Data files

ITC binding experiment for the binding of NADPH to Gre2p in HEPES buffer (100 mM, pH 7.5) at 25 °C. *.apj file

ITC binding experiment for the binding of NADP+ to Gre2p in KPi buffer (100 mM, pH 7.5) at 25 °C. *.apj file

ITC binding experiment for the binding of NADP+ to Gre2p in PBS buffer (1x, pH 7.5) at 25 °C. Note that for successfull fitting, the stoichiometry of binding had to be fixed at 0.85, in agreement with data from the other binding experiments. *.apj file

ITC binding experiment for the binding of NADPH to Gre2p in HEPES buffer (100 mM, pH 7.5) at 25 °C. *.csv file.

ITC binding experiment for the binding of NADPH to Gre2p in PBS buffer (1x, pH 7.5) at 25 °C. *.csv file.

ITC binding experiment for the binding of NADP+ to Gre2p in KPi buffer (100 mM, pH 7.5) at 25 °C. *.csv file.

ITC binding experiment for the binding of NADP+ to Gre2p in PBS buffer (1x, pH 7.5) at 25 °C. Note that for successfull fitting, the stoichiometry of binding had to be fixed at 0.85, in agreement with data from the other binding experiments. *.csv file.

ITC binding experiment for the binding of NADPH to Gre2p in KPi buffer (100 mM, pH 7.5) at 25 °C. *.apj file

ITC binding experiment for the binding of NADPH to Gre2p in PBS buffer (1x, pH 7.5) at 25 °C. *.apj file

ITC binding experiment for the binding of NADPH to Gre2p in KPi buffer (100 mM, pH 7.5) at 25 °C. *.csv file.

Activity (initial rates) of Gre2p were measured followng NADPH absorbance at different substrate [NDK] concentrations. Initial rates are calculated (mM/s) and plotted as a function of [NDK] to allow fitting with a enzyme kinetic model, e.g. Michaelis Menten. These are the raw data obtained directly from the Synergy UV-Vis Spectrophotometer.

Activity (initial rates) of Gre2p were measured followng NADPH absorbance at different substrate [hexane-2,5-dione] concentrations. Initial rates are calculated (mM/s) and plotted as a function of [hexane-2,5-dione] to allow fitting with a enzyme kinetic model, e.g. Michaelis Menten. This is a file that can be opened with the Origin Software for analysis and contains data copied in manually from the xlsx.

Activity (initial rates) of Gre2p were measured followng NADPH absorbance at different substrate [hexane-2,5-dione] concentrations. Initial rates are calculated (mM/s) and plotted as a function of [hexane-2,5-dione] to allow fitting with a enzyme kinetic model, e.g. Michaelis Menten. These are the raw data obtained directly from the Synergy UV-Vis Spectrophotometer.

Specific activity of Gre2p was measured after different treatments (none, on ice, at room temperature, in the ITC, stirred, shaken). These data are used to perform a Selwyn Test to determine if enzyme inactivation or slow-onset inhibition occurs. This is a file that can be opened with the Origin Software for analysis and contains data copied in manually from the xlsx.

Specific activity of Gre2p was measured after incubation with different Tween-20 concentrations (none, 0.01, 0.1, 1.0%). These data are also used to perform a Selwyn Test to determine if enzyme inactivation or slow-onset inhibition occurs. This is a file that can be opened with the Origin Software for analysis and contains data copied in manually from the xlsx.

Specific activity of Gre2p was measured after incubation with different Tween-20 concentrations (none, 0.01, 0.1, 1.0%). These data are also used to perform a Selwyn Test to determine if enzyme inactivation or slow-onset inhibition occurs. These are the raw data obtained directly from the Synergy UV-Vis Spectrophotometer.

Activity (initial rates) of Gre2p were measured followng NADPH absorbance at different substrate [NDK] concentrations. Initial rates are calculated (mM/s) and plotted as a function of [NDK] to allow fitting with a enzyme kinetic model, e.g. Michaelis Menten. This is a file that can be opened with the Origin Software for analysis and contains data copied in manually from the xlsx.