Effect of glucose‐6‐P on the catalytic and structural properties of glycogen phosphorylase a
Authors:
- Angeliki E. MelpidouAMAngeliki E. Melpidou
- Nikolaos G. OikonomakosNONikolaos G. Oikonomakos
- 5 April 1983
- journal article
- Published by Wiley in FEBS Letters
- Vol. 154 (1) , 105-110
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°C results in ∼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.Keywords
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