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  • Title: Effect of glucose-6-P on the catalytic and structural properties of glycogen phosphorylase a.
    Author: Melpidou AE, Oikonomakos NG.
    Journal: FEBS Lett; 1983 Apr 05; 154(1):105-10. PubMed ID: 6832361.
    Abstract:
    Kinetic studies of muscle phosphorylase a in cationic buffer (pH 6.8) demonstrate that glucose-6-P competitively inhibits the binding of the substrate, glucose-1-P, to the enzyme. The inhibitory effect of glucose-6-P is largely overcome by glycerol-2-P. AMP counteracts inhibition of the enzyme by glucose-6-P, while glucose and glucose-6-P can interact to produce a synergistic inhibition of phosphorylase a activity. Preincubation of phosphorylase a with glucose-6-P at 20 degrees C results in approximately 3-fold increase in activity, while ultracentrifugation experiments carried out under the same conditions showed that phosphorylase a can be converted to dimers by glucose-6-P.
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