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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....

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Source

Identifiers

PMID: 12733906
DOI: 10.1021/ja029106f

Genes

PAH

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-12733906-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

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