Structural basis of autoregulation of phenylalanine hydroxylase

@article{Kobe1999StructuralBO,
  title={Structural basis of autoregulation of phenylalanine hydroxylase},
  author={Bostjan Kobe and Ian G. Jennings and Colin House and Belinda J. Michell and Kenneth E. Goodwill and Bernard D Santarsiero and Raymond C. Stevens and Richard G. H. Cotton and Bruce E. Kemp},
  journal={Nature Structural Biology},
  year={1999},
  volume={6},
  pages={442-448}
}
Phenylalanine hydroxylase converts phenylalanine to tyrosine, a rate-limiting step in phenylalanine catabolism and protein and neurotransmitter biosynthesis. It is tightly regulated by the substrates phenylalanine and tetrahydrobiopterin and by phosphorylation. We present the crystal structures of dephosphorylated and phosphorylated forms of a dimeric enzyme with catalytic and regulatory properties of the wild-type protein. The structures reveal a catalytic domain flexibly linked to a… CONTINUE READING

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