Component

Human pyruvate carboxylase / PC

Human pyruvate carboxylase / PC. Species, exposure and limitations are retained in each linked claim.

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 it acts on

  1. Genetic depletion of PC in human islets reduced glutathione and the GSH/GSSG ratio under nitrosative stress.

    Human pyruvate carboxylase / PC → Human pancreatic-islet glutathione synthesis source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_span
    {"source_cache": "artifacts/biotin-research/34818536.fulltext.txt", "locator": "Exact primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "48bcb3951c9b630862fdda839e0a54b80abe9e2cf2e79d0bfb7547e2af317523", "start_char": 35800, "end_char": 36138, "text_sha256": "b1dd7e5022ba64d19114d853d2f75c43e061cdca76e1938e95c19379e96c3933"}
    experimental_model
    Primary human-islet tracer metabolomics and PC knockdown under inflammatory/nitrosative stress
    exposure
    Glucose tracer, PC knockdown and nitric-oxide donor exposure
    limitations
    Genetic perturbation of PC in isolated islets is not dietary biotin depletion or evidence that biotin supplements raise glutathione in replete people.
    nutrient_topic
    Biotin research collection; topical membership is not evidence of a direct dietary effect. · Biotin
    organism
    Homo sapiens
    plain_language
    PC connects carbon metabolism to the cell’s ability to maintain glutathione.
    primary_references
    [b7-p34818536] Glucose metabolism and pyruvate carboxylase enhance glutathione synthesis and restrict oxidative stress in pancreatic islets. (2021). https://pubmed.ncbi.nlm.nih.gov/34818536/ DOI: 10.1016/j.celrep.2021.110037
    tissue_or_cell_type
    Primary human pancreatic islets
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Biotin: carboxylases, recycling, deficiency and nutrient interactions (2026-09-17) · lines 871–882

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Primary human-islet tracer metabolomics and PC knockdown under inflammatory/nitrosative stress · source_derived_draft · unverified_draft

    ### b7-pc-islet-gsh Genetic depletion of PC in human islets reduced glutathione and the GSH/GSSG ratio under nitrosative stress. Condition category: machinery_impairment nutrient_topic: Biotin research collection; topical membership is not evidence of a direct dietary effect. plain_language: PC connects carbon metabolism to the cell’s ability to maintain glutathione. organism: Homo sapiens tissue_or_cell_type: Primary human pancreatic islets experimental_model: Primary human-islet tracer metabolomics and PC knockdown under inflammatory/nitrosative stress limitations: Genetic perturbation of PC in isolated islets is not dietary biotin depletion or evidence that biotin supplements raise glutathione in replete people. exposure: Glucose tracer, PC knockdown and nitric-oxide donor exposure evidence_span: {"source_cache": "artifacts/biotin-research/34818536.fulltext.txt", "locator": "Exact primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "48bcb3951c9b630862fdda839e0a54b80abe9e2cf2e79d0bfb7547e2af317523", "start_char": 35800, "end_char": 36138, "text_sha256": "b1dd7e5022ba64d19114d853d2f75c43e061cdca76e1938e95c19379e96c3933"} [b7-p34818536] Glucose metabolism and pyruvate carboxylase enhance glutathione synthesis and restrict oxidative stress in pancreatic islets. (2021). https://pubmed.ncbi.nlm.nih.gov/34818536/ DOI: 10.1016/j.celrep.2021.110037
    Complete structured claim and evidence

  2. Human PC catalyzes two-step pyruvate carboxylation to oxaloacetate.

    Human pyruvate carboxylase / PC → Pyruvate source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/biotin-research/36283412.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "2a5fb8ec1c27e243b8c8ba158f2c58ab1592d9895eecf16438175b2a5778de15", "start_char": 0, "end_char": 1060, "text_sha256": "2a5fb8ec1c27e243b8c8ba158f2c58ab1592d9895eecf16438175b2a5778de15"}
    experimental_model
    Time-resolved cryo-EM and biochemical analysis of human PC
    exposure
    Pyruvate, ATP and acetyl-CoA catalytic conditions
    limitations
    Purified-enzyme regulation is not evidence that consuming B5 or biotin stimulates this pathway in every tissue.
    nutrient_topic
    Biotin research collection; topical membership is not evidence of a direct dietary effect. · Biotin
    organism
    Homo sapiens
    plain_language
    PC replenishes a key carbon molecule used by several metabolic pathways.
    primary_references
    [b7-p36283412] Mechanistic insight into allosteric activation of human pyruvate carboxylase by acetyl-CoA. (2022). https://pubmed.ncbi.nlm.nih.gov/36283412/ DOI: 10.1016/j.molcel.2022.09.033
    tissue_or_cell_type
    Purified human pyruvate carboxylase

