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- W1969185269 abstract "Two relatively simple procedures are described for the purification of phosphofructokinase from the extreme thermophile, Thermus X-1. The native enzyme has a molecular weight of 1.32 × 105 and contains four apparently identical polypeptide chains. One substrate, fructose-6-phosphate, induces a cooperative protein transition while the other substrate, ATP, does not. Phosphoenolpyruvate functions as an avid negative effector and ADP is a positive effector. The enzyme has an optimum temperature for catalysis of 80 °C. Persistence of the catalytic and allosteric properties over the temperature range 20–80 °C suggests that the same protein structure is retained throughout this temperature range. Thermus X-1 phosphofructokinase is more stable to inactivation by heat, urea, guanidine hydrochloride or acidification than the phosphofructokinases obtained from the mesophilic organisms Escherichia coli and Clostridium pasteurianum. Comparison of the amino acid compositions of the three enzymes indicates no substantive differences in their hydrophobicity, hydrogen bonding potential or average residue size. The markedly elevated optimum temperature for catalysis exhibited by the Thermus enzyme appears to result from stabilization of its catalytically functional conformational to a reversible thermal inactivation above 40 °C and to ligation of the substrate fructose-6-phosphate." @default.
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- W1969185269 date "1975-12-01" @default.
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- W1969185269 title "A thermostable phosphofructokinase from the extreme thermophile Thermus X-1" @default.
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- W1969185269 doi "https://doi.org/10.1016/0003-9861(75)90081-8" @default.
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