Component

Crotonyl-CoA

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

4 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. 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

What acts on it

  1. FAD-containing human GCDH dehydrogenates glutaryl-CoA through glutaconyl-CoA and decarboxylates it to crotonyl-CoA.

    Glutaryl-CoA → Crotonyl-CoA source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Human GCDH crystallography and substrate-mechanism analysis
    limitations
    The downstream shared ECHS1/HADH/ACAT1 reactions are separate records; these individual enzyme assays do not measure the full lysine-derived flux in a person.
    organism
    Homo sapiens
    plain_language
    GCDH shortens the lysine-derived carbon chain.
    primary_references
    [fu2004] Crystal Structures of Human Glutaryl-CoA Dehydrogenase with and without an Alternate Substrate: Structural Bases of Dehydrogenation and Decarboxylation Reactions (2004). https://pubs.acs.org/doi/10.1021/bi049290c DOI: 10.1021/bi049290c
    tissue_or_cell_type
    Mitochondrial matrix

    L-Lysine: mechanism-first literature curation (2026-09-17) · lines 136–144

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human GCDH crystallography and substrate-mechanism analysis · source_derived_draft · unverified_draft

    ### gcdh-crotonyl-coa FAD-containing human GCDH dehydrogenates glutaryl-CoA through glutaconyl-CoA and decarboxylates it to crotonyl-CoA. Plain language: GCDH shortens the lysine-derived carbon chain. Condition category: normal organism: Homo sapiens tissue_or_cell_type: Mitochondrial matrix experimental_model: Human GCDH crystallography and substrate-mechanism analysis limitations: The downstream shared ECHS1/HADH/ACAT1 reactions are separate records; these individual enzyme assays do not measure the full lysine-derived flux in a person. [fu2004] Crystal Structures of Human Glutaryl-CoA Dehydrogenase with and without an Alternate Substrate: Structural Bases of Dehydrogenation and Decarboxylation Reactions (2004). https://pubs.acs.org/doi/10.1021/bi049290c DOI: 10.1021/bi049290c
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Butyrate inhibited histone decrotonylation in the study linking class-I HDAC activity to crotonylation; separate mouse microbiota depletion altered colonic crotonyl marks.

    Butyrate → Histone crotonylation in human cell and biochemical assays source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract and full-text HCT116/HDAC assay results
    experimental_model
    Human cell/biochemical assays and separately analyzed mouse colon.
    limitations
    Crotonylation is a distinct modification from acetylation, butyrylation and beta-hydroxybutyrylation.
    nutrient_topic
    Butyrate collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Butyrate
    plain_language
    Its epigenetic effects extended beyond acetylation.
    primary_references
    Microbiota derived short chain fatty acids promote histone crotonylation in the colon through histone deacetylases. · 2018 · https://pubmed.ncbi.nlm.nih.gov/29317660/ · DOI 10.1038/s41467-017-02651-5

    Butyrate: microbial production, fuel use, signaling and nutrient interactions (2026-09-19) · lines 302–308

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human cell/biochemical assays and separately analyzed mouse colon. · source_derived_draft · unverified_draft

    ## butyrate-decrotonylation Its epigenetic effects extended beyond acetylation. Butyrate inhibited histone decrotonylation in the study linking class-I HDAC activity to crotonylation; separate mouse microbiota depletion altered colonic crotonyl marks. Model: Human cell/biochemical assays and separately analyzed mouse colon. Limitations: Crotonylation is a distinct modification from acetylation, butyrylation and beta-hydroxybutyrylation. Evidence access: Primary abstract and full-text HCT116/HDAC assay results Microbiota derived short chain fatty acids promote histone crotonylation in the colon through histone deacetylases. · 2018 · https://pubmed.ncbi.nlm.nih.gov/29317660/ · DOI 10.1038/s41467-017-02651-5
    Complete structured claim and evidence

  2. BbuA converted gamma-butyrobetainyl-CoA to TMA and crotonyl-CoA in the reconstituted anaerobic pathway.

    Emergencia timonensis BbuA / GbuA TMA-generating enzyme → Gamma-butyrobetainyl-CoA source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text and pathway reconstitution
    experimental_model
    E. timonensis BbuA biochemical characterization.
    limitations
    Flavin participation is supported; detailed catalytic chemistry remained proposed in this paper.
    nutrient_topic
    L-Carnitine collection; isomer, preparation, species, exposure and manipulation remain explicit. · L-Carnitine
    plain_language
    A microbial enzyme releases the trimethylamine group.
    primary_references
    Elucidation of an anaerobic pathway for metabolism of l-carnitine-derived γ-butyrobetaine to trimethylamine in human gut bacteria. · 2021 · https://pubmed.ncbi.nlm.nih.gov/34362844/ · DOI 10.1073/pnas.2101498118

    L-Carnitine: synthesis, acyl-group transport, fuel selection and nutrient interactions (2026-09-19) · lines 378–384

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · E. timonensis BbuA biochemical characterization. · source_derived_draft · unverified_draft

    ## l-carnitine-bbua-lyase A microbial enzyme releases the trimethylamine group. BbuA converted gamma-butyrobetainyl-CoA to TMA and crotonyl-CoA in the reconstituted anaerobic pathway. Model: E. timonensis BbuA biochemical characterization. Limitations: Flavin participation is supported; detailed catalytic chemistry remained proposed in this paper. Evidence access: Primary full text and pathway reconstitution Elucidation of an anaerobic pathway for metabolism of l-carnitine-derived γ-butyrobetaine to trimethylamine in human gut bacteria. · 2021 · https://pubmed.ncbi.nlm.nih.gov/34362844/ · DOI 10.1073/pnas.2101498118
    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