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. Author manuscript; available in PMC: 2017 Feb 1.
Published in final edited form as: Biochemistry. 2015 Feb 12;54(7):1516–1524. doi: 10.1021/bi501426w

Figure 7.

Figure 7

Ka-app values for point mutations introduced with the intent of interrupting the Trp527/Arg528/Asp499 subunit interface interaction. The Ka-app values for the wild type proteins, both in the presence and absence of Fru-1,6-BP are indicated by horizontal reference lines. V498G and D499T mutant proteins were not activity and are not represented in the graph. Modification of Trp527 and Asp499 both caused increased affinity for PEP, similar to the allosteric activation by Fru-1,6-BP.