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Abstract

Phenylalanine hydroxylase (PAH) is a key enzyme in the regulation of phenylalanine metabolism. Allosteric regulation plays a crucial role in modulating PAH activity, influencing phenylalanine homeostasis. This review explores the allosteric regulation of PAH, focusing on the mechanisms by which various ligands, including phenylalanine, tetrahydrobiopterin, and other small molecules, influence enzyme activity. Structural and biochemical studies have provided insights into the allosteric modulation of PAH, revealing complex regulatory networks that govern enzyme function. Understanding the allosteric regulation of PAH is essential for unraveling the molecular basis of phenylketonuria and developing novel therapeutic strategies for metabolic disorders.