Component

Stearoyl-CoA

Context-specific entity; species, compartment and exposure are stated on each claim.

1 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.

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.

Recorded relationships

Where it participates (unsigned role)

  1. Reconstituting the non-heme iron and heme sites of a human SCD/cytochrome-b5 proteoliposome complex restored conversion of stearoyl-CoA to oleoyl-CoA.

    Human stearoyl-CoA desaturase / SCD → Oleoyl-CoA source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human proteins translated in wheat-germ extract and assembled in liposomes.
    limitations
    The tested substrate was stearoyl-CoA, not vaccenic acid; nutrient status was not tested.
    nutrient_topic
    CLA collection; isomer, preparation, species, exposure and manipulation remain explicit. · Conjugated linoleic acid / CLA isomer family
    plain_language
    The desaturation machinery needs metal-containing partners.
    primary_references
    Wheat germ cell-free translation, purification, and assembly of a functional human stearoyl-CoA desaturase complex. · 2008 · https://pubmed.ncbi.nlm.nih.gov/18765284/ · DOI 10.1016/j.pep.2008.08.002

    Conjugated linoleic acid: isomers, signaling, nutrient interactions and discovery (2026-09-19) · lines 46–52

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human proteins translated in wheat-germ extract and assembled in liposomes. · source_derived_draft · unverified_draft

    ## cla-scd-cofactors The desaturation machinery needs metal-containing partners. Reconstituting the non-heme iron and heme sites of a human SCD/cytochrome-b5 proteoliposome complex restored conversion of stearoyl-CoA to oleoyl-CoA. Model: Human proteins translated in wheat-germ extract and assembled in liposomes. Limitations: The tested substrate was stearoyl-CoA, not vaccenic acid; nutrient status was not tested. Evidence access: Primary abstract Wheat germ cell-free translation, purification, and assembly of a functional human stearoyl-CoA desaturase complex. · 2008 · https://pubmed.ncbi.nlm.nih.gov/18765284/ · DOI 10.1016/j.pep.2008.08.002
    Complete structured claim and evidence

In the sources

Preserved passages that mention this component, quoted exactly. Open one to read it in context.

    This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.

    Evidence, AI assistance and curation standards