    Biotin: carboxylases, recycling, deficiency and nutrient interactions (2026-09-17) · lines 546–557

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Time-resolved cryo-EM and biochemical analysis of human PC · source_derived_draft · unverified_draft

    ### b7-pc-reaction Human PC catalyzes two-step pyruvate carboxylation to oxaloacetate. Condition category: normal nutrient_topic: Biotin research collection; topical membership is not evidence of a direct dietary effect. plain_language: PC replenishes a key carbon molecule used by several metabolic pathways. organism: Homo sapiens tissue_or_cell_type: Purified human pyruvate carboxylase experimental_model: Time-resolved cryo-EM and biochemical analysis of human PC limitations: Purified-enzyme regulation is not evidence that consuming B5 or biotin stimulates this pathway in every tissue. exposure: Pyruvate, ATP and acetyl-CoA catalytic conditions evidence_span: {"source_cache": "artifacts/biotin-research/36283412.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "2a5fb8ec1c27e243b8c8ba158f2c58ab1592d9895eecf16438175b2a5778de15", "start_char": 0, "end_char": 1060, "text_sha256": "2a5fb8ec1c27e243b8c8ba158f2c58ab1592d9895eecf16438175b2a5778de15"} [b7-p36283412] Mechanistic insight into allosteric activation of human pyruvate carboxylase by acetyl-CoA. (2022). https://pubmed.ncbi.nlm.nih.gov/36283412/ DOI: 10.1016/j.molcel.2022.09.033
    Complete structured claim and evidence

  3. The human PC C-terminal structure displayed a conserved tetrameric arrangement, with a PC tetramerization domain identified by structural and mutagenesis analysis.

    Human pyruvate carboxylase / PC → Human pyruvate carboxylase / PC source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/biotin-research/18297087.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "64ad42b855e8e31bb8103ad2740baab36988d47779218fbbf19b13f34f4a4d10", "start_char": 0, "end_char": 1026, "text_sha256": "64ad42b855e8e31bb8103ad2740baab36988d47779218fbbf19b13f34f4a4d10"}
    experimental_model
    Crystal structures of human PC lacking the BC domain and full-length S. aureus PC; mutagenesis
    exposure
    Structural and mutagenesis experiments
    limitations
    The human structure was a C-terminal fragment, not intact human PC; bacterial domain positions must not be silently assigned to human enzyme.
    nutrient_topic
    Biotin research collection; topical membership is not evidence of a direct dietary effect. · Biotin
    organism
    Homo sapiens; Staphylococcus aureus
    plain_language
    Enzyme assembly matters as well as the availability of biotin.
    primary_references
    [b7-p18297087] Crystal structures of human and Staphylococcus aureus pyruvate carboxylase and molecular insights into the carboxyltransfer reaction. (2008). https://pubmed.ncbi.nlm.nih.gov/18297087/ DOI: 10.1038/nsmb.1393
    tissue_or_cell_type
    Purified proteins

    Biotin: carboxylases, recycling, deficiency and nutrient interactions (2026-09-17) · lines 585–596

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Crystal structures of human PC lacking the BC domain and full-length S. aureus PC; mutagenesis · source_derived_draft · unverified_draft

    ### b7-pc-tetramer The human PC C-terminal structure displayed a conserved tetrameric arrangement, with a PC tetramerization domain identified by structural and mutagenesis analysis. Condition category: normal nutrient_topic: Biotin research collection; topical membership is not evidence of a direct dietary effect. plain_language: Enzyme assembly matters as well as the availability of biotin. organism: Homo sapiens; Staphylococcus aureus tissue_or_cell_type: Purified proteins experimental_model: Crystal structures of human PC lacking the BC domain and full-length S. aureus PC; mutagenesis limitations: The human structure was a C-terminal fragment, not intact human PC; bacterial domain positions must not be silently assigned to human enzyme. exposure: Structural and mutagenesis experiments evidence_span: {"source_cache": "artifacts/biotin-research/18297087.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "64ad42b855e8e31bb8103ad2740baab36988d47779218fbbf19b13f34f4a4d10", "start_char": 0, "end_char": 1026, "text_sha256": "64ad42b855e8e31bb8103ad2740baab36988d47779218fbbf19b13f34f4a4d10"} [b7-p18297087] Crystal structures of human and Staphylococcus aureus pyruvate carboxylase and molecular insights into the carboxyltransfer reaction. (2008). https://pubmed.ncbi.nlm.nih.gov/18297087/ DOI: 10.1038/nsmb.1393
    Complete structured claim and evidence

What acts on it

  1. HLCS rapidly biotinylated the biotin-acceptor fragment of human PC, with transfer limited by enzyme-substrate association.

