Density functional theory calculations have been used to compute geometries and 19F NMR spectra of various intermediate (IAs) and transition-state analogues (TSAs) of the phosphoryl transfer enzyme �-phosphoglucomutase (�-PGM). A variety of four-, five-, and six-coordinate IAs and TSAs have been identified in the active site of �-PGM. These IAs and TSAs are bound to either or both Asp8 and �-glucose 6-phosphate (�-G6P). The six-coordinate AlF4�-TSA, is present at low pH, while a five-coordinate MgF3�-TSA has been observed at high pH, rather than an AlF30-TSA. The spectra of three other MgF3�-TSAs [sugars: 2-deoxy-�-G6P, 6-deoxy-6-(phosphonomethyl)-�-G6P and a-galactose 1-phosphate] bound in the active site have also been computed and accurately predict the shifts of peaks in accordance with changes in the hydrogen bonding environment of the active site. Finally, computations have also been used to substantiate the identity of the minor conformer of the �-PGM-MgF3 TSA.

Utilization of computed <sup>19</sup>F NMR to identify active site intermediate and transition-state analogs in β-PGM

244th National Meeting (2012)

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Utilization of computed 19F NMR to identify active site intermediate and transition-state analogs in β-PGM

Utilization of computed ¹⁹F NMR to identify active site intermediate and transition-state analogs in β-PGM