Temperature Dependence of Kinetic Parameters for Hyperthermophilic Glutamate Dehydrogenase fromAeropyrum pernixK1

Reformulation of the Michaelis–Menten Equation: How Enzyme-Catalyzed Reactions Depend on Gibbs Energy

“…To this end, eqs 4 and 5 may be used to fit experimental data in which v m and K M are measured as a function of temperature. For example Bhuiya et al (5) have measured the kinetic parameters of a hyperthermophylic glutamate dehydrogenase found in Aeropyrum pernix K1, which binds its substrate, L-glutamate, and causes oxidative deamination. Their data are shown in Table 1 along with calculated values based on eqs 4 and 5.…”

“…The K M values in Table 1 were reported directly by Bhuiya et al (5). The v m values in the table were calculated from their reported catalytic efficiencies, defined as v m ͞K M .…”

Glutamate Dehydrogenase (GdhA) of Streptococcus pneumoniae Is Required for High Temperature Adaptation

“…In another example, the polymerization of the cell division protein FtsZ is temperature dependent, and the level of entropy for assembly of the protein changes with temperature in the host (16). Another example is glutamate dehydrogenase, which has been identified as a protein thermosensor in the hyperthermophile Aeropyrum pernix K1 (17).…”

Enzyme Free Energy Diagrams: Enzyme–Substrate Binding Is Always Spontaneous

“…decreased from 2.02 mM (50 °C) to 0.56 mM (90 °C), while V max rose from 8 to 84 μmol/min/mg enz. 6 Keeping in mind that…”

“…The thermodynamics of the binding equilibrium (step 1) and the kinetics of the catalytic step (2) can be characterized by examining their dependence on temperature. Bozlee used data from Bhuiya et al on glutamate dehydrogenase activity: For five temperatures from 50 to 90 °C, Bhiuya et al found that K m decreased from 2.02 mM (50 °C) to 0.56 mM (90 °C), while V max rose from 8 to 84 μmol/min/mg enz …”