Component

Human angiotensin-converting enzyme / ACE

The peptidyl dipeptidase of the renin-angiotensin system. Distinct from the ledger's ACE2 node.

6 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 acts on it

  1. Catalytically active intact nattokinase is not required for the ACE-inhibitory activity of the material, because heat inactivation raises rather than removes it.

    Nattokinase / subtilisin NAT → Human angiotensin-converting enzyme / ACE source_derived_draftungraded
    Experimental context and source evidence
    duration
    Not stated here
    evidence_access
    Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
    experimental_model
    Purified subtilisin NAT
    exposure
    Active compared with heat-inactivated subtilisin NAT
    limitations
    This is a statement about one activity only. Every direct-proteolysis mechanism in this chapter does require the intact active enzyme.
    organism
    Purified subtilisin NAT
    plain_language
    Catalytically active intact nattokinase is not required for the ACE-inhibitory activity of the material, because heat inactivation raises rather than removes it.
    primary_references
    Inhibition of angiotensin I converting enzyme by subtilisin NAT (nattokinase) in natto, a Japanese traditional fermented food. (2012) https://pubmed.ncbi.nlm.nih.gov/22453301/ DOI: 10.1039/c2fo10245e
    route
    In vitro
    tissue
    ACE inhibition assay

    Nattokinase: what the purified enzyme cleaves, what survives being eaten, and the gap between the two (2026-09-23) · lines 741–741

    Original AI-assisted curation built from a supplied entity-first document of 105 entities and 129 claims. Every reference in that document was resolved against live PubMed with its abstract read and its DOI cross-checked on 2026-09-23, and the EFSA novel-food opinion was retrieved and read in full. That check corrected two PMIDs that pointed at unrelated papers, two DOIs, and two papers recorded as carrying no erratum that do carry one; it also reversed three findings the supplied document had stated backwards. Two papers carry a published correction, recorded as such and not as a retraction. Three sources are not indexed in PubMed and are cited by what they have. Laboratory lineages are recorded, so the four papers from one group, the three from another and the two readings of a single applicant dossier cannot be counted as separate lines of support. Study-specific doses, units, populations and limitations retained; activity units are never converted between systems. Not publisher full text. · supports · Purified subtilisin NAT · source_derived_draft · unverified_draft

    Catalytically active intact nattokinase is not required for the ACE-inhibitory activity of the material, because heat inactivation raises rather than removes it.
    Complete structured claim and evidence

  2. Heat treatment at 120 C for 15 min markedly increased the ACE-inhibitory activity of subtilisin NAT while inactivating it as a protease and fragmenting it into small peptides.

    Heat-inactivated nattokinase → Human angiotensin-converting enzyme / ACE source_derived_draftungraded
    Experimental context and source evidence
    duration
    15 min heating
    evidence_access
    Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
    experimental_model
    Purified subtilisin NAT
    exposure
    Subtilisin NAT, heat-treated at 120 C for 15 min
    limitations
    This is the clearest evidence in the chapter that destroying the enzyme creates a different pharmacological species rather than nothing. The authors state the inhibition is not due to an enzymatic action of the protease. Inhibition was of mixed type: Vmax fell and Km rose.
    organism
    Purified subtilisin NAT
    plain_language
    Heat treatment at 120 C for 15 min markedly increased the ACE-inhibitory activity of subtilisin NAT while inactivating it as a protease and fragmenting it into small peptides.
    primary_references
    Inhibition of angiotensin I converting enzyme by subtilisin NAT (nattokinase) in natto, a Japanese traditional fermented food. (2012) https://pubmed.ncbi.nlm.nih.gov/22453301/ DOI: 10.1039/c2fo10245e
    route
    In vitro
    tissue
    ACE inhibition assay

    Nattokinase: what the purified enzyme cleaves, what survives being eaten, and the gap between the two (2026-09-23) · lines 675–675

    Original AI-assisted curation built from a supplied entity-first document of 105 entities and 129 claims. Every reference in that document was resolved against live PubMed with its abstract read and its DOI cross-checked on 2026-09-23, and the EFSA novel-food opinion was retrieved and read in full. That check corrected two PMIDs that pointed at unrelated papers, two DOIs, and two papers recorded as carrying no erratum that do carry one; it also reversed three findings the supplied document had stated backwards. Two papers carry a published correction, recorded as such and not as a retraction. Three sources are not indexed in PubMed and are cited by what they have. Laboratory lineages are recorded, so the four papers from one group, the three from another and the two readings of a single applicant dossier cannot be counted as separate lines of support. Study-specific doses, units, populations and limitations retained; activity units are never converted between systems. Not publisher full text. · supports · Purified subtilisin NAT · source_derived_draft · unverified_draft

