PDB/5FII[Secondary Source ID] - Search Results

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The phenylketonuria-associated substitution R68S converts phenylalanine hydroxylase to a constitutively active enzyme but reduces its stability.

Khan CA, Meisburger SP, Ando N, Fitzpatrick PF. Khan CA, et al. J Biol Chem. 2019 Mar 22;294(12):4359-4367. doi: 10.1074/jbc.RA118.006477. Epub 2019 Jan 23. J Biol Chem. 2019. PMID: 30674554 Free PMC article.

Biophysical characterization of full-length human phenylalanine hydroxylase provides a deeper understanding of its quaternary structure equilibrium.

Arturo EC, Gupta K, Hansen MR, Borne E, Jaffe EK. Arturo EC, et al. J Biol Chem. 2019 Jun 28;294(26):10131-10145. doi: 10.1074/jbc.RA119.008294. Epub 2019 May 10. J Biol Chem. 2019. PMID: 31076506 Free PMC article.

Simulations of the regulatory ACT domain of human phenylalanine hydroxylase (PAH) unveil its mechanism of phenylalanine binding.

Ge Y, Borne E, Stewart S, Hansen MR, Arturo EC, Jaffe EK, Voelz VA. Ge Y, et al. J Biol Chem. 2018 Dec 21;293(51):19532-19543. doi: 10.1074/jbc.RA118.004909. Epub 2018 Oct 4. J Biol Chem. 2018. PMID: 30287685 Free PMC article.

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