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- W2023402989 abstract "An emerging concept in enzymology is the catalytic transition state ensemble: instead of the single, well-defined transition state (TS) of classical theory, enzymatic reactions progress through multiple ‘valleys’ in the energy landscape, each with its own TS. Long-lived conformations of the enzyme-substrate (ES) complex would take different pathways through the TS ensemble, and would therefore result in functional heterogeneity (i.e., a distribution of catalytic rate constants). The functional properties of enzymes are therefore completely controlled by the nature of the energetic landscape for the ES complex and the TS ensemble. We have developed TIRFM (total internal reflection fluorescence microscopy) and FCS (fluorescence correlation spectroscopy) methods to measure turnover by single immobilized enzyme molecules. We applied these methods, complemented by molecular dynamics simulations and ab initio calculations, to two isoforms of glutathione-S-transferase (GST) to examine the validity of the TS ensemble model. GST isoform A1-1 is an abundant hepatic enzyme involved in detoxification, and is extremely promiscuous in its substrate range. GST A4-4 is the predominant isoform in the heart and brain, and is specific towards lipid peroxidation products. Contrasting the behavior of these two enzymes will address fundamental questions about the mechanisms of substrate promiscuity.View Large Image | View Hi-Res Image | Download PowerPoint Slide" @default.
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- W2023402989 date "2011-02-01" @default.
- W2023402989 modified "2023-09-29" @default.
- W2023402989 title "Single-Molecule Enzymology: Studies on Glutathione-S-Transferases" @default.
- W2023402989 doi "https://doi.org/10.1016/j.bpj.2010.12.1272" @default.
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