Component

11-cis-retinol dehydrogenase / RDH5

Cis-retinol oxidation enzyme.

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.

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

What it acts on

  1. Bovine RDH5 expressed in COS cells oxidized 11-cis-retinol using NAD+; NADP did not support the tested activity.

    11-cis-retinol dehydrogenase / RDH5 → 11-cis-retinal source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Recombinant p32/RDH5 activity assay
    limitations
    Cofactor specificity is biochemical; no niacin-deficiency phenotype was tested.
    nutrient_topic
    Vitamin A research collection; topical membership is not evidence of a direct dietary effect. · Vitamin A
    organism
    Bos taurus protein; COS cells
    plain_language
    RDH5 oxidizes the cis alcohol into the visual chromophore.
    primary_references
    [simon-1995] The retinal pigment epithelial-specific 11-cis retinol dehydrogenase belongs to the family of short chain alcohol dehydrogenases (1995). https://pubmed.ncbi.nlm.nih.gov/7836368/ DOI: 10.1074/jbc.270.3.1107
    tissue_or_cell_type
    RPE-derived enzyme

    Vitamin A: forms, mechanisms, deficiency and excess (2026-09-17) · lines 723–732

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant p32/RDH5 activity assay · source_derived_draft · unverified_draft

    ### a-vision-rdh5-oxidation Bovine RDH5 expressed in COS cells oxidized 11-cis-retinol using NAD+; NADP did not support the tested activity. Condition category: normal nutrient_topic: Vitamin A research collection; topical membership is not evidence of a direct dietary effect. plain_language: RDH5 oxidizes the cis alcohol into the visual chromophore. organism: Bos taurus protein; COS cells tissue_or_cell_type: RPE-derived enzyme experimental_model: Recombinant p32/RDH5 activity assay limitations: Cofactor specificity is biochemical; no niacin-deficiency phenotype was tested. [simon-1995] The retinal pigment epithelial-specific 11-cis retinol dehydrogenase belongs to the family of short chain alcohol dehydrogenases (1995). https://pubmed.ncbi.nlm.nih.gov/7836368/ DOI: 10.1074/jbc.270.3.1107
    Complete structured claim and evidence

What acts on it

  1. RDH5 variants segregating with fundus albipunctatus showed lower recombinant enzyme activity than wild type.

    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    experimental_model
    Patient genetics and recombinant enzyme assay
    limitations
    Variants were evaluated in a small number of families.
    nutrient_topic
    Vitamin A research collection; topical membership is not evidence of a direct dietary effect. · Vitamin A
    organism
    Homo sapiens
    plain_language
    The inherited protein changes weaken the recycling reaction.
    primary_references
    [yamamoto-1999] Mutations in the gene encoding 11-cis retinol dehydrogenase cause delayed dark adaptation and fundus albipunctatus (1999). https://pubmed.ncbi.nlm.nih.gov/10369264/ DOI: 10.1038/9707
    tissue_or_cell_type
    RPE enzyme model
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Vitamin A: forms, mechanisms, deficiency and excess (2026-09-17) · lines 734–743

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Patient genetics and recombinant enzyme assay · source_derived_draft · unverified_draft

    ### a-vision-rdh5-mutant-activity RDH5 variants segregating with fundus albipunctatus showed lower recombinant enzyme activity than wild type. Condition category: machinery_impairment nutrient_topic: Vitamin A research collection; topical membership is not evidence of a direct dietary effect. plain_language: The inherited protein changes weaken the recycling reaction. organism: Homo sapiens tissue_or_cell_type: RPE enzyme model experimental_model: Patient genetics and recombinant enzyme assay limitations: Variants were evaluated in a small number of families. [yamamoto-1999] Mutations in the gene encoding 11-cis retinol dehydrogenase cause delayed dark adaptation and fundus albipunctatus (1999). https://pubmed.ncbi.nlm.nih.gov/10369264/ DOI: 10.1038/9707
    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