Component
Human N-acetylgalactosamine-4-sulfatase / ARSB
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
In the vanadate-inhibited human ARSB structure, vanadate replaced sulfate at the active site and was covalently linked to the modified catalytic residue.
Experimental context and source evidence
- evidence_access
- Primary abstract
- experimental_model
- Human lysosomal sulfatase crystallography.
- limitations
- Structural inhibition is not evidence that oral vanadium causes mucopolysaccharidosis.
- nutrient_topic
- Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
- plain_language
- Vanadium’s targets extend beyond insulin signaling and ATPases.
- primary_references
- Structure of a human lysosomal sulfatase. · 1997 · https://pubmed.ncbi.nlm.nih.gov/9032078/ · DOI 10.1016/s0969-2126(97)00185-8
Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 270–276
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human lysosomal sulfatase crystallography. · source_derived_draft · unverified_draft
## vanadium-sulfatase-binding Vanadium’s targets extend beyond insulin signaling and ATPases. In the vanadate-inhibited human ARSB structure, vanadate replaced sulfate at the active site and was covalently linked to the modified catalytic residue. Model: Human lysosomal sulfatase crystallography. Limitations: Structural inhibition is not evidence that oral vanadium causes mucopolysaccharidosis. Evidence access: Primary abstract Structure of a human lysosomal sulfatase. · 1997 · https://pubmed.ncbi.nlm.nih.gov/9032078/ · DOI 10.1016/s0969-2126(97)00185-8
Complete structured claim and evidenceHuman ARSB crystallography identified calcium coordinated in the sulfate-containing catalytic site and an essential modified Cys91 residue.
Experimental context and source evidence
- evidence_access
- Primary abstract
- experimental_model
- Human lysosomal sulfatase structure.
- limitations
- Does not show calcium supplementation reverses vanadate inhibition.
- nutrient_topic
- Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
- plain_language
- Calcium and enzyme maturation define the machinery that the inhibitor encounters.
- primary_references
- Structure of a human lysosomal sulfatase. · 1997 · https://pubmed.ncbi.nlm.nih.gov/9032078/ · DOI 10.1016/s0969-2126(97)00185-8
Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 278–284
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human lysosomal sulfatase structure. · source_derived_draft · unverified_draft
## vanadium-sulfatase-calcium Calcium and enzyme maturation define the machinery that the inhibitor encounters. Human ARSB crystallography identified calcium coordinated in the sulfate-containing catalytic site and an essential modified Cys91 residue. Model: Human lysosomal sulfatase structure. Limitations: Does not show calcium supplementation reverses vanadate inhibition. Evidence access: Primary abstract Structure of a human lysosomal sulfatase. · 1997 · https://pubmed.ncbi.nlm.nih.gov/9032078/ · DOI 10.1016/s0969-2126(97)00185-8
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.