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

Role of the N-terminus in human 4-hydroxyphenylpyruvate dioxygenase activity.

Journal of biochemistry - 1 Mar 2020

Feng An-Ning, Huang Chih-Wei, Lin Chi-Huei, Chang Yung-Lung, Ni Meng-Yuan, Lee Hwei-Jen

Abstract excerpt

4-Hydroxyphenylpyruvate dioxygenase (HPPD) is a key enzyme in tyrosine catabolism, catalysing the oxidation of 4-hydroxyphenylpyruvate to homogentisate. Genetic deficiency of this enzyme causes type III tyrosinaemia. The enzyme comprises two barrel-shaped domains formed by the N- and C-termini, with the active site located in the C-terminus. This study investigated the role of the N-terminus, located at the...

Read the complete abstract on PubMed

Topics

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

Share to Catalysis
Share to Catalytic Domain
Share to Circular Dichroism

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hydrogen Bonding

Share to Hydrophobic and Hydrophilic Interactions

Share to Molecular Dynamics Simulation

Share to Protein Domains

Share to Tyrosine

Source

Identifiers

PMID: 31722428
DOI: 10.1093/jb/mvz092

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

Role of the N-terminus in human 4-hydroxyphenylpyruvate dioxygenase activity.PMID 31722428Read ↗

The interactions in the carboxyl terminus of human 4-hydroxyphenylpyruvate dioxygenase are critical to mediate the conformation of the final helix and the tail to shield the active site for catalysis.Semantic proximity Read ↗

Functional role of residues involved in substrate binding of human 4-hydroxyphenylpyruvate dioxygenase.Semantic proximity Read ↗

4-hydroxyphenylpyruvate dioxygenase catalysis: identification of catalytic residues and production of a hydroxylated intermediate shared with a structurally unrelated enzyme.Semantic proximity Read ↗

Asp274 and his346 are essential for heme binding and catalytic function of human indoleamine 2,3-dioxygenase.Semantic proximity Read ↗

The novel R347g pathogenic mutation of aromatic amino acid decarboxylase provides additional molecular insights into enzyme catalysis and deficiency.Semantic proximity Read ↗

Crystal structure of tyrosine hydroxylase at 2.3 A and its implications for inherited neurodegenerative diseases.Semantic proximity Read ↗

A three-dimensional model of mammalian tyrosinase active site accounting for loss of function mutations.Semantic proximity Read ↗

Cross-talk between thiamin diphosphate binding and phosphorylation loop conformation in human branched-chain alpha-keto acid decarboxylase/dehydrogenase.Semantic proximity Read ↗

Roles of His291-alpha and His146-beta' in the reductive acylation reaction catalyzed by human branched-chain alpha-ketoacid dehydrogenase: refined phosphorylation loop structure in the active site.Semantic proximity Read ↗

Computational characterization of the substrate-binding mode in coproporphyrinogen III oxidase.Semantic proximity Read ↗

C-terminal hybrid mutant of Bacillus pumilus cyanide dihydratase dramatically enhances thermal stability and pH tolerance by reinforcing oligomerization.Semantic proximity Read ↗

Triosephosphate isomerase I170V alters catalytic site, enhances stability and induces pathology in a Drosophila model of TPI deficiency.Semantic proximity Read ↗

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