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Article

Towards the identification of the allosteric Phe-binding site in phenylalanine hydroxylase.

Journal of biomolecular structure & dynamics - 1 Jan 2016

Carluccio Carla, Fraternali Franca, Salvatore Francesco, Fornili Arianna, Zagari Adriana

Abstract excerpt

The enzyme phenylalanine hydroxylase (PAH) is defective in the inherited disorder phenylketonuria. PAH, a tetrameric enzyme, is highly regulated and displays positive cooperativity for its substrate, Phe. Whether Phe binds to an allosteric site is a matter of debate, despite several studies worldwide. To address this issue, we generated a dimeric model for Phe-PAH interactions, by performing molecular docking...

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Share to Allosteric Regulation
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 26479306
DOI: 10.1080/07391102.2015.1052016

Genes

PAH

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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