Component

Protein-bound lysine residue

Protein-bound site or substrate state, not free dietary L-lysine. Sequence and assay context limit the relationship.

6 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 acts on it

  1. HLCS transfers the activated biotin moiety to the epsilon-amino group of a specific lysine in a carboxylase biotin-acceptor domain.

    Human holocarboxylase synthetase / HLCS → Protein-bound lysine residue source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/biotin-research/19740736.fulltext.txt", "locator": "Exact primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d785655901465bc9798378986d954b87111e3bd73d6877d9d60ae3d95cac0a37", "start_char": 2587, "end_char": 3080, "text_sha256": "fa0ec838311a45e8ccebf38a73e340a46417eae6bc300064c1165a4a0b711889"}
    experimental_model
    Purified full-length and residue-58 human HLCS isoforms expressed in E. coli
    exposure
    Biotin/ATP activation and single-turnover biotin transfer
    limitations
    Minimal-substrate kinetics do not prove a universal tissue allocation hierarchy; expression host is not the protein species.
    nutrient_topic
    Biotin research collection; topical membership is not evidence of a direct dietary effect. · Biotin
    organism
    Homo sapiens
    plain_language
    Biotin becomes a tethered part of the enzyme; free lysine and enzyme-bound lysine are different entities.
    primary_references
    [b7-p19740736] Distinct amino termini of two human HCS isoforms influence biotin acceptor substrate recognition. (2009). https://pubmed.ncbi.nlm.nih.gov/19740736/ DOI: 10.1074/jbc.m109.046201
    tissue_or_cell_type
    Purified proteins and minimal biotin-accepting substrate

    Biotin: carboxylases, recycling, deficiency and nutrient interactions (2026-09-17) · lines 364–375

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified full-length and residue-58 human HLCS isoforms expressed in E. coli · source_derived_draft · unverified_draft

    ### b7-hlcs-lysine-transfer HLCS transfers the activated biotin moiety to the epsilon-amino group of a specific lysine in a carboxylase biotin-acceptor domain. Condition category: normal nutrient_topic: Biotin research collection; topical membership is not evidence of a direct dietary effect. plain_language: Biotin becomes a tethered part of the enzyme; free lysine and enzyme-bound lysine are different entities. organism: Homo sapiens tissue_or_cell_type: Purified proteins and minimal biotin-accepting substrate experimental_model: Purified full-length and residue-58 human HLCS isoforms expressed in E. coli limitations: Minimal-substrate kinetics do not prove a universal tissue allocation hierarchy; expression host is not the protein species. exposure: Biotin/ATP activation and single-turnover biotin transfer evidence_span: {"source_cache": "artifacts/biotin-research/19740736.fulltext.txt", "locator": "Exact primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d785655901465bc9798378986d954b87111e3bd73d6877d9d60ae3d95cac0a37", "start_char": 2587, "end_char": 3080, "text_sha256": "fa0ec838311a45e8ccebf38a73e340a46417eae6bc300064c1165a4a0b711889"} [b7-p19740736] Distinct amino termini of two human HCS isoforms influence biotin acceptor substrate recognition. (2009). https://pubmed.ncbi.nlm.nih.gov/19740736/ DOI: 10.1074/jbc.m109.046201
    Complete structured claim and evidence

  2. EP300 transfers an acetyl group from acetyl-CoA to a protein lysine side chain.

    EP300 → Protein-bound lysine residue source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Human p300 catalytic-domain structure and biochemical assays.
    limitations
    This reaction modifies lysine already in a protein. It does not show that extra oral lysine increases the reaction or improves a clinical outcome.
    organism
    Human
    plain_language
    Acetyl groups can be written onto lysines already present in proteins.
    primary_references
    [p300-2008] The structural basis of protein acetylation by the p300/CBP transcriptional coactivator (2008). https://pubmed.ncbi.nlm.nih.gov/18273021/ DOI: 10.1038/nature06546
    tissue_or_cell_type
    Not specified as a whole tissue; see experimental model.

    L-Lysine: mechanism-first literature curation (2026-09-17) · lines 527–535

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human p300 catalytic-domain structure and biochemical assays. · source_derived_draft · unverified_draft

    ### ep300-lysine-acetylation EP300 transfers an acetyl group from acetyl-CoA to a protein lysine side chain. Plain language: Acetyl groups can be written onto lysines already present in proteins. Condition category: normal organism: Human tissue_or_cell_type: Not specified as a whole tissue; see experimental model. experimental_model: Human p300 catalytic-domain structure and biochemical assays. limitations: This reaction modifies lysine already in a protein. It does not show that extra oral lysine increases the reaction or improves a clinical outcome. [p300-2008] The structural basis of protein acetylation by the p300/CBP transcriptional coactivator (2008). https://pubmed.ncbi.nlm.nih.gov/18273021/ DOI: 10.1038/nature06546
    Complete structured claim and evidence

  3. At the cytosolic 80S ribosome, the alpha-amino group of A-site lysyl-tRNA accepts the P-site nascent peptide, incorporating lysine into a peptide bond; the extended chain remains attached to the incoming tRNA.

