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    Pah phenylalanine hydroxylase [ Rattus norvegicus (Norway rat) ]

    Gene ID: 24616, updated on 9-Dec-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Manipulation of a cation-pi sandwich reveals conformational flexibility in phenylalanine hydroxylase.

    Manipulation of a cation-π sandwich reveals conformational flexibility in phenylalanine hydroxylase.
    Arturo EC, Merkel GW, Hansen MR, Lisowski S, Almeida D, Gupta K, Jaffe EK., Free PMC Article

    06/12/2021
    results support a model for allostery in PheH in which phenylalanine stabilizes the dimerization of the regulatory domains and exposes the active site for substrate binding and other structural changes needed for activity

    Domain Movements upon Activation of Phenylalanine Hydroxylase Characterized by Crystallography and Chromatography-Coupled Small-Angle X-ray Scattering.
    Meisburger SP, Taylor AB, Khan CA, Zhang S, Fitzpatrick PF, Ando N., Free PMC Article

    05/5/2018
    The results identify the location of the allosteric site as the interface of the regulatory domain dimer formed in activated PheH.

    Identification of the Allosteric Site for Phenylalanine in Rat Phenylalanine Hydroxylase.
    Zhang S, Fitzpatrick PF., Free PMC Article

    08/20/2016
    use of SAXS and X-ray crystallography together to inspect PAH structure provides, to our knowledge, the first complete view of the enzyme in a tetrameric form that was not possible with prior partial crystal structures

    First structure of full-length mammalian phenylalanine hydroxylase reveals the architecture of an autoinhibited tetramer.
    Arturo EC, Gupta K, Héroux A, Stith L, Cross PJ, Parker EJ, Loll PJ, Jaffe EK., Free PMC Article

    08/6/2016
    allosteric activation of phenylalanine hydroxylase is linked to dimerization of regulatory domains

    The Amino Acid Specificity for Activation of Phenylalanine Hydroxylase Matches the Specificity for Stabilization of Regulatory Domain Dimers.
    Zhang S, Hinck AP, Fitzpatrick PF., Free PMC Article

    11/7/2015
    Data suggest that phenylalanine [concentration-dependent] activation of phenylalanine hydroxylase does not involve the active site; mutating the active-site residue Arg270 to lysine abolishes phenylalanine-dependent enzyme activation.

    Activation of phenylalanine hydroxylase by phenylalanine does not require binding in the active site.
    Roberts KM, Khan CA, Hinck CS, Fitzpatrick PF., Free PMC Article

    02/21/2015
    the conformational change upon phosphorylation of phenylalanine hydroxylase is different from and less extensive than that upon phenylalanine activation.

    Regulation of phenylalanine hydroxylase: conformational changes upon phosphorylation detected by H/D exchange and mass spectrometry.
    Li J, Fitzpatrick PF., Free PMC Article

    08/31/2013
    A new model for allosteric regulation of phenylalanine hydroxylase: implications for disease and therapeutics.

    A new model for allosteric regulation of phenylalanine hydroxylase: implications for disease and therapeutics.
    Jaffe EK, Stith L, Lawrence SH, Andrake M, Dunbrack RL Jr., Free PMC Article

    04/20/2013
    the regulatory domain of phenylalanine hydroxylase can bind phenylalanine

    Direct evidence for a phenylalanine site in the regulatory domain of phenylalanine hydroxylase.
    Li J, Ilangovan U, Daubner SC, Hinck AP, Fitzpatrick PF., Free PMC Article

    02/26/2011
    Metal ligand mutants of Pah are characterized.

    Characterization of metal ligand mutants of phenylalanine hydroxylase: Insights into the plasticity of a 2-histidine-1-carboxylate triad.
    Li J, Fitzpatrick PF., Free PMC Article

    01/21/2010
    Promoter characterized, sequences bind HNF1 and CREB transcription factors present in rat nuclear extracts

    Sequence analysis of the rat phenylalanine hydroxylase gene promoter.
    Rees D, Fisher MJ, McDowall IL.

    01/21/2010
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