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. Author manuscript; available in PMC: 2017 Jun 1.
Published in final edited form as: J Phys Chem B. 2016 Apr 29;120(26):6021–6037. doi: 10.1021/acs.jpcb.6b01911

Figure 10.

Figure 10

Theoretically and experimentally probing the effects of an allosteric regulator on activity. Data points show experimentally measured activity from Feller et al. for the enzyme α-amylase using substrate analogue [S] (EPS) and allosteric activator [R] (NaCl).52 Best fit theoretical curves described by eq 63 are overlaid on the data. The best fit parameters are eβ(εAεI) = 7.8 × 10−4, KMA=0.6mM,KMI=0.2mM,RDA=0.03mM,RDI=7.9mM,kcatA=14s-1, and kcatI=0.01s-1.