Component
FLAD1 p.Ser495del variant
Ser495 deletion named using FADS1 numbering; studied in recombinant FADS2.
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
Recombinant FADS2 carrying p.Ser495del retained less bound flavin than wild-type FADS2.
Experimental context and source evidence
- availability_state
- machinery_impairment Imported condition classification; unverified.
- evidence_location
- Figure 4B
- experimental_model
- Purified recombinant human FADS2 variant
- exposure
- Wild-type versus variant purified enzyme.
- limitations
- Variant numbering follows FADS1; this is not a finding for all FLAD1 variants.
- nutrient_topic
- Riboflavin research collection; topical membership is not evidence of a direct dietary effect. · Riboflavin (vitamin B2)
- organism
- Homo sapiens protein
- plain_language
- This FLAD1 variant retains bound FAD less effectively.
- primary_references
- [transport-flad1-disease-2016] Riboflavin-Responsive and -Non-responsive Mutations in FAD Synthase Cause Multiple Acyl-CoA Dehydrogenase and Combined Respiratory-Chain Deficiency (2016). https://pmc.ncbi.nlm.nih.gov/articles/PMC4908180/ DOI: 10.1016/j.ajhg.2016.04.006
- tissue_or_cell_type
- Purified protein
- trigger_kind
- machinery_impairment Imported condition classification; unverified.
Riboflavin: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 386–397
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified recombinant human FADS2 variant · source_derived_draft · unverified_draft
### transport-flad1-s495del-binding Recombinant FADS2 carrying p.Ser495del retained less bound flavin than wild-type FADS2. Condition category: machinery_impairment nutrient_topic: Riboflavin research collection; topical membership is not evidence of a direct dietary effect. plain_language: This FLAD1 variant retains bound FAD less effectively. organism: Homo sapiens protein tissue_or_cell_type: Purified protein experimental_model: Purified recombinant human FADS2 variant limitations: Variant numbering follows FADS1; this is not a finding for all FLAD1 variants. exposure: Wild-type versus variant purified enzyme. evidence_location: Figure 4B [transport-flad1-disease-2016] Riboflavin-Responsive and -Non-responsive Mutations in FAD Synthase Cause Multiple Acyl-CoA Dehydrogenase and Combined Respiratory-Chain Deficiency (2016). https://pmc.ncbi.nlm.nih.gov/articles/PMC4908180/ DOI: 10.1016/j.ajhg.2016.04.006
Complete structured claim and evidence
What acts on it
Excess FAD reconstitution restored bound flavin and increased proteolytic stability of recombinant p.Ser495del FADS2.
Experimental context and source evidence
- availability_state
- machinery_impairment Imported condition classification; unverified.
- evidence_location
- Figure 4A-B
- experimental_model
- Recombinant variant FAD reconstitution and proteolysis
- exposure
- Molar excess FAD during in vitro reconstitution.
- limitations
- Direct FAD exposure in vitro; does not prove universal rescue by dietary riboflavin.
- nutrient_topic
- Riboflavin research collection; topical membership is not evidence of a direct dietary effect. · Riboflavin (vitamin B2)
- organism
- Homo sapiens protein
- plain_language
- FAD helped stabilize this particular altered enzyme.
- primary_references
- [transport-flad1-disease-2016] Riboflavin-Responsive and -Non-responsive Mutations in FAD Synthase Cause Multiple Acyl-CoA Dehydrogenase and Combined Respiratory-Chain Deficiency (2016). https://pmc.ncbi.nlm.nih.gov/articles/PMC4908180/ DOI: 10.1016/j.ajhg.2016.04.006
- tissue_or_cell_type
- Purified protein
- trigger_kind
- machinery_impairment Imported condition classification; unverified.
Riboflavin: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 399–410
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant variant FAD reconstitution and proteolysis · source_derived_draft · unverified_draft
### transport-flad1-s495del-stabilization Excess FAD reconstitution restored bound flavin and increased proteolytic stability of recombinant p.Ser495del FADS2. Condition category: machinery_impairment nutrient_topic: Riboflavin research collection; topical membership is not evidence of a direct dietary effect. plain_language: FAD helped stabilize this particular altered enzyme. organism: Homo sapiens protein tissue_or_cell_type: Purified protein experimental_model: Recombinant variant FAD reconstitution and proteolysis limitations: Direct FAD exposure in vitro; does not prove universal rescue by dietary riboflavin. exposure: Molar excess FAD during in vitro reconstitution. evidence_location: Figure 4A-B [transport-flad1-disease-2016] Riboflavin-Responsive and -Non-responsive Mutations in FAD Synthase Cause Multiple Acyl-CoA Dehydrogenase and Combined Respiratory-Chain Deficiency (2016). https://pmc.ncbi.nlm.nih.gov/articles/PMC4908180/ DOI: 10.1016/j.ajhg.2016.04.006
Complete structured claim and evidence
Where it participates (unsigned role)
FAD-saturated p.Ser495del and p.Arg530Cys FADS2 remained substantially less catalytically active than wild type.
Experimental context and source evidence
- availability_state
- machinery_impairment Imported condition classification; unverified.
- evidence_location
- Figure 5
- experimental_model
- FAD-saturated purified FADS2 variants
- exposure
- Molar-excess FAD reconstitution followed by catalytic assays.
- limitations
- The two variants differ in binding/stability responses; the result concerns maximal in vitro activity.
- nutrient_topic
- Riboflavin research collection; topical membership is not evidence of a direct dietary effect. · Riboflavin (vitamin B2)
- organism
- Homo sapiens protein
- plain_language
- Stabilizing a variant does not necessarily restore normal enzyme output.
- primary_references
- [transport-flad1-disease-2016] Riboflavin-Responsive and -Non-responsive Mutations in FAD Synthase Cause Multiple Acyl-CoA Dehydrogenase and Combined Respiratory-Chain Deficiency (2016). https://pmc.ncbi.nlm.nih.gov/articles/PMC4908180/ DOI: 10.1016/j.ajhg.2016.04.006
- tissue_or_cell_type
- Purified protein
- trigger_kind
- machinery_impairment Imported condition classification; unverified.
Riboflavin: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 412–423
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · FAD-saturated purified FADS2 variants · source_derived_draft · unverified_draft
### transport-flad1-residual-catalytic-defect FAD-saturated p.Ser495del and p.Arg530Cys FADS2 remained substantially less catalytically active than wild type. Condition category: machinery_impairment nutrient_topic: Riboflavin research collection; topical membership is not evidence of a direct dietary effect. plain_language: Stabilizing a variant does not necessarily restore normal enzyme output. organism: Homo sapiens protein tissue_or_cell_type: Purified protein experimental_model: FAD-saturated purified FADS2 variants limitations: The two variants differ in binding/stability responses; the result concerns maximal in vitro activity. exposure: Molar-excess FAD reconstitution followed by catalytic assays. evidence_location: Figure 5 [transport-flad1-disease-2016] Riboflavin-Responsive and -Non-responsive Mutations in FAD Synthase Cause Multiple Acyl-CoA Dehydrogenase and Combined Respiratory-Chain Deficiency (2016). https://pmc.ncbi.nlm.nih.gov/articles/PMC4908180/ DOI: 10.1016/j.ajhg.2016.04.006
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.