Component
Human FAD synthetase isoform 1
FLAD1-encoded isoform 1 tested as a recombinant protein; not fatty acid desaturase FADS1.
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
In vitro synthesized human FADS1 entered isolated rat liver mitochondria and was processed; transfected-cell imaging also localized it to mitochondria.
Experimental context and source evidence
- evidence_location
- Abstract; mitochondrial import and confocal imaging
- experimental_model
- Import into purified rat liver mitochondria; BHK-21/Caco-2 confocal imaging
- exposure
- In vitro synthesized and transiently expressed human FADS1.
- limitations
- Construct/import evidence does not establish its abundance in every human tissue.
- nutrient_topic
- Riboflavin research collection; topical membership is not evidence of a direct dietary effect. · Riboflavin (vitamin B2)
- organism
- Human protein; rat mitochondria; hamster and human cells
- plain_language
- One FLAD1 isoform can provide FAD-synthesis machinery inside mitochondria.
- primary_references
- [transport-fads-localization-2010] Mitochondrial localization of human FAD synthetase isoform 1. (2010). https://pubmed.ncbi.nlm.nih.gov/20060505/ DOI: 10.1016/j.mito.2009.12.149
- tissue_or_cell_type
- Liver mitochondria and cultured epithelial cells
Riboflavin: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 347–358
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Import into purified rat liver mitochondria; BHK-21/Caco-2 confocal imaging · source_derived_draft · unverified_draft
### transport-flad1-isoform1-mitochondria In vitro synthesized human FADS1 entered isolated rat liver mitochondria and was processed; transfected-cell imaging also localized it to mitochondria. Condition category: normal nutrient_topic: Riboflavin research collection; topical membership is not evidence of a direct dietary effect. plain_language: One FLAD1 isoform can provide FAD-synthesis machinery inside mitochondria. organism: Human protein; rat mitochondria; hamster and human cells tissue_or_cell_type: Liver mitochondria and cultured epithelial cells experimental_model: Import into purified rat liver mitochondria; BHK-21/Caco-2 confocal imaging limitations: Construct/import evidence does not establish its abundance in every human tissue. exposure: In vitro synthesized and transiently expressed human FADS1. evidence_location: Abstract; mitochondrial import and confocal imaging [transport-fads-localization-2010] Mitochondrial localization of human FAD synthetase isoform 1. (2010). https://pubmed.ncbi.nlm.nih.gov/20060505/ DOI: 10.1016/j.mito.2009.12.149
Complete structured claim and evidence
Where it participates (unsigned role)
Recombinant human FLAD1 isoforms 1 and 2 exhibited FAD synthetase activity; isoform 2 was purified, and activity required MgCl2.
Experimental context and source evidence
- cross_nutrient
- B2 activation and Mg-dependent FAD synthesis provide a biochemical partner to B1-dependent complexes; direct transfer of newly made FAD to DLD was not tested.
- evidence
- [{"paper_key": "brizio-2006-fad", "source_bundle": "artifacts/thiamine_metabolism_sources.json", "passage_ids": ["abstract"], "locator": "Primary publication abstract", "preservation": "Exact text retained in the source bundle; full source document retained when openly retrievable."}]
- experimental_model
- Recombinant human FLAD1 isoforms expressed in E. coli.
- limitations
- No tissue Mg threshold or combined B1/B2 deficiency experiment.
- nutrient
- Thiamine (vitamin B1) · Thiamine (vitamin B1)
- nutrient_topic
- Thiamine research collection; topical membership is not evidence of a direct dietary effect. · Thiamine (vitamin B1)
- organism
- Homo sapiens
- plain_language
- The flavin used by E3 must first be made from the riboflavin pathway. This distinct magnesium-dependent synthesis reaction should not be confused with magnesium binding to B1 enzymes.
