Component

Short-chain enoyl-CoA hydratase / ECHS1

Independent protein record; interpretation is limited by each linked claim and its study context.

3 recorded relationships. Experimental role, claim status and evidence remain attached to each record.

Read recorded mechanisms Open recursive mind map

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. ECHS1-deficient patients showed a dominant valine-metabolism defect rather than the expected isolated isoleucine block; liver retained tiglyl-CoA hydration capacity.

    Short-chain enoyl-CoA hydratase / ECHS1 → Tiglyl-CoA processing capacity in human tissues source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary full text
    experimental_model
    Four-patient biochemical study with tissue enzyme comparisons.
    limitations
    Does not establish the same backup capacity in every cell type.
    nutrient_topic
    L-Isoleucine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Isoleucine
    plain_language
    A pathway diagram alone can overstate an enzyme as an unavoidable gate.
    primary_references
    Clinical and biochemical characterization of four patients with mutations in ECHS1. · 2015 · https://pubmed.ncbi.nlm.nih.gov/26081110/ · DOI 10.1186/s13023-015-0290-1
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    L-Isoleucine: transport, translation, catabolism and cross-nutrient mechanisms (2026-09-19) · lines 202–208

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Four-patient biochemical study with tissue enzyme comparisons. · source_derived_draft · unverified_draft

    ## isoleucine-echs1-boundary A pathway diagram alone can overstate an enzyme as an unavoidable gate. ECHS1-deficient patients showed a dominant valine-metabolism defect rather than the expected isolated isoleucine block; liver retained tiglyl-CoA hydration capacity. Model: Four-patient biochemical study with tissue enzyme comparisons. Limitations: Does not establish the same backup capacity in every cell type. Evidence access: Primary full text Clinical and biochemical characterization of four patients with mutations in ECHS1. · 2015 · https://pubmed.ncbi.nlm.nih.gov/26081110/ · DOI 10.1186/s13023-015-0290-1
    Complete structured claim and evidence

  2. Human fibroblast and liver assays measured tiglyl-CoA hydration in the isoleucine branch; residual activity persisted despite ECHS1 deficiency, indicating overlapping hydratase capacity.

    Short-chain enoyl-CoA hydratase / ECHS1 → Tiglyl-CoA source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    Human ECHS1-deficient fibroblasts and liver; substrate-selective enzyme assays.
    limitations
    ECHS1 activity does not establish that it is the sole required isoleucine hydratase.
    nutrient_topic
    L-Isoleucine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Isoleucine
    plain_language
    A reaction can have backup enzyme capacity in a tissue.
    primary_references
    Clinical and biochemical characterization of four patients with mutations in ECHS1. · 2015 · https://pubmed.ncbi.nlm.nih.gov/26081110/ · DOI 10.1186/s13023-015-0290-1

    L-Isoleucine: transport, translation, catabolism and cross-nutrient mechanisms (2026-09-19) · lines 194–200

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human ECHS1-deficient fibroblasts and liver; substrate-selective enzyme assays. · source_derived_draft · unverified_draft

    ## isoleucine-tiglyl-hydration A reaction can have backup enzyme capacity in a tissue. Human fibroblast and liver assays measured tiglyl-CoA hydration in the isoleucine branch; residual activity persisted despite ECHS1 deficiency, indicating overlapping hydratase capacity. Model: Human ECHS1-deficient fibroblasts and liver; substrate-selective enzyme assays. Limitations: ECHS1 activity does not establish that it is the sole required isoleucine hydratase. Evidence access: Primary full text Clinical and biochemical characterization of four patients with mutations in ECHS1. · 2015 · https://pubmed.ncbi.nlm.nih.gov/26081110/ · DOI 10.1186/s13023-015-0290-1
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Short-chain enoyl-CoA hydratase ECHS1 hydrates trans-crotonyl-CoA to (S)-3-hydroxybutyryl-CoA.

    Crotonyl-CoA → (S)-3-Hydroxybutyryl-CoA source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Crotonyl-CoA hydratase assays in control human fibroblasts
    limitations
    This shared short-chain reaction can process lysine-derived crotonyl-CoA, but the assay does not trace its carbon from lysine. Disease results are not used to label the control reaction as machinery impairment.
    organism
    Homo sapiens
    plain_language
    Water is added across the four-carbon intermediate's double bond.
    primary_references
    [ferdinandusse2015] Clinical and biochemical characterization of four patients with mutations in ECHS1 (2015). https://link.springer.com/article/10.1186/s13023-015-0290-1 DOI: 10.1186/s13023-015-0290-1
    tissue_or_cell_type
    Fibroblasts; mitochondrial enzyme

    L-Lysine: mechanism-first literature curation (2026-09-17) · lines 357–365

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Crotonyl-CoA hydratase assays in control human fibroblasts · source_derived_draft · unverified_draft

    ### echs1-crotonyl-coa-hydration Short-chain enoyl-CoA hydratase ECHS1 hydrates trans-crotonyl-CoA to (S)-3-hydroxybutyryl-CoA. Plain language: Water is added across the four-carbon intermediate's double bond. Condition category: normal organism: Homo sapiens tissue_or_cell_type: Fibroblasts; mitochondrial enzyme experimental_model: Crotonyl-CoA hydratase assays in control human fibroblasts limitations: This shared short-chain reaction can process lysine-derived crotonyl-CoA, but the assay does not trace its carbon from lysine. Disease results are not used to label the control reaction as machinery impairment. [ferdinandusse2015] Clinical and biochemical characterization of four patients with mutations in ECHS1 (2015). https://link.springer.com/article/10.1186/s13023-015-0290-1 DOI: 10.1186/s13023-015-0290-1
    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