Reaction Mechanism of Non-allosteric Phosphofructokinase
نویسندگان
چکیده
منابع مشابه
Studies on the reaction mechanism of skeletal muscle phosphofructokinase.
The kinetics and mechanism of action of rabbit skeletal muscle phosphofructokinase (ATP:D-fructose 6-phosphate 1 -phosphotransferase, EC 2.7.1.11) were investigated by several techniques. The initial velocity, product inhibition, isotope exchange patterns, and the result of a pulse labeling experiment are consistent with a mechanism in which ADP (or inosine diphosphate) dissociates from the enz...
متن کاملEnhancing Allosteric Inhibition in Thermus thermophilus Phosphofructokinase
The coupling between the binding of the substrate Fru-6-P and the inhibitor phospho(enol)pyruvate (PEP) in phosphofructokinase (PFK) from the extreme thermophile Thermus thermophilus is much weaker than that seen in a PFK from Bacillus stearothermophilus. From the crystal structures of Bacillus stearothermophilus PFK (BsPFK) the residues at positions 59, 158, and 215 in BsPFK are located on the...
متن کاملReevaluation of the accepted allosteric mechanism of phosphofructokinase from Bacillus stearothermophilus.
The binding of phosphoenolpyruvate (PEP) to the single allosteric site on phosphofructokinase (EC ) from Bacillus stearothermophilus (BsPFK) diminishes the ability of the enzyme to bind the substrate fructose 6-phosphate (Fru-6-P). Comparisons of crystal structures with either Fru-6-P or phosphoglycolate, an analog of PEP, bound have shown that Arg-162 interacts with the negatively charged Fru-...
متن کاملKinetic mechanism of Ascaris suum phosphofructokinase desensitized to allosteric modulation by diethylpyrocarbonate modification.
The kinetic mechanism of phosphofructokinase has been determined at pH 8 for native enzyme and pH 6.8 for an enzyme desensitized to allosteric modulation by diethylpyrocarbonate modification. In both cases, the mechanism is predominantly steady state ordered with MgATP binding first in the direction of fructose 6-phosphate (F6P) phosphorylation and rapid equilibrium random in the direction of M...
متن کاملA non-equilibrium dynamic mechanism for the allosteric effect
Allosteric regulation is often viewed as thermodynamic in nature. However protein internal motions during an enzymatic reaction cycle can be slow hopping processes over numerous potential barriers. We propose that regulating molecules may function by modifying the nonequilibrium protein dynamics. The theory predicts that an enzyme under the new mechanism has different temperature dependence, wa...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1978
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1978.tb12435.x