Component

Nattokinase catalytic turnover on a model peptide substrate

The kcat term measured against succinyl-Ala-Ala-Pro-Phe-p-nitroanilide.

1 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.

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. Alanine substitution at Ser33, Asp60, Ser62 or Thr220 raised the free energy of the transition state and lowered kcat.

    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    duration
    Not stated here
    evidence_access
    Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
    experimental_model
    Recombinant subtilisin NK mutants
    exposure
    Ser33Ala, Asp60Ala, Ser62Ala and Thr220Ala single mutants
    limitations
    Measured against succinyl-Ala-Ala-Pro-Phe-p-nitroanilide. The exact kinetic constants were not extracted for this ledger, and an effect size on a chromogenic model substrate does not transfer to fibrin, PAI-1 or von Willebrand factor.
    organism
    Recombinant subtilisin NK mutants
    plain_language
    Alanine substitution at Ser33, Asp60, Ser62 or Thr220 raised the free energy of the transition state and lowered kcat.
    primary_references
    Probing the importance of hydrogen bonds in the active site of the subