Component

Protein-bound methionine

Independent chemical species record for Protein-bound methionine.

4 recorded relationships. Experimental role, claim status and evidence remain attached to each record.

Read recorded mechanisms Open recursive mind map

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.

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.

Recorded relationships

What it acts on

  1. Oxidation of paired CaMKII regulatory methionines sustained kinase activity after calcium/calmodulin was removed.

    Protein-bound methionine → Oxidized regulatory methionines in the CaMKII study source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Biochemical kinase assays with cardiomyocyte and mouse experiments; exact purified construct species not resolved here.
    limitations
    Initial calcium/calmodulin exposure and sustained autonomous activity are distinct; not a dietary methionine effect.
    nutrient_topic
    L-Methionine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Methionine
    plain_language
    Oxidation can leave a signaling protein switched on.
    primary_references
    A dynamic pathway for calcium-independent activation of CaMKII by methionine oxidation. · 2008 · https://pubmed.ncbi.nlm.nih.gov/18455987/ · DOI 10.1016/j.cell.2008.02.048

    L-Methionine: transport, methylation, sulfur metabolism and cross-nutrient mechanisms (2026-09-19) · lines 332–338

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Biochemical kinase assays with cardiomyocyte and mouse experiments; exact purified construct species not resolved here. · source_derived_draft · unverified_draft

    ## methionine-camkii-oxidation Oxidation can leave a signaling protein switched on. Oxidation of paired CaMKII regulatory methionines sustained kinase activity after calcium/calmodulin was removed. Model: Biochemical kinase assays with cardiomyocyte and mouse experiments; exact purified construct species not resolved here. Limitations: Initial calcium/calmodulin exposure and sustained autonomous activity are distinct; not a dietary methionine effect. Evidence access: Primary abstract A dynamic pathway for calcium-independent activation of CaMKII by methionine oxidation. · 2008 · https://pubmed.ncbi.nlm.nih.gov/18455987/ · DOI 10.1016/j.cell.2008.02.048
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Phosphorylation-mimicking MARS1 favored non-cognate tRNAs and increased methionine incorporation at normally non-methionine positions.

    Human cytosolic methionyl-tRNA synthetase / MARS1 → Methionylation of non-cognate human tRNAs source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    Human MARS1 mutants and cultured-cell/protein assays.
    limitations
    Not evidence that all altered proteins retain normal function or that methionine loading is protective.
    nutrient_topic
    L-Methionine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Methionine
    plain_language
    Cells can trade some translation accuracy for a stress response.
    primary_references
    Promiscuous methionyl-tRNA synthetase mediates adaptive mistranslation to protect cells against oxidative stress. · 2014 · https://pubmed.ncbi.nlm.nih.gov/25097229/ · DOI 10.1242/jcs.152470

    L-Methionine: transport, methylation, sulfur metabolism and cross-nutrient mechanisms (2026-09-19) · lines 76–82

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human MARS1 mutants and cultured-cell/protein assays. · source_derived_draft · unverified_draft

    ## methionine-mars-mischarging Cells can trade some translation accuracy for a stress response. Phosphorylation-mimicking MARS1 favored non-cognate tRNAs and increased methionine incorporation at normally non-methionine positions. Model: Human MARS1 mutants and cultured-cell/protein assays. Limitations: Not evidence that all altered proteins retain normal function or that methionine loading is protective. Evidence access: Primary full text Promiscuous methionyl-tRNA synthetase mediates adaptive mistranslation to protect cells against oxidative stress. · 2014 · https://pubmed.ncbi.nlm.nih.gov/25097229/ · DOI 10.1242/jcs.152470
    Complete structured claim and evidence

  2. Msra-null mice had greater CaMKII oxidation, myocardial apoptosis and post-infarction dysfunction; methionine-sulfoxide reduction reversed oxidation-dependent activation in supporting assays.

    Mouse methionine sulfoxide reductase A / Msra → Oxidized CaMKII and cardiac injury in mice source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary abstract
    experimental_model
    Msra-knockout mice with biochemical support.
    limitations
    MSRA and selenium-dependent MSRB1 differ in substrate stereochemistry; they are not interchangeable.
    nutrient_topic
    L-Methionine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Methionine
    plain_language
    Repairing an oxidized residue can reset a signaling switch.
    primary_references
    A dynamic pathway for calcium-independent activation of CaMKII by methionine oxidation. · 2008 · https://pubmed.ncbi.nlm.nih.gov/18455987/ · DOI 10.1016/j.cell.2008.02.048
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    L-Methionine: transport, methylation, sulfur metabolism and cross-nutrient mechanisms (2026-09-19) · lines 340–346

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Msra-knockout mice with biochemical support. · source_derived_draft · unverified_draft

    ## methionine-msra-camkii-repair Repairing an oxidized residue can reset a signaling switch. Msra-null mice had greater CaMKII oxidation, myocardial apoptosis and post-infarction dysfunction; methionine-sulfoxide reduction reversed oxidation-dependent activation in supporting assays. Model: Msra-knockout mice with biochemical support. Limitations: MSRA and selenium-dependent MSRB1 differ in substrate stereochemistry; they are not interchangeable. Evidence access: Primary abstract A dynamic pathway for calcium-independent activation of CaMKII by methionine oxidation. · 2008 · https://pubmed.ncbi.nlm.nih.gov/18455987/ · DOI 10.1016/j.cell.2008.02.048
    Complete structured claim and evidence

  3. MSRB1 reduces protein methionine-R-sulfoxide back toward the methionine state; stereochemistry and protein context matter.

    MSRB1 → Protein-bound methionine-R-sulfoxide source_derived_draftliterature_reviewed:direct_experimental
    Experimental context and source evidence
    experimental_model
    Human and mouse MsrB protein characterization and localization.
    limitations
    This experiment-specific relationship does not establish a human dietary-deficiency threshold or supplementation benefit.
    organism
    Human and mouse proteins

    Selenium: literature corrections and mechanism additions · lines 1042–1051

    Metabolic Ledger literature curation, 17 September 2026; primary papers linked individually · supports · Human and mouse MsrB protein characterization and localization. · secondary_verified · secondary_verified

    ## msrb1-repairs-methionine MSRB1 repairs one specific form of oxidized methionine in proteins. MSRB1 reduces protein methionine-R-sulfoxide back toward the methionine state; stereochemistry and protein context matter. Experimental model: Human and mouse MsrB protein characterization and localization. Organism: Human and mouse proteins Limitations: This experiment-specific relationship does not establish a human dietary-deficiency threshold or supplementation benefit. Primary reference: [Methionine sulfoxide reduction in mammals: characterization of methionine-R-sulfoxide reductases](https://pubmed.ncbi.nlm.nih.gov/14699060/)
    Complete structured claim and evidence

In the sources

Preserved passages that mention this component, quoted exactly. Open one to read it in context.

    This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.

    Evidence, AI assistance and curation standards