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• W2156571746 abstract "Phosphoglucose isomerase (PGI) is a multifunctional protein, which, inside the cell, functions as a housekeeping enzyme of glycolysis and gluconeogenesis and, outside the cell, exerts wholly unrelated cytokine properties. We have determined the structure of human PGI to a resolution of 1.6 A using X-ray crystallography. The structure is highly similar to other PGIs, especially the architecture of the active site. Fortuitous binding of a sulphate molecule from the crystallisation solution has facilitated an accurate description of the substrate phosphate-binding site. Comparison with both native and inhibitor-bound rabbit PGI structures shows that two loops move closer to the active site upon binding inhibitor. Interestingly, the human structure most closely resembles the inhibitor-bound structure, suggesting that binding of the phosphate moiety of the substrate may trigger this conformational change. We suggest a new mechanism for catalysis that uses Glu357 as the base catalyst for the isomerase reaction rather than His388 as proposed previously. The human PGI structure has also provided a detailed framework with which to map mutations associated with non-spherocytic haemolytic anaemia." @default.
• W2156571746 created "2016-06-24" @default.
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• W2156571746 date "2001-06-01" @default.
• W2156571746 modified "2023-10-06" @default.
• W2156571746 title "The crystal structure of human phosphoglucose isomerase at 1.6 Å resolution: implications for catalytic mechanism, cytokine activity and haemolytic anaemia" @default.
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• W2156571746 doi "https://doi.org/10.1006/jmbi.2001.4680" @default.
• W2156571746 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/11371164" @default.
• W2156571746 hasPublicationYear "2001" @default.
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