Component
Human carnitine palmitoyltransferase 1B / CPT1B
Human carnitine palmitoyltransferase 1B / CPT1B. Species, exposure and limitations are retained in each linked claim.
3 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.
Other things that act on it
Enzymes, hormones, genes, and other components with a recorded effect. These are not nutrients, so they do not count toward the arrows above. Each finding names the chapter that recorded it.
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.
What it acts on
Human CPT1B expressed in yeast catalyzed transfer from palmitoyl-CoA onto carnitine, forming palmitoylcarnitine and releasing CoA.
Experimental context and source evidence
- evidence_access
- Primary abstract and reviewed UniProt catalytic-reaction record
- experimental_model
- Human heart/muscle isoform in Pichia mitochondria; canonical reaction also recorded in UniProt Q92523/Rhea 12661.
- limitations
- This isoform assay does not measure whole-body fat loss.
- nutrient_topic
- L-Carnitine collection; isomer, preparation, species, exposure and manipulation remain explicit. · L-Carnitine
- plain_language
- The outer-membrane enzyme loads a fatty-acid group onto carnitine.
- primary_references
- Functional studies of yeast-expressed human heart muscle carnitine palmitoyltransferase I. · 1997 · https://pubmed.ncbi.nlm.nih.gov/9344464/ · DOI 10.1006/abbi.1997.0314
L-Carnitine: synthesis, acyl-group transport, fuel selection and nutrient interactions (2026-09-19) · lines 90–96
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human heart/muscle isoform in Pichia mitochondria; canonical reaction also recorded in UniProt Q92523/Rhea 12661. · source_derived_draft · unverified_draft
## l-carnitine-cpt1-transfer The outer-membrane enzyme loads a fatty-acid group onto carnitine. Human CPT1B expressed in yeast catalyzed transfer from palmitoyl-CoA onto carnitine, forming palmitoylcarnitine and releasing CoA. Model: Human heart/muscle isoform in Pichia mitochondria; canonical reaction also recorded in UniProt Q92523/Rhea 12661. Limitations: This isoform assay does not measure whole-body fat loss. Evidence access: Primary abstract and reviewed UniProt catalytic-reaction record Functional studies of yeast-expressed human heart muscle carnitine palmitoyltransferase I. · 1997 · https://pubmed.ncbi.nlm.nih.gov/9344464/ · DOI 10.1006/abbi.1997.0314
Complete structured claim and evidence
What acts on it
Wild-type human CPT1B showed high-affinity malonyl-CoA binding and inhibition in recombinant mitochondrial assays.
Experimental context and source evidence
- evidence_span
- {"source_cache": "artifacts/biotin-research/10651636.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e99728ef83700f17a810421385b71ea243576419df807dc4749b588beb01d400", "start_char": 0, "end_char": 1542, "text_sha256": "e99728ef83700f17a810421385b71ea243576419df807dc4749b588beb01d400"}
- experimental_model
- Human CPT1B wild type and N-terminal deletions expressed in yeast mitochondria
- exposure
- Malonyl-CoA binding and activity assays
- limitations
- Expression host is yeast; these data concern human CPT1B, not every CPT1 isoform or a biotin supplementation outcome.
- nutrient_topic
- Biotin research collection; topical membership is not evidence of a direct dietary effect. · Biotin
- organism
- Homo sapiens
- plain_language
- Malonyl-CoA links the carboxylase pathway to the carnitine-dependent fat-entry step.
