Component
Mouse arylformamidase / Afmid
Context-specific entity; species, compartment and exposure are stated on each claim.
2 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 mouse Afmid hydrolyzed N-formyl-L-kynurenine with a Km of 0.18–0.19 mM, matching native mouse cytosolic enzyme.
Experimental context and source evidence
- evidence_access
- Primary abstract
- experimental_model
- Mouse liver enzyme expressed in E. coli.
- limitations
- This experiment is mouse enzyme evidence, not direct human AFMID validation.
- nutrient_topic
- Tryptophan collection; molecular form, preparation, species, exposure and manipulation remain explicit. · L-Tryptophan
- plain_language
- A second enzyme removes the formyl group to produce kynurenine.
- primary_references
- Cloning, expression, and catalytic triad of recombinant arylformamidase. · 2005 · https://pubmed.ncbi.nlm.nih.gov/15935693/ · DOI 10.1016/j.pep.2005.04.013
Tryptophan: transport, protein synthesis, neuroactive metabolites, NAD and microbial pathways (2026-09-19) · lines 186–192
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Mouse liver enzyme expressed in E. coli. · source_derived_draft · unverified_draft
## tryptophan-afmid-hydrolysis A second enzyme removes the formyl group to produce kynurenine. Recombinant mouse Afmid hydrolyzed N-formyl-L-kynurenine with a Km of 0.18–0.19 mM, matching native mouse cytosolic enzyme. Model: Mouse liver enzyme expressed in E. coli. Limitations: This experiment is mouse enzyme evidence, not direct human AFMID validation. Evidence access: Primary abstract Cloning, expression, and catalytic triad of recombinant arylformamidase. · 2005 · https://pubmed.ncbi.nlm.nih.gov/15935693/ · DOI 10.1016/j.pep.2005.04.013
Complete structured claim and evidenceS162A, D247A or H279A substitutions in mouse Afmid each removed more than 99% of measured enzyme activity.
Experimental context and source evidence
- availability_state
- machinery_impairment Imported condition classification; unverified.
- evidence_access
- Primary abstract
- experimental_model
- Recombinant mouse enzyme mutations.
- limitations
- Does not quantify human variant effects or prove a clinical repletion failure.
- nutrient_topic
- Tryptophan collection; molecular form, preparation, species, exposure and manipulation remain explicit. · L-Tryptophan
- plain_language
- One defective catalytic residue can block the next step despite available substrate.
- primary_references
- Cloning, expression, and catalytic triad of recombinant arylformamidase. · 2005 · https://pubmed.ncbi.nlm.nih.gov/15935693/ · DOI 10.1016/j.pep.2005.04.013
- trigger_kind
- machinery_impairment Imported condition classification; unverified.
Tryptophan: transport, protein synthesis, neuroactive metabolites, NAD and microbial pathways (2026-09-19) · lines 194–200
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Recombinant mouse enzyme mutations. · source_derived_draft · unverified_draft
## tryptophan-afmid-triad One defective catalytic residue can block the next step despite available substrate. S162A, D247A or H279A substitutions in mouse Afmid each removed more than 99% of measured enzyme activity. Model: Recombinant mouse enzyme mutations. Limitations: Does not quantify human variant effects or prove a clinical repletion failure. Evidence access: Primary abstract Cloning, expression, and catalytic triad of recombinant arylformamidase. · 2005 · https://pubmed.ncbi.nlm.nih.gov/15935693/ · DOI 10.1016/j.pep.2005.04.013
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.