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. Author manuscript; available in PMC: 2010 Dec 1.
Published in final edited form as: Arch Biochem Biophys. 2009 Oct 9;492(1-2):29–39. doi: 10.1016/j.abb.2009.10.001

Figure 2.

Figure 2

Thermodynamic linkage scheme for allosteric coupling between IIAGlc and MgATP. E is the EGK-glycerol complex, A is MgATP, KAo is the Michaelis constant for MgATP in the absence of IIAGlc, KA∞ is the Michaelis constant for MgATP in the saturating presence of IIAGlc, KIIo is the dissociation constant for IIAGlc binding in the absence of MgATP, KII∞ is the dissociation constant for IIAGlc binding in the saturating presence of MgATP, Vo is Vmax in the absence of IIAGlc, and V∞ is Vmax in the saturating presence of IIAGlc.