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- W2011041133 abstract "Potato tuber phosphofructokinase was purified 19·.6-fold by a combination of ethanol fractionation and DEAE-cellulose column chromatography. The enzyme was very unstable; its pH optimum was 8·0. K m for fructose-6-phosphate, ATP and Mg 2+ was 2·1 × 10 −4 M, 4·5 × 10 −5 M and 4·0 × 10 −4 M respectively. ITP, GTP, UTP and CTP can act as phosphate donors, but are less active than ATP. Inhibition of enzyme activity by high levels of ATP was reversed by increasing the concentration of fructose-6-phosphate; the affinity of enzyme for fructose-6-phosphate decreased with increasing concentration of ATP. 5′-AMP, 3′,5′-AMP, 3′-AMP, deoxy AMP, UMP, IMP, CMP, GMP, ADP, CDP, GDP and UDP did not reverse the inhibition of enzyme by ATP. ADP, phosphoenolpyruvate and citrate inhibited phosphofructokinase activity but Pi did not affect it. Phosphofructokinase was not reactivated reversibly by mild change of pH and addition of effectors." @default.
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- W2011041133 date "1973-12-01" @default.
- W2011041133 modified "2023-09-25" @default.
- W2011041133 title "Phosphofructokinase of Solanum tuberosum tuber" @default.
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- W2011041133 doi "https://doi.org/10.1016/0031-9422(73)80494-7" @default.
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