinase in crude extracts was found not to depend on the stage of the life cycle or on the nature of the carbon-energy source supporting growth. In addition, the antiserum that was prepared against enzyme, purified 50 times, of cells grown on glucose precipitated all of the activity present in crude extracts of sporulating cells and that present in extracts of cells grown on glucose, pyruvate, or malate. Therefore, it was proposed that a single, constitutively synthesized pyruvate kinase is present in B. licheniformis." @default.
• W1916573076 created "2016-06-24" @default.
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• W1916573076 date "1971-03-01" @default.
• W1916573076 modified "2023-10-15" @default.
• W1916573076 title "Pyruvate Kinase of the Spore-forming Bacterium, Bacillus licheniformis" @default.
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• W1916573076 doi "https://doi.org/10.1016/s0021-9258(18)62371-3" @default.
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