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  • Title: Structural analysis of human glutamine:fructose-6-phosphate amidotransferase, a key regulator in type 2 diabetes.
    Author: Nakaishi Y, Bando M, Shimizu H, Watanabe K, Goto F, Tsuge H, Kondo K, Komatsu M.
    Journal: FEBS Lett; 2009 Jan 05; 583(1):163-7. PubMed ID: 19059404.
    Abstract:
    Glutamine:fructose-6-phosphate amidotransferase (GFAT) is a rate-limiting enzyme in the hexoamine biosynthetic pathway and plays an important role in type 2 diabetes. We now report the first structures of the isomerase domain of the human GFAT in the presence of cyclic glucose-6-phosphate and linear glucosamine-6-phosphate. The C-terminal tail including the active site displays a rigid conformation, similar to the corresponding Escherichia coli enzyme. The diversity of the CF helix near the active site suggests the helix is a major target for drug design. Our study provides insights into the development of therapeutic drugs for type 2 diabetes.
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