- primary_references
- [b7-p10651636] The first 28 N-terminal amino acid residues of human heart muscle carnitine palmitoyltransferase I are essential for malonyl CoA sensitivity and high-affinity binding. (2000). https://pubmed.ncbi.nlm.nih.gov/10651636/ DOI: 10.1021/bi9918700
- tissue_or_cell_type
- Recombinant human muscle/heart CPT1B
Biotin: carboxylases, recycling, deficiency and nutrient interactions (2026-09-17) · lines 741–752
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human CPT1B wild type and N-terminal deletions expressed in yeast mitochondria · source_derived_draft · unverified_draft
### b7-malonyl-cpt1b Wild-type human CPT1B showed high-affinity malonyl-CoA binding and inhibition in recombinant mitochondrial assays. Condition category: normal nutrient_topic: Biotin research collection; topical membership is not evidence of a direct dietary effect. plain_language: Malonyl-CoA links the carboxylase pathway to the carnitine-dependent fat-entry step. organism: Homo sapiens tissue_or_cell_type: Recombinant human muscle/heart CPT1B experimental_model: Human CPT1B wild type and N-terminal deletions expressed in yeast mitochondria limitations: Expression host is yeast; these data concern human CPT1B, not every CPT1 isoform or a biotin supplementation outcome. exposure: Malonyl-CoA binding and activity assays evidence_span: {"source_cache": "artifacts/biotin-research/10651636.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e99728ef83700f17a810421385b71ea243576419df807dc4749b588beb01d400", "start_char": 0, "end_char": 1542, "text_sha256": "e99728ef83700f17a810421385b71ea243576419df807dc4749b588beb01d400"} [b7-p10651636] The first 28 N-terminal amino acid residues of human heart muscle carnitine palmitoyltransferase I are essential for malonyl CoA sensitivity and high-affinity binding. (2000). https://pubmed.ncbi.nlm.nih.gov/10651636/ DOI: 10.1021/bi9918700
Complete structured claim and evidence
Where it participates (unsigned role)
Deleting the first 28 residues of human CPT1B removed high-affinity malonyl-CoA binding and inhibition despite retained catalytic activity.
Experimental context and source evidence
- evidence_span
- {"source_cache": "artifacts/biotin-research/10651636.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e99728ef83700f17a810421385b71ea243576419df807dc4749b588beb01d400", "start_char": 0, "end_char": 1542, "text_sha256": "e99728ef83700f17a810421385b71ea243576419df807dc4749b588beb01d400"}
- experimental_model
- Human CPT1B wild type and N-terminal deletions expressed in yeast mitochondria
- exposure
- Malonyl-CoA binding and activity assays
- limitations
- Expression host is yeast; these data concern human CPT1B, not every CPT1 isoform or a biotin supplementation outcome.
- nutrient_topic
- Biotin research collection; topical membership is not evidence of a direct dietary effect. · Biotin
- organism
- Homo sapiens
- plain_language
- This engineered change separates the enzyme brake from its basic catalytic function.
- primary_references
- [b7-p10651636] The first 28 N-terminal amino acid residues of human heart muscle carnitine palmitoyltransferase I are essential for malonyl CoA sensitivity and high-affinity binding. (2000). https://pubmed.ncbi.nlm.nih.gov/10651636/ DOI: 10.1021/bi9918700
- tissue_or_cell_type
- Recombinant human muscle/heart CPT1B
Biotin: carboxylases, recycling, deficiency and nutrient interactions (2026-09-17) · lines 754–765
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human CPT1B wild type and N-terminal deletions expressed in yeast mitochondria · source_derived_draft · unverified_draft
### b7-cpt1b-delta28 Deleting the first 28 residues of human CPT1B removed high-affinity malonyl-CoA binding and inhibition despite retained catalytic activity. Condition category: normal nutrient_topic: Biotin research collection; topical membership is not evidence of a direct dietary effect. plain_language: This engineered change separates the enzyme brake from its basic catalytic function. organism: Homo sapiens tissue_or_cell_type: Recombinant human muscle/heart CPT1B experimental_model: Human CPT1B wild type and N-terminal deletions expressed in yeast mitochondria limitations: Expression host is yeast; these data concern human CPT1B, not every CPT1 isoform or a biotin supplementation outcome. exposure: Malonyl-CoA binding and activity assays evidence_span: {"source_cache": "artifacts/biotin-research/10651636.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e99728ef83700f17a810421385b71ea243576419df807dc4749b588beb01d400", "start_char": 0, "end_char": 1542, "text_sha256": "e99728ef83700f17a810421385b71ea243576419df807dc4749b588beb01d400"} [b7-p10651636] The first 28 N-terminal amino acid residues of human heart muscle carnitine palmitoyltransferase I are essential for malonyl CoA sensitivity and high-affinity binding. (2000). https://pubmed.ncbi.nlm.nih.gov/10651636/ DOI: 10.1021/bi9918700
Complete structured claim and evidence
The events it takes part in
A mechanism often involves more than two components. These are the full events, with every participant and its role.
Situations it appears in
Low-supply and faulty-machinery situations recorded in the chapters where this component plays a part.
In the sources
Preserved passages that mention this component, quoted exactly. Open one to read it in context.
Open hypotheses
Proposed ideas that involve this component. They are labeled as hypotheses and do not change any recorded statement.
This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.