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- W2912106920 abstract "Phosphoglucose isomerases (PGIs) are a class of enzymes that catalyze the reversible isomerization of fructose-6-phosphate (F6P) and glucose-6-phosphate (G6P). PGIs are crucial in glycolysis and gluconeogenesis pathways and have been proposed as “moonlighting” proteins in different organisms. In humans, an inactive or inefficient PGI leads to nonspherocytic hemolytic anemia, and PGI elevation is a known marker for tumor metastasis, which highlights the importance of understanding the function of PGIs. The proposed function of Thermotoga maritimaPGI (TmPGI), based on structural similarity, was confirmed by kinetic and colorimetric assays in addition to 1H nuclear magnetic resonance (NMR) spectroscopy. Evidence of solvent exchange in the 1H NMR spectra supports that TmPGI isomerization proceeds through the ene-diol intermediate mechanism, rather than the alternative direct hydride shift. The ene-diol mechanism consists of three basic steps: ring opening, isomerization, and ring closure. A glutamate (E281) and a histidine (H310) residue in the active site each have been proposed as the catalytic base that forms the ene-diol intermediate based on previous crystal structures of PGIs. To determine which of these residues is the PGI residue critical for base catalysis, alanine mutations, E281A and H310A, corresponding to the TmPGI residues in the active site. The E281A mutant activity and solvent exchange behavior were consistent with wild-type TmPGI at high enzyme concentrations (μM), suggesting that the proposed catalytic glutamate is not critical for PGI function. In addition to the catalytic base activity, TmPGI H310 has been proposed as the residue performing the first ring opening step; thus, the proposed active site histidine residue may be performing both ring-opening and isomerization steps of PGIs that utilize the ene-diol pathway. Preliminary results with H310A will be presented to investigate this hypothesis." @default.
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- W2912106920 date "2019-02-01" @default.
- W2912106920 modified "2023-09-30" @default.
- W2912106920 title "Investigating the Catalytic Base Residues in the Phosphoglucose Isomerase From Thermotoga maritima" @default.
- W2912106920 doi "https://doi.org/10.1016/j.bpj.2018.11.398" @default.
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