    Lysyl-tRNA-Lys → Protein-bound lysine residue source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Human cell lysate translation products; rabbit reticulocyte ribosome-nascent-chain cryo-EM
    limitations
    AAG-coded translation controls directly show elongation. The structural experiment concerns poly(A)-dependent stalling; it does not establish a dietary deficiency response or instant release of the lysine-carrying tRNA.
    organism
    Homo sapiens and Oryctolagus cuniculus
    plain_language
    The ribosome adds charged lysine to a growing protein chain.
    primary_references
    [chandrasekaran2019] Mechanism of ribosome stalling during translation of a poly(A) tail (2019). https://pmc.ncbi.nlm.nih.gov/articles/PMC6900289/ DOI: 10.1038/s41594-019-0331-x
    tissue_or_cell_type
    Cytosolic translation; cultured-cell lysate and reticulocyte lysate

    L-Lysine: mechanism-first literature curation (2026-09-17) · lines 347–355

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human cell lysate translation products; rabbit reticulocyte ribosome-nascent-chain cryo-EM · source_derived_draft · unverified_draft

    ### ribosomal-lysine-incorporation At the cytosolic 80S ribosome, the alpha-amino group of A-site lysyl-tRNA accepts the P-site nascent peptide, incorporating lysine into a peptide bond; the extended chain remains attached to the incoming tRNA. Plain language: The ribosome adds charged lysine to a growing protein chain. Condition category: normal organism: Homo sapiens and Oryctolagus cuniculus tissue_or_cell_type: Cytosolic translation; cultured-cell lysate and reticulocyte lysate experimental_model: Human cell lysate translation products; rabbit reticulocyte ribosome-nascent-chain cryo-EM limitations: AAG-coded translation controls directly show elongation. The structural experiment concerns poly(A)-dependent stalling; it does not establish a dietary deficiency response or instant release of the lysine-carrying tRNA. [chandrasekaran2019] Mechanism of ribosome stalling during translation of a poly(A) tail (2019). https://pmc.ncbi.nlm.nih.gov/articles/PMC6900289/ DOI: 10.1038/s41594-019-0331-x
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. The human ACC1 biotin-carrier domain contains biotin covalently attached to Lys786.

    Human acetyl-CoA carboxylase 1 / ACACA → Human ACC1 biotinylated at Lys786 source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/biotin-research/39383219.fulltext.txt", "locator": "Exact primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "5f7d3cd6a5865a03b8dc9c510f60249ee2c9f6516773780e5d7b4aef0a9b2db8", "start_char": 17700, "end_char": 18021, "text_sha256": "577b5c24795f7637a47e725c7e87ae9632c6aa96e74424b66d14ccd76a87e3bb"}
    experimental_model
    Cryo-EM of endogenous and recombinant human ACC1 filaments
    exposure
    Inactive substrate-containing and dephosphorylated/citrate-treated states
    limitations
    Filament presence alone does not mean enzyme activation; the paper resolved both active and inactive arrangements.
    nutrient_topic
    Biotin research collection; topical membership is not evidence of a direct dietary effect. · Biotin
    organism
    Homo sapiens
    plain_language
    Biotin is attached at a specific amino-acid site on ACC1.
    primary_references
    [b7-p39383219] Filament structures unveil the dynamic organization of human acetyl-CoA carboxylase. (2024). https://pubmed.ncbi.nlm.nih.gov/39383219/ DOI: 10.1126/sciadv.ado4880
    tissue_or_cell_type
    Purified human ACC1

    Biotin: carboxylases, recycling, deficiency and nutrient interactions (2026-09-17) · lines 650–661

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Cryo-EM of endogenous and recombinant human ACC1 filaments · source_derived_draft · unverified_draft

    ### b7-acc1-k786 The human ACC1 biotin-carrier domain contains biotin covalently attached to Lys786. Condition category: normal nutrient_topic: Biotin research collection; topical membership is not evidence of a direct dietary effect. plain_language: Biotin is attached at a specific amino-acid site on ACC1. organism: Homo sapiens tissue_or_cell_type: Purified human ACC1 experimental_model: Cryo-EM of endogenous and recombinant human ACC1 filaments limitations: Filament presence alone does not mean enzyme activation; the paper resolved both active and inactive arrangements. exposure: Inactive substrate-containing and dephosphorylated/citrate-treated states evidence_span: {"source_cache": "artifacts/biotin-research/39383219.fulltext.txt", "locator": "Exact primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "5f7d3cd6a5865a03b8dc9c510f60249ee2c9f6516773780e5d7b4aef0a9b2db8", "start_char": 17700, "end_char": 18021, "text_sha256": "577b5c24795f7637a47e725c7e87ae9632c6aa96e74424b66d14ccd76a87e3bb"} [b7-p39383219] Filament structures unveil the dynamic organization of human acetyl-CoA carboxylase. (2024). https://pubmed.ncbi.nlm.nih.gov/39383219/ DOI: 10.1126/sciadv.ado4880
    Complete structured claim and evidence

