Structure Basis of Allosteric Regulation Glycogen Phosphorylase

4 Structure basis of allosteric regulation Glycogen phosphorylase 

TABLE 11.15 Allosteric effectors of muscle glycogen phosphorylase 

Note The equilibrium constants for allosteric transitions for phospho- and dephospho-GP are  

Heterotropic transition Heterotropic interactions may be transmitted to the regulatory sites by the tower helices and by changes at the subunit contacts. The simultaneous binding of allosteric activator and allosteric inhibitor gives rise to a structure intermediate between the T and the R structures. The heterotropic effect is exerted throughout the subunit interface contacts. 

Comparison of allosteric enzymes, GP, phosphofructokinase (PFK) and aspartate carbamoyltransferase (CT) Despite the diversity in the subunit-subunit interfaces, the structures have in common the feature that each interface appears to be designed 

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