    Heat treatment at 120 C for 15 min markedly increased the ACE-inhibitory activity of subtilisin NAT while inactivating it as a protease and fragmenting it into small peptides.
    Complete structured claim and evidence

  3. The Phe-Tyr dipeptide, liberated in the same way, inhibited angiotensin-converting enzyme.

    Phe-Tyr dipeptide → Human angiotensin-converting enzyme / ACE source_derived_draftungraded
    Experimental context and source evidence
    duration
    Not stated here
    evidence_access
    Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
    experimental_model
    Purified enzyme assay
    exposure
    FY dipeptide
    limitations
    As above.
    organism
    Purified enzyme assay
    plain_language
    The Phe-Tyr dipeptide, liberated in the same way, inhibited angiotensin-converting enzyme.
    primary_references
    Inhibition of angiotensin I converting enzyme by subtilisin NAT (nattokinase) in natto, a Japanese traditional fermented food. (2012) https://pubmed.ncbi.nlm.nih.gov/22453301/ DOI: 10.1039/c2fo10245e
    route
    In vitro
    tissue
    ACE inhibition kinetics

    Nattokinase: what the purified enzyme cleaves, what survives being eaten, and the gap between the two (2026-09-23) · lines 708–708

    Original AI-assisted curation built from a supplied entity-first document of 105 entities and 129 claims. Every reference in that document was resolved against live PubMed with its abstract read and its DOI cross-checked on 2026-09-23, and the EFSA novel-food opinion was retrieved and read in full. That check corrected two PMIDs that pointed at unrelated papers, two DOIs, and two papers recorded as carrying no erratum that do carry one; it also reversed three findings the supplied document had stated backwards. Two papers carry a published correction, recorded as such and not as a retraction. Three sources are not indexed in PubMed and are cited by what they have. Laboratory lineages are recorded, so the four papers from one group, the three from another and the two readings of a single applicant dossier cannot be counted as separate lines of support. Study-specific doses, units, populations and limitations retained; activity units are never converted between systems. Not publisher full text. · supports · Purified enzyme assay · source_derived_draft · unverified_draft

    The Phe-Tyr dipeptide, liberated in the same way, inhibited angiotensin-converting enzyme.
    Complete structured claim and evidence

  4. The Leu-Gly-Gly peptide identified from simulated digestion inhibited ACE competitively with an IC50 of 10.78 micromolar.

    Leu-Gly-Gly peptide → Human angiotensin-converting enzyme / ACE source_derived_draftungraded
    Experimental context and source evidence
    duration
    Not stated here
    evidence_access
    Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
    experimental_model
    In vitro simulated digestion
    exposure
    LGG peptide
    limitations
    An IC50 against purified ACE. Docking and network-pharmacology analyses in the same report are modelling, not measurement.
    organism
    In vitro simulated digestion
    plain_language
    The Leu-Gly-Gly peptide identified from simulated digestion inhibited ACE competitively with an IC50 of 10.78 micromolar.
    primary_references
    Identification and mechanistic characterization of novel ACE-inhibitory peptides derived from Nattokinase. (2026) https://pubmed.ncbi.nlm.nih.gov/41844106/ DOI: 10.1016/j.foodchem.2026.148875
    route
    In vitro
    tissue
    ACE inhibition kinetics with molecular docking

    Nattokinase: what the purified enzyme cleaves, what survives being eaten, and the gap between the two (2026-09-23) · lines 719–719

    Original AI-assisted curation built from a supplied entity-first document of 105 entities and 129 claims. Every reference in that document was resolved against live PubMed with its abstract read and its DOI cross-checked on 2026-09-23, and the EFSA novel-food opinion was retrieved and read in full. That check corrected two PMIDs that pointed at unrelated papers, two DOIs, and two papers recorded as carrying no erratum that do carry one; it also reversed three findings the supplied document had stated backwards. Two papers carry a published correction, recorded as such and not as a retraction. Three sources are not indexed in PubMed and are cited by what they have. Laboratory lineages are recorded, so the four papers from one group, the three from another and the two readings of a single applicant dossier cannot be counted as separate lines of support. Study-specific doses, units, populations and limitations retained; activity units are never converted between systems. Not publisher full text. · supports · In vitro simulated digestion · source_derived_draft · unverified_draft

