Component
Human methionine adenosyltransferase 1A / MAT1A
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
MAT1A supplies subunits of tetrameric MAT I and dimeric MAT III, which convert methionine and ATP to SAM.
Experimental context and source evidence
- evidence_access
- Primary abstract
- experimental_model
- Human MAT1A disease cohort; established isoenzyme chemistry.
- limitations
- MAT1A and MAT2A retain separate identities.
- nutrient_topic
- L-Methionine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Methionine
- plain_language
- The liver has distinct enzyme assemblies for activating methionine.
- primary_references
- Mudd's disease (MAT I/III deficiency): a survey of data for MAT1A homozygotes and compound heterozygotes. · 2015 · https://pubmed.ncbi.nlm.nih.gov/26289392/ · DOI 10.1186/s13023-015-0321-y
L-Methionine: transport, methylation, sulfur metabolism and cross-nutrient mechanisms (2026-09-19) · lines 148–154
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human MAT1A disease cohort; established isoenzyme chemistry. · source_derived_draft · unverified_draft
## methionine-mat1-isoenzymes The liver has distinct enzyme assemblies for activating methionine. MAT1A supplies subunits of tetrameric MAT I and dimeric MAT III, which convert methionine and ATP to SAM. Model: Human MAT1A disease cohort; established isoenzyme chemistry. Limitations: MAT1A and MAT2A retain separate identities. Evidence access: Primary abstract Mudd's disease (MAT I/III deficiency): a survey of data for MAT1A homozygotes and compound heterozygotes. · 2015 · https://pubmed.ncbi.nlm.nih.gov/26289392/ · DOI 10.1186/s13023-015-0321-y
Complete structured claim and evidenceReduced MAT I/III function caused persistent hypermethioninemia in patients with biallelic MAT1A variants.
Experimental context and source evidence
- availability_state
- machinery_impairment Imported condition classification; unverified.
- evidence_access
- Primary abstract
- experimental_model
- Aggregated clinical data from 64 homozygous/compound-heterozygous patients.
- limitations
- Does not imply that high methionine always means this genetic disorder.
- nutrient_topic
- L-Methionine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Methionine
- plain_language
- High substrate can signal failure to process it.
- primary_references
- Mudd's disease (MAT I/III deficiency): a survey of data for MAT1A homozygotes and compound heterozygotes. · 2015 · https://pubmed.ncbi.nlm.nih.gov/26289392/ · DOI 10.1186/s13023-015-0321-y
- trigger_kind
- machinery_impairment Imported condition classification; unverified.
L-Methionine: transport, methylation, sulfur metabolism and cross-nutrient mechanisms (2026-09-19) · lines 156–162
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Aggregated clinical data from 64 homozygous/compound-heterozygous patients. · source_derived_draft · unverified_draft
## methionine-mat1-loss High substrate can signal failure to process it. Reduced MAT I/III function caused persistent hypermethioninemia in patients with biallelic MAT1A variants. Model: Aggregated clinical data from 64 homozygous/compound-heterozygous patients. Limitations: Does not imply that high methionine always means this genetic disorder. Evidence access: Primary abstract Mudd's disease (MAT I/III deficiency): a survey of data for MAT1A homozygotes and compound heterozygotes. · 2015 · https://pubmed.ncbi.nlm.nih.gov/26289392/ · DOI 10.1186/s13023-015-0321-y
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.