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Article

Spectroscopic and kinetic studies of PKU-inducing mutants of phenylalanine hydroxylase: Arg158Gln and Glu280Lys.

Journal of the American Chemical Society - 14 May 2003

Kemsley Jyllian N, Wasinger Erik C, Datta Supratim, Mitić Natasa, Acharya Tara, Hedman Britt, Caradonna John P, Hodgson Keith O, Solomon Edward I

Abstract excerpt

Phenylalanine hydroxylase (PAH) is a tetrahydrobiopterin-dependent, nonheme iron enzyme that catalyzes the hydroxylation of L-Phe to L-Tyr in the rate-limiting step of phenylalanine catabolism. This reaction is tightly coupled in the wild-type enzyme to oxidation of the tetrahydropterin cofactor. Dysfunction of PAH activity in humans leads to the disease phenylketonuria (PKU). We have investigated two...

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PMID: 12733906
DOI: 10.1021/ja029106f

Genes

PAH

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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