    The Leu-Gly-Gly peptide identified from simulated digestion inhibited ACE competitively with an IC50 of 10.78 micromolar.
    Complete structured claim and evidence

  5. The Leu-Tyr dipeptide, liberated by fragmentation of subtilisin NAT, inhibited angiotensin-converting enzyme.

    Leu-Tyr dipeptide → Human angiotensin-converting enzyme / ACE source_derived_draftungraded
    Experimental context and source evidence
    duration
    Not stated here
    evidence_access
    Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
    experimental_model
    Purified enzyme assay
    exposure
    LY dipeptide
    limitations
    Its presence in the heat-inactivated material was confirmed by HPLC-MS. No human exposure measurement exists for it.
    organism
    Purified enzyme assay
    plain_language
    The Leu-Tyr dipeptide, liberated by fragmentation of subtilisin NAT, inhibited angiotensin-converting enzyme.
    primary_references
    Inhibition of angiotensin I converting enzyme by subtilisin NAT (nattokinase) in natto, a Japanese traditional fermented food. (2012) https://pubmed.ncbi.nlm.nih.gov/22453301/ DOI: 10.1039/c2fo10245e
    route
    In vitro
    tissue
    ACE inhibition kinetics

    Nattokinase: what the purified enzyme cleaves, what survives being eaten, and the gap between the two (2026-09-23) · lines 697–697

    Original AI-assisted curation built from a supplied entity-first document of 105 entities and 129 claims. Every reference in that document was resolved against live PubMed with its abstract read and its DOI cross-checked on 2026-09-23, and the EFSA novel-food opinion was retrieved and read in full. That check corrected two PMIDs that pointed at unrelated papers, two DOIs, and two papers recorded as carrying no erratum that do carry one; it also reversed three findings the supplied document had stated backwards. Two papers carry a published correction, recorded as such and not as a retraction. Three sources are not indexed in PubMed and are cited by what they have. Laboratory lineages are recorded, so the four papers from one group, the three from another and the two readings of a single applicant dossier cannot be counted as separate lines of support. Study-specific doses, units, populations and limitations retained; activity units are never converted between systems. Not publisher full text. · supports · Purified enzyme assay · source_derived_draft · unverified_draft

    The Leu-Tyr dipeptide, liberated by fragmentation of subtilisin NAT, inhibited angiotensin-converting enzyme.
    Complete structured claim and evidence

  6. The Thr-Trp peptide from the same digestion acted as a noncompetitive ACE inhibitor.

    Thr-Trp dipeptide → Human angiotensin-converting enzyme / ACE source_derived_draftungraded
    Experimental context and source evidence
    duration
    Not stated here
    evidence_access
    Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
    experimental_model
    In vitro simulated digestion
    exposure
    TW peptide
    limitations
    As above. A different inhibition mode from LGG in the same peptide pool.
    organism
    In vitro simulated digestion
    plain_language
    The Thr-Trp peptide from the same digestion acted as a noncompetitive ACE inhibitor.
    primary_references
    Identification and mechanistic characterization of novel ACE-inhibitory peptides derived from Nattokinase. (2026) https://pubmed.ncbi.nlm.nih.gov/41844106/ DOI: 10.1016/j.foodchem.2026.148875
    route
    In vitro
    tissue
    ACE inhibition kinetics with molecular docking

    Nattokinase: what the purified enzyme cleaves, what survives being eaten, and the gap between the two (2026-09-23) · lines 730–730

    Original AI-assisted curation built from a supplied entity-first document of 105 entities and 129 claims. Every reference in that document was resolved against live PubMed with its abstract read and its DOI cross-checked on 2026-09-23, and the EFSA novel-food opinion was retrieved and read in full. That check corrected two PMIDs that pointed at unrelated papers, two DOIs, and two papers recorded as carrying no erratum that do carry one; it also reversed three findings the supplied document had stated backwards. Two papers carry a published correction, recorded as such and not as a retraction. Three sources are not indexed in PubMed and are cited by what they have. Laboratory lineages are recorded, so the four papers from one group, the three from another and the two readings of a single applicant dossier cannot be counted as separate lines of support. Study-specific doses, units, populations and limitations retained; activity units are never converted between systems. Not publisher full text. · supports · In vitro simulated digestion · source_derived_draft · unverified_draft

    The Thr-Trp peptide from the same digestion acted as a noncompetitive ACE inhibitor.
    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