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

Substrate-protein interaction in human tryptophan dioxygenase: the critical role of H76.

Journal of the American Chemical Society - 11 Mar 2009

Batabyal Dipanwita, Yeh Syun-Ru

Abstract excerpt

The initial and rate-limiting step of the kynurenine pathway in humans involves the oxidation of tryptophan to N-formyl kynurenine catalyzed by two hemeproteins, tryptophan 2,3-dioxygenase (hTDO) and indoleamine 2,3-dioxygenase (hIDO). In hTDO, the conserved H76 residue is believed to act as an active site base to deprotonate the indole NH group of Trp, the initial step of the Trp oxidation reaction. In hIDO,...

Read the complete abstract on PubMed

Topics

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

Share to Biocatalysis
Share to Carboxylic Acids
Share to Catalytic Domain

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Hydrogen Bonding

Share to Indoles

Share to Molecular Structure

Share to Oxidation-Reduction

Share to Quaternary Ammonium Compounds

Source

Open in PubMed Open full text

Identifiers

PMID: 19209904
DOI: 10.1021/ja807969a
PMCID: PMC4535339

Provenance

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.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Substrate-protein interaction in human tryptophan dioxygenase: the critical role of H76.PMID 19209904Read ↗

The role of serine 167 in human indoleamine 2,3-dioxygenase: a comparison with tryptophan 2,3-dioxygenase.Semantic proximity Read ↗

Cooperative binding of L-trp to human tryptophan 2,3-dioxygenase: resonance Raman spectroscopic analysis.Semantic proximity Read ↗

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

A Trp199Glu MauG variant reveals a role for Trp199 interactions with pre-methylamine dehydrogenase during tryptophan tryptophylquinone biosynthesis.Semantic proximity Read ↗

Redox and spectroscopic properties of human indoleamine 2,3-dioxygenase and a His303Ala variant: implications for catalysis.Semantic proximity Read ↗

Chemical rescue of the distal histidine mutants of tryptophan 2,3-dioxygenase.Semantic proximity Read ↗

A conserved tryptophan in nitric oxide synthase regulates heme-dioxy reduction by tetrahydrobiopterin.Semantic proximity Read ↗

Human hepatic tryptophan 2,3-dioxygenase ubiquitin-dependent protein degradation: The critical role of its exosite as the molecular lynchpin of its substrate-mediated protein stabilizationSemantic proximity Read ↗

Understanding Biological Hydrogen Transfer Through the Lens of Temperature Dependent Kinetic Isotope Effects.Semantic proximity Read ↗

Active site aspartate residues are critical for tryptophan tryptophylquinone biogenesis in methylamine dehydrogenase.Semantic proximity Read ↗

A new conceptual framework for enzyme catalysis. Hydrogen tunnelling coupled to enzyme dynamics in flavoprotein and quinoprotein enzymes.Semantic proximity Read ↗

The stacking tryptophan of galactose oxidase: a second-coordination sphere residue that has profound effects on tyrosyl radical behavior and enzyme catalysis.Semantic proximity Read ↗

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