  2. ACLY silencing reduced acetylation of the core histones assayed in HCT116 cells.

    Human ATP-citrate lyase / ACLY → Core histone lysine acetylation source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    cross_nutrient
    true
    evidence_location
    BioC text lines 11, 17, 51; Fig. 2A,E
    experimental_model
    ACLY siRNA versus control
    exposure
    72-hour siRNA treatment.
    limitations
    Tubulin acetylation was not comparably reduced. This is a source-specific cellular result, not a universal block of protein acetylation. This experiment does not establish a dietary pantothenate threshold or benefit from B5 supplementation.
    nutrient_topic
    Pantothenic acid (vitamin B5) research collection; topical membership is not evidence of a direct dietary effect. · Pantothenate (vitamin B5)
    organism
    Homo sapiens
    plain_language
    Histone acetylation depended partly on this source of acetyl-CoA in colon-cancer cells.
    primary_references
    [b5-met-chromatin2009] ATP-citrate lyase links cellular metabolism to histone acetylation. (2009). https://pubmed.ncbi.nlm.nih.gov/19461003/ DOI: 10.1126/science.1164097
    tissue_or_cell_type
    HCT116 cells and acid-extracted histones
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Pantothenic acid (vitamin B5): coenzyme A, deficiency and nutrient interactions (2026-09-17) · lines 991–1003

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · ACLY siRNA versus control · source_derived_draft · unverified_draft

    ### b5-met-acly-hct-histones ACLY silencing reduced acetylation of the core histones assayed in HCT116 cells. Condition category: machinery_impairment nutrient_topic: Pantothenic acid (vitamin B5) research collection; topical membership is not evidence of a direct dietary effect. plain_language: Histone acetylation depended partly on this source of acetyl-CoA in colon-cancer cells. organism: Homo sapiens tissue_or_cell_type: HCT116 cells and acid-extracted histones experimental_model: ACLY siRNA versus control limitations: Tubulin acetylation was not comparably reduced. This is a source-specific cellular result, not a universal block of protein acetylation. This experiment does not establish a dietary pantothenate threshold or benefit from B5 supplementation. exposure: 72-hour siRNA treatment. cross_nutrient: true evidence_location: BioC text lines 11, 17, 51; Fig. 2A,E [b5-met-chromatin2009] ATP-citrate lyase links cellular metabolism to histone acetylation. (2009). https://pubmed.ncbi.nlm.nih.gov/19461003/ DOI: 10.1126/science.1164097
    Complete structured claim and evidence

  3. Serum-induced histone acetylation in immortalized mouse embryonic fibroblasts depended on glucose availability and was prevented by Acly silencing.

    D-glucose → Core histone lysine acetylation source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    true
    evidence_location
    BioC text line 21; Fig. 3B–C
    experimental_model
    Serum stimulation with/without glucose and Acly siRNA
    exposure
    Experimental serum stimulation and glucose withdrawal; no selective pantothenate deprivation.
    limitations
    Glucose was the experimentally varied fuel. This is not evidence of B5 deficiency; cellular acetyl-CoA sources differ by context. This experiment does not establish a dietary pantothenate threshold or benefit from B5 supplementation.
    nutrient_topic
    Pantothenic acid (vitamin B5) research collection; topical membership is not evidence of a direct dietary effect. · Pantothenate (vitamin B5)
    organism
    Mus musculus
    plain_language
    Glucose supply affected histone acetylation through an acetyl-CoA-producing enzyme in this cell model.
    primary_references
    [b5-met-chromatin2009] ATP-citrate lyase links cellular metabolism to histone acetylation. (2009). https://pubmed.ncbi.nlm.nih.gov/19461003/ DOI: 10.1126/science.1164097
    tissue_or_cell_type
    Immortalized mouse embryonic fibroblasts

    Pantothenic acid (vitamin B5): coenzyme A, deficiency and nutrient interactions (2026-09-17) · lines 1019–1031

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Serum stimulation with/without glucose and Acly siRNA · source_derived_draft · unverified_draft

    ### b5-met-glucose-acly-histones Serum-induced histone acetylation in immortalized mouse embryonic fibroblasts depended on glucose availability and was prevented by Acly silencing. Condition category: normal nutrient_topic: Pantothenic acid (vitamin B5) research collection; topical membership is not evidence of a direct dietary effect. plain_language: Glucose supply affected histone acetylation through an acetyl-CoA-producing enzyme in this cell model. organism: Mus musculus tissue_or_cell_type: Immortalized mouse embryonic fibroblasts experimental_model: Serum stimulation with/without glucose and Acly siRNA limitations: Glucose was the experimentally varied fuel. This is not evidence of B5 deficiency; cellular acetyl-CoA sources differ by context. This experiment does not establish a dietary pantothenate threshold or benefit from B5 supplementation. exposure: Experimental serum stimulation and glucose withdrawal; no selective pantothenate deprivation. cross_nutrient: true evidence_location: BioC text line 21; Fig. 3B–C [b5-met-chromatin2009] ATP-citrate lyase links cellular metabolism to histone acetylation. (2009). https://pubmed.ncbi.nlm.nih.gov/19461003/ DOI: 10.1126/science.1164097
    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.

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