Abstract
Glycogen phosphorylase. The structural basis of the allosteric response and comparison with other allosteric proteins.
Highlights
From the Laboratory of Molecular Biophysics, University of Oxford, Rex Richards Building, Oxford OX1 3QU, United Kingdom
R states for three other allosteric proteins: Escherichiu coli aspartate carbamoyltransferase (g-13), rabbit muscle glycogen phosphorylase (GP)’ [14,15,16,17], and bacterial phosphofructokinase [18,19,20,21]. In this Minireview the recent x-ray structural evidence for glycogen phosphorylase is summarized and the allosteric mechanism compared with the mechanisms of the other three proteins
Phosphorylase b (GPb), the form of the enzyme found in resting muscle, requires AMP for activity and is inhibited by glucose6-P and ATP
Summary
From the Laboratory of Molecular Biophysics, University of Oxford, Rex Richards Building, Oxford OX1 3QU, United Kingdom. In the crystals sulfate mimics phosphate and binds at the catalytic site, the AMP allosteric site, and the Ser(P) site (in GPb).
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