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• W2563200832 abstract "Mammalian phenylalanine hydroxylase (PAH) has a potential allosteric regulatory binding site for l-phenylalanine (l-Phe), in addition to its catalytic site. This arrangement is supported by a crystal structure of a homodimeric truncated form of the regulatory domain of human PAH (hPAH-RD1–118/19–118) [Patel D et al. (2016) Sci Rep doi: 10.1038/srep23748]. In this study, a fusion protein of the domain (MBP-(pepXa)-hPAH-RD1–120) was overexpressed and recovered in a metastable and soluble state, which allowed the isolation of a dimeric and a monomeric fusion protein. When cleaved from MBP, hPAH-RD forms aggregates which are stereospecifically inhibited by l-Phe (> 95%) at low physiological concentrations. Aggregation of the cleaved dimer of the mutant form hPAH-G46S-RD was not inhibited by l-Phe, which is compatible with structurally/conformationally changed βαββαβ ACT domain folds in the mutant." @default.
• W2563200832 created "2017-01-06" @default.
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• W2563200832 date "2017-01-21" @default.
• W2563200832 modified "2023-10-16" @default.
• W2563200832 title "PKU mutation p.G46S prevents the stereospecific binding ofl-phenylalanine to the dimer of human phenylalanine hydroxylase regulatory domain" @default.
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• W2563200832 doi "https://doi.org/10.1002/2211-5463.12175" @default.
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