Component
Protein-bound L-threonine residue
Context-specific entity; species, compartment and exposure are stated on each claim.
2 recorded relationships. Experimental role, claim status and evidence remain attached to each record.
How nutrients influence it
Every nutrient with a recorded effect on this component, credited to the nutrient that acted rather than the chapter that recorded it. Open a nutrient to see the findings and the conditions they were measured under.
Other things that act on it
Enzymes, hormones, genes, and other components with a recorded effect. These are not nutrients, so they do not count toward the arrows above. Each finding names the chapter that recorded it.
How nutrients reach it in more than one step
Chains of two or more recorded steps that end here, grouped by the nutrient they start from. Each step is a separate finding, so a chain is a route a mechanism could take, not proof that it does.
Tracing routes…
What it does
Every recorded relationship this component is part of, grouped by its role. Plain wording comes first; the technical statement follows.
What acts on it
GalNAc-T2 initiates mucin-type O-glycosylation by transferring GalNAc from UDP-GalNAc to serine or threonine residues within proteins.
Experimental context and source evidence
- evidence_access
- Primary abstract
- experimental_model
- Human GalNAc-T2 structural and NMR enzymology.
- limitations
- Free dietary threonine is not the glycosyltransferase acceptor used in this protein-modification reaction.
- nutrient_topic
- L-Threonine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Threonine
- plain_language
- A threonine residue already built into a protein can carry a sugar.
- primary_references
- Structural Analysis of a GalNAc-T2 Mutant Reveals an Induced-Fit Catalytic Mechanism for GalNAc-Ts. · 2018 · https://pubmed.ncbi.nlm.nih.gov/29601100/ · DOI 10.1002/chem.201800701
L-Threonine: translation, intestinal barrier, metabolism and cross-nutrient mechanisms (2026-09-19) · lines 186–192
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human GalNAc-T2 structural and NMR enzymology. · source_derived_draft · unverified_draft
## l-threonine-galnt2-sugar A threonine residue already built into a protein can carry a sugar. GalNAc-T2 initiates mucin-type O-glycosylation by transferring GalNAc from UDP-GalNAc to serine or threonine residues within proteins. Model: Human GalNAc-T2 structural and NMR enzymology. Limitations: Free dietary threonine is not the glycosyltransferase acceptor used in this protein-modification reaction. Evidence access: Primary abstract Structural Analysis of a GalNAc-T2 Mutant Reveals an Induced-Fit Catalytic Mechanism for GalNAc-Ts. · 2018 · https://pubmed.ncbi.nlm.nih.gov/29601100/ · DOI 10.1002/chem.201800701
Complete structured claim and evidence
Where it participates (unsigned role)
GALNT2 F104S disrupted the UDP-GalNAc-dependent active conformation and peptide-substrate binding.
Experimental context and source evidence
- availability_state
- machinery_impairment Imported condition classification; unverified.
- evidence_access
- Primary abstract
- experimental_model
- Human mutant crystal structure, NMR and molecular-dynamics analysis.
- limitations
- No correction of this defect by threonine supplementation was demonstrated.
- nutrient_topic
- L-Threonine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Threonine
- plain_language
- A sugar donor and amino-acid-containing protein are insufficient if the modifying enzyme cannot bind correctly.
- primary_references
- Structural Analysis of a GalNAc-T2 Mutant Reveals an Induced-Fit Catalytic Mechanism for GalNAc-Ts. · 2018 · https://pubmed.ncbi.nlm.nih.gov/29601100/ · DOI 10.1002/chem.201800701
- trigger_kind
- machinery_impairment Imported condition classification; unverified.
L-Threonine: translation, intestinal barrier, metabolism and cross-nutrient mechanisms (2026-09-19) · lines 194–200
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human mutant crystal structure, NMR and molecular-dynamics analysis. · source_derived_draft · unverified_draft
## l-threonine-galnt2-f104s A sugar donor and amino-acid-containing protein are insufficient if the modifying enzyme cannot bind correctly. GALNT2 F104S disrupted the UDP-GalNAc-dependent active conformation and peptide-substrate binding. Model: Human mutant crystal structure, NMR and molecular-dynamics analysis. Limitations: No correction of this defect by threonine supplementation was demonstrated. Evidence access: Primary abstract Structural Analysis of a GalNAc-T2 Mutant Reveals an Induced-Fit Catalytic Mechanism for GalNAc-Ts. · 2018 · https://pubmed.ncbi.nlm.nih.gov/29601100/ · DOI 10.1002/chem.201800701
Complete structured claim and evidence
The events it takes part in
A mechanism often involves more than two components. These are the full events, with every participant and its role.
Situations it appears in
Low-supply and faulty-machinery situations recorded in the chapters where this component plays a part.
In the sources
Preserved passages that mention this component, quoted exactly. Open one to read it in context.
Open hypotheses
Proposed ideas that involve this component. They are labeled as hypotheses and do not change any recorded statement.
This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.