Component

Catalytically inactive RDH10

Activity-impaired recombinant RDH10 construct used to distinguish catalytic and activating roles.

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. RDH10 coexpression increased DHRS3 retinaldehyde reductase activity even when RDH10 itself was catalytically inactive.

    Experimental context and source evidence
    evidence_location
    Abstract
    experimental_model
    Human RDH10/DHRS3 coexpression in HEK293 and Sf9 cells, plus Dhrs3-null embryos.
    exposure
    Coexpression including inactive RDH10 constructs.
    limitations
    Does not identify an exact complex stoichiometry or require substrate channeling.
    nutrient_topic
    Vitamin A research collection; topical membership is not evidence of a direct dietary effect. · Vitamin A
    organism
    Homo sapiens recombinant proteins
    outcome
    RDH10 coexpression increased DHRS3 retinaldehyde reductase activity even when RDH10 itself was catalytically inactive.
    plain_language
    The partner enzyme also acts through a noncatalytic interaction.
    primary_references
    [va-adams-2014] The retinaldehyde reductase activity of DHRS3 is reciprocally activated by retinol dehydrogenase 10 to control retinoid homeostasis (2014). https://pmc.ncbi.nlm.nih.gov/articles/PMC4031538/ DOI: 10.1074/jbc.M114.552257
    tissue_or_cell_type
    Sf9 microsomes and HEK293 cells

    Vitamin A: forms, mechanisms, deficiency and excess (2026-09-17) · lines 531–543

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human RDH10/DHRS3 coexpression in HEK293 and Sf9 cells, plus Dhrs3-null embryos. · source_derived_draft · unverified_draft

    ### va-rdh10-activates-dhrs3 RDH10 coexpression increased DHRS3 retinaldehyde reductase activity even when RDH10 itself was catalytically inactive. Condition category: normal nutrient_topic: Vitamin A research collection; topical membership is not evidence of a direct dietary effect. plain_language: The partner enzyme also acts through a noncatalytic interaction. organism: Homo sapiens recombinant proteins tissue_or_cell_type: Sf9 microsomes and HEK293 cells experimental_model: Human RDH10/DHRS3 coexpression in HEK293 and Sf9 cells, plus Dhrs3-null embryos. limitations: Does not identify an exact complex stoichiometry or require substrate channeling. exposure: Coexpression including inactive RDH10 constructs. outcome: RDH10 coexpression increased DHRS3 retinaldehyde reductase activity even when RDH10 itself was catalytically inactive. evidence_location: Abstract [va-adams-2014] The retinaldehyde reductase activity of DHRS3 is reciprocally activated by retinol dehydrogenase 10 to control retinoid homeostasis (2014). https://pmc.ncbi.nlm.nih.gov/articles/PMC4031538/ DOI: 10.1074/jbc.M114.552257
    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