Conformational selection turns on phenylalanine hydroxylase

Kirill A. Konovalov, Wei Wang, Xuhui Huang

Research output: Contribution to journalArticlepeer-review

1 Scopus citations


Phenylalanine hydroxylase catalyzes a critical step in the phenylalanine catabolic pathway, and impairment of the human enzyme is linked to phenylketonuria. Phenylalanine is also a positive allosteric regulator of the enzyme, and the allosteric binding site has been determined by crystallography. However, the allosteric activation mechanism remains unclear. Using large-scale simulations to explore how phenylalanine binds to the regulatory site, Ge et al. discovered gating motions of the protein that suggest a conformational selection mechanism.
Original languageEnglish (US)
Pages (from-to)19544-19545
Number of pages2
JournalJournal of Biological Chemistry
Issue number51
StatePublished - Jan 4 2021
Externally publishedYes

Bibliographical note

KAUST Repository Item: Exported on 2022-06-07
Acknowledged KAUST grant number(s): OSR-2016-CRG5-3007
Acknowledgements: This work was supported by the Hong Kong Research Grant Council (HKUST C6009-15G, 16307718, 16318816, and AoE/M-09/12) and King Abdullah University of Science and Technology (KAUST) Office of Sponsored Research (OSR) (OSR-2016-CRG5-3007). The authors declare that they have no conflicts of interest with the contents of this article.; Recipient of Hong Kong Ph.D. Fellowship Scheme PF16-06144.
This publication acknowledges KAUST support, but has no KAUST affiliated authors.

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology


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