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. 2018 Feb 6;5:4. doi: 10.3389/fmolb.2018.00004

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Copyright © 2018 Lisi, Currier and Loria.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Analysis of IGPS catalytic activity. Glutaminase profiles in the presence (A) and absence (B) of PRFAR were fit for Michaelis–Menten kinetic parameters and error bars are based on n ≥ 3 measurements and in some cases are smaller than the size of the data point. Traces are color coded as follows: black (303 K), red (313 K), blue (323 K), orange (333 K), green (343 K), and purple (353 K, Basal). Corresponding Arrhenius plots from kinetic traces of activated and basal IGPS are shown in (C) and the temperature dependence of K_m is shown in (D). The temperature driven changes in free energy (ΔΔG) between apo and PRFAR-bound IGPS are shown in (E) as a difference of (ΔG)_apo – (ΔG)_PRFAR obtained using the Eyring expression.