    Human holocarboxylase synthetase / HLCS → Human pyruvate carboxylase / PC source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/biotin-research/22123817.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "559afe20b6f8601a2d055d42fb121c89eaf1ece76afaa5cc0817c20787893233", "start_char": 0, "end_char": 1502, "text_sha256": "559afe20b6f8601a2d055d42fb121c89eaf1ece76afaa5cc0817c20787893233"}
    experimental_model
    Single-turnover biotin transfer to minimal BCCP fragments from all five human carboxylases
    exposure
    Stopped-flow and quench-flow transfer kinetics
    limitations
    Fragment kinetics support differential recognition, not a universal nutrient-deficiency survival order in humans.
    nutrient_topic
    Biotin research collection; topical membership is not evidence of a direct dietary effect. · Biotin
    organism
    Homo sapiens
    plain_language
    This mitochondrial enzyme has a biotin attachment domain recognized by HLCS.
    primary_references
    [b7-p22123817] Selectivity in post-translational biotin addition to five human carboxylases. (2012). https://pubmed.ncbi.nlm.nih.gov/22123817/ DOI: 10.1074/jbc.m111.275982
    tissue_or_cell_type
    Purified HLCS and acceptor fragments

    Biotin: carboxylases, recycling, deficiency and nutrient interactions (2026-09-17) · lines 390–401

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Single-turnover biotin transfer to minimal BCCP fragments from all five human carboxylases · source_derived_draft · unverified_draft

    ### b7-hlcs-pc-acceptor HLCS rapidly biotinylated the biotin-acceptor fragment of human PC, with transfer limited by enzyme-substrate association. Condition category: normal nutrient_topic: Biotin research collection; topical membership is not evidence of a direct dietary effect. plain_language: This mitochondrial enzyme has a biotin attachment domain recognized by HLCS. organism: Homo sapiens tissue_or_cell_type: Purified HLCS and acceptor fragments experimental_model: Single-turnover biotin transfer to minimal BCCP fragments from all five human carboxylases limitations: Fragment kinetics support differential recognition, not a universal nutrient-deficiency survival order in humans. exposure: Stopped-flow and quench-flow transfer kinetics evidence_span: {"source_cache": "artifacts/biotin-research/22123817.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "559afe20b6f8601a2d055d42fb121c89eaf1ece76afaa5cc0817c20787893233", "start_char": 0, "end_char": 1502, "text_sha256": "559afe20b6f8601a2d055d42fb121c89eaf1ece76afaa5cc0817c20787893233"} [b7-p22123817] Selectivity in post-translational biotin addition to five human carboxylases. (2012). https://pubmed.ncbi.nlm.nih.gov/22123817/ DOI: 10.1074/jbc.m111.275982
    Complete structured claim and evidence

  2. Acetyl-CoA stabilized human PC in a catalytically competent conformation in time-resolved structural and biochemical experiments.

    Acetyl-CoA → Human pyruvate carboxylase / PC source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/biotin-research/36283412.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "2a5fb8ec1c27e243b8c8ba158f2c58ab1592d9895eecf16438175b2a5778de15", "start_char": 0, "end_char": 1060, "text_sha256": "2a5fb8ec1c27e243b8c8ba158f2c58ab1592d9895eecf16438175b2a5778de15"}
    experimental_model
    Time-resolved cryo-EM and biochemical analysis of human PC
    exposure
    Pyruvate, ATP and acetyl-CoA catalytic conditions
    limitations
    Purified-enzyme regulation is not evidence that consuming B5 or biotin stimulates this pathway in every tissue.
    nutrient_topic
    Biotin research collection; topical membership is not evidence of a direct dietary effect. · Biotin
    organism
    Homo sapiens
    plain_language
    Acetyl-CoA helps put PC into its working shape.
    primary_references
    [b7-p36283412] Mechanistic insight into allosteric activation of human pyruvate carboxylase by acetyl-CoA. (2022). https://pubmed.ncbi.nlm.nih.gov/36283412/ DOI: 10.1016/j.molcel.2022.09.033
    tissue_or_cell_type
    Purified human pyruvate carboxylase

