Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Kinetic mechanism of phenylalanine hydroxylase: intrinsic binding and rate constants from single-turnover experiments.

Biochemistry - 12 Feb 2013

Roberts Kenneth M, Pavon Jorge Alex, Fitzpatrick Paul F

Abstract excerpt

Phenylalanine hydroxylase (PheH) catalyzes the key step in the catabolism of dietary phenylalanine, its hydroxylation to tyrosine using tetrahydrobiopterin (BH(4)) and O(2). A complete kinetic mechanism for PheH was determined by global analysis of single-turnover data in the reaction of PheHΔ117, a truncated form of the enzyme lacking the N-terminal regulatory domain. Formation of the productive...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Catalysis
Share to Hydroxylation
Share to Oxidation-Reduction

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Phenylalanine

Share to Phenylalanine Hydroxylase

Share to Pterins

Share to Substrate Specificity

Share to Tyrosine

Source

Open in PubMed Open full text

Identifiers

PMID: 23327364
DOI: 10.1021/bi301675e
PMCID: PMC3572726

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Kinetic mechanism of phenylalanine hydroxylase: intrinsic binding and rate constants from single-turnover experiments.PMID 23327364Read ↗

Spectroscopy and kinetics of wild-type and mutant tyrosine hydroxylase: mechanistic insight into O2 activation.Semantic proximity Read ↗

Insights into the catalytic mechanisms of phenylalanine and tryptophan hydroxylase from kinetic isotope effects on aromatic hydroxylation.Semantic proximity Read ↗

The activity of wild-type and mutant phenylalanine hydroxylase and its regulation by phenylalanine and tetrahydrobiopterin at physiological and pathological concentrations: an isothermal titration calorimetry study.Semantic proximity Read ↗

Phenylalanine hydroxylase: function, structure, and regulation.Semantic proximity Read ↗

Spectroscopic and kinetic studies of PKU-inducing mutants of phenylalanine hydroxylase: Arg158Gln and Glu280Lys.Semantic proximity Read ↗

Structural comparison of bacterial and human iron-dependent phenylalanine hydroxylases: similar fold, different stability and reaction rates.Semantic proximity Read ↗

Conserved tyrosine-369 in the active site of Escherichia coli copper amine oxidase is not essential.Semantic proximity Read ↗

Recombinant heteromeric phenylalanine monooxygenase and the oxygenation of carbon and sulfur substrates.Semantic proximity Read ↗

The structural basis of phenylketonuria.Semantic proximity Read ↗

Directed Metabolic Pathway Evolution Enables Functional Pterin-Dependent Aromatic-Amino-Acid Hydroxylation in Escherichia coli.Semantic proximity Read ↗

Characterization of metal ligand mutants of phenylalanine hydroxylase: Insights into the plasticity of a 2-histidine-1-carboxylate triad.Semantic proximity Read ↗

Mutation at a strictly conserved, active site tyrosine in the copper amine oxidase leads to uncontrolled oxygenase activity.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.