- primary_references
- [brizio-2006-fad] Over-expression in Escherichia coli and characterization of two recombinant isoforms of human FAD synthetase (2006). https://pubmed.ncbi.nlm.nih.gov/16643857/ DOI: 10.1016/j.bbrc.2006.04.003
- tissue_or_cell_type
- Purified/expressed proteins
Thiamine: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 745–757
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human FLAD1 isoforms expressed in E. coli. · source_derived_draft · unverified_draft
### b1-fad-b2-cofactor-synthesis Recombinant human FLAD1 isoforms 1 and 2 exhibited FAD synthetase activity; isoform 2 was purified, and activity required MgCl2. Condition category: normal nutrient_topic: Thiamine research collection; topical membership is not evidence of a direct dietary effect. plain_language: The flavin used by E3 must first be made from the riboflavin pathway. This distinct magnesium-dependent synthesis reaction should not be confused with magnesium binding to B1 enzymes. organism: Homo sapiens tissue_or_cell_type: Purified/expressed proteins experimental_model: Recombinant human FLAD1 isoforms expressed in E. coli. limitations: No tissue Mg threshold or combined B1/B2 deficiency experiment. evidence: [{"paper_key": "brizio-2006-fad", "source_bundle": "artifacts/thiamine_metabolism_sources.json", "passage_ids": ["abstract"], "locator": "Primary publication abstract", "preservation": "Exact text retained in the source bundle; full source document retained when openly retrievable."}] cross_nutrient: B2 activation and Mg-dependent FAD synthesis provide a biochemical partner to B1-dependent complexes; direct transfer of newly made FAD to DLD was not tested. nutrient: Thiamine (vitamin B1) [brizio-2006-fad] Over-expression in Escherichia coli and characterization of two recombinant isoforms of human FAD synthetase (2006). https://pubmed.ncbi.nlm.nih.gov/16643857/ DOI: 10.1016/j.bbrc.2006.04.003
Complete structured claim and evidenceFADS2 lacked mitochondrial import/localization in the experiments that imported and localized FADS1.
Experimental context and source evidence
- evidence_location
- Abstract; FADS2 comparator
- experimental_model
- Parallel FADS1/FADS2 import and localization comparison
- exposure
- In vitro synthesized and transiently expressed human isoforms.
- limitations
- No import in this assay does not exclude condition-dependent localization outside the tested systems.
- nutrient_topic
- Riboflavin research collection; topical membership is not evidence of a direct dietary effect. · Riboflavin (vitamin B2)
- organism
- Human proteins in mammalian model preparations
- plain_language
- FLAD1 isoforms differ in access to the mitochondrial compartment.
- primary_references
- [transport-fads-localization-2010] Mitochondrial localization of human FAD synthetase isoform 1. (2010). https://pubmed.ncbi.nlm.nih.gov/20060505/ DOI: 10.1016/j.mito.2009.12.149
- tissue_or_cell_type
- Rat liver mitochondria; BHK-21 and Caco-2 cells
Riboflavin: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 360–371
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Parallel FADS1/FADS2 import and localization comparison · source_derived_draft · unverified_draft
### transport-flad1-isoform2-compartment FADS2 lacked mitochondrial import/localization in the experiments that imported and localized FADS1. Condition category: normal nutrient_topic: Riboflavin research collection; topical membership is not evidence of a direct dietary effect. plain_language: FLAD1 isoforms differ in access to the mitochondrial compartment. organism: Human proteins in mammalian model preparations tissue_or_cell_type: Rat liver mitochondria; BHK-21 and Caco-2 cells experimental_model: Parallel FADS1/FADS2 import and localization comparison limitations: No import in this assay does not exclude condition-dependent localization outside the tested systems. exposure: In vitro synthesized and transiently expressed human isoforms. evidence_location: Abstract; FADS2 comparator [transport-fads-localization-2010] Mitochondrial localization of human FAD synthetase isoform 1. (2010). https://pubmed.ncbi.nlm.nih.gov/20060505/ DOI: 10.1016/j.mito.2009.12.149
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.