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The acquired data are more physiologically relevant and enable confirmation of the previously established enzyme mechanism (at 5 ☌), yielding parameters relevant for in vivo modelling. Here, we overcame enzyme lability through stop-flow limited turnover analysis, whereby kinetic parameters at 30 ☌ were obtained. Low temperature was used as the ligand free enzyme is unstable at higher temperatures. It has been shown that the steady-state behavior of the enzyme at 5 ☌ can be accounted for by its pre-steady-state behavior if the presence of a natively activated subpopulation (approximately 10 %) is assumed. MGST1 forms a homotrimer displaying third-of-the-sites-reactivity and up to 30-fold activation through modification of its Cys-49 residue. Glutathione transferases (GSTs) are a class of phase II detoxifying enzymes catalyzing the conjugation of glutathione (GSH) to endogenous and exogenous electrophilic molecules, microsomal glutathione transferase 1 (MGST1) being one of its key members.

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