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

J. Biol. Chem.. 2019; 
KhanCrystal A,MeisburgerSteve P,AndoNozomi,FitzpatrickPa
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Mutagenesis Services … The R68S mutation was introduced into both using the QuikChange (Agilent) site- directed mutagenesis method with oligonucleotides from Integrated … The coding regions of all expression plasmids were sequenced by GenScript Biotech Corporation to verify the mutation and to … Get A Quote

摘要

The naturally occurring R68S substitution of phenylalanine hydroxylase (PheH) causes phenylketonuria (PKU). However, the molecular basis for how the R68S variant leads to PKU remains unclear. Kinetic characterization of R68S PheH establishes that the enzyme is fully active in the absence of allosteric binding of phenylalanine, in contrast to the WT enzyme. Analytical ultracentrifugation establishes that the isolated regulatory domain of R68S PheH is predominantly monomeric in the absence of phenylalanine and dimerizes in its presence, similar to the regulatory domain of the WT enzyme. Fluorescence and small-angle X-ray scattering analyses establish that the overall conformation of the resting form of R68S... More

关键词

allosteric regulation,allostery,analytical ultracentrifugation,enzyme kinetics,enzyme stability,hydroxylase,phenylalanine hydroxylase,phenylketonuria,protein conformation,protein structure,small-angle X-ray scattering (S