Component

DHRS3 Y188A

Catalytically inactive human DHRS3 substrate-site substitution.

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. DHRS3 coexpression enhanced RDH10 retinol dehydrogenase activity independently of DHRS3 catalytic activity.

    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 DHRS3 constructs.
    limitations
    Net retinoic-acid output depends on both opposing reactions and cellular conditions.
    nutrient_topic
    Vitamin A research collection; topical membership is not evidence of a direct dietary effect. · Vitamin A
    organism
    Homo sapiens recombinant proteins
    outcome
    DHRS3 coexpression enhanced RDH10 retinol dehydrogenase activity independently of DHRS3 catalytic activity.
    plain_language
    The two enzymes mutually stimulate one another.
    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 545–557

    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-dhrs3-activates-rdh10 DHRS3 coexpression enhanced RDH10 retinol dehydrogenase activity independently of DHRS3 catalytic activity. Condition category: normal nutrient_topic: Vitamin A research collection; topical membership is not evidence of a direct dietary effect. plain_language: The two enzymes mutually stimulate one another. 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: Net retinoic-acid output depends on both opposing reactions and cellular conditions. exposure: Coexpression including inactive DHRS3 constructs. outcome: DHRS3 coexpression enhanced RDH10 retinol dehydrogenase activity independently of DHRS3 catalytic activity. 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