    Biotin: carboxylases, recycling, deficiency and nutrient interactions (2026-09-17) · lines 559–570

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Time-resolved cryo-EM and biochemical analysis of human PC · source_derived_draft · unverified_draft

    ### b7-pc-acetylcoa Acetyl-CoA stabilized human PC in a catalytically competent conformation in time-resolved structural and biochemical experiments. Condition category: normal nutrient_topic: Biotin research collection; topical membership is not evidence of a direct dietary effect. plain_language: Acetyl-CoA helps put PC into its working shape. organism: Homo sapiens tissue_or_cell_type: Purified human pyruvate carboxylase experimental_model: Time-resolved cryo-EM and biochemical analysis of human PC limitations: Purified-enzyme regulation is not evidence that consuming B5 or biotin stimulates this pathway in every tissue. exposure: Pyruvate, ATP and acetyl-CoA catalytic conditions evidence_span: {"source_cache": "artifacts/biotin-research/36283412.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "2a5fb8ec1c27e243b8c8ba158f2c58ab1592d9895eecf16438175b2a5778de15", "start_char": 0, "end_char": 1060, "text_sha256": "2a5fb8ec1c27e243b8c8ba158f2c58ab1592d9895eecf16438175b2a5778de15"} [b7-p36283412] Mechanistic insight into allosteric activation of human pyruvate carboxylase by acetyl-CoA. (2022). https://pubmed.ncbi.nlm.nih.gov/36283412/ DOI: 10.1016/j.molcel.2022.09.033
    Complete structured claim and evidence

  3. Acetyl-CoA-dependent stabilization of human PC triggered ATP hydrolysis and communication between its two reaction centers.

    Acetyl-CoA → Human pyruvate carboxylase / PC source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/biotin-research/36283412.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "2a5fb8ec1c27e243b8c8ba158f2c58ab1592d9895eecf16438175b2a5778de15", "start_char": 0, "end_char": 1060, "text_sha256": "2a5fb8ec1c27e243b8c8ba158f2c58ab1592d9895eecf16438175b2a5778de15"}
    experimental_model
    Time-resolved cryo-EM and biochemical analysis of human PC
    exposure
    Pyruvate, ATP and acetyl-CoA catalytic conditions
    limitations
    Purified-enzyme regulation is not evidence that consuming B5 or biotin stimulates this pathway in every tissue.
    nutrient_topic
    Biotin research collection; topical membership is not evidence of a direct dietary effect. · Biotin
    organism
    Homo sapiens
    plain_language
    The biotin-carrying enzyme coordinates two reaction stations rather than performing one isolated chemical step.
    primary_references
    [b7-p36283412] Mechanistic insight into allosteric activation of human pyruvate carboxylase by acetyl-CoA. (2022). https://pubmed.ncbi.nlm.nih.gov/36283412/ DOI: 10.1016/j.molcel.2022.09.033
    tissue_or_cell_type
    Purified human pyruvate carboxylase

    Biotin: carboxylases, recycling, deficiency and nutrient interactions (2026-09-17) · lines 572–583

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Time-resolved cryo-EM and biochemical analysis of human PC · source_derived_draft · unverified_draft

    ### b7-pc-communication Acetyl-CoA-dependent stabilization of human PC triggered ATP hydrolysis and communication between its two reaction centers. Condition category: normal nutrient_topic: Biotin research collection; topical membership is not evidence of a direct dietary effect. plain_language: The biotin-carrying enzyme coordinates two reaction stations rather than performing one isolated chemical step. organism: Homo sapiens tissue_or_cell_type: Purified human pyruvate carboxylase experimental_model: Time-resolved cryo-EM and biochemical analysis of human PC limitations: Purified-enzyme regulation is not evidence that consuming B5 or biotin stimulates this pathway in every tissue. exposure: Pyruvate, ATP and acetyl-CoA catalytic conditions evidence_span: {"source_cache": "artifacts/biotin-research/36283412.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "2a5fb8ec1c27e243b8c8ba158f2c58ab1592d9895eecf16438175b2a5778de15", "start_char": 0, "end_char": 1060, "text_sha256": "2a5fb8ec1c27e243b8c8ba158f2c58ab1592d9895eecf16438175b2a5778de15"} [b7-p36283412] Mechanistic insight into allosteric activation of human pyruvate carboxylase by acetyl-CoA. (2022). https://pubmed.ncbi.nlm.nih.gov/36283412/ DOI: 10.1016/j.molcel.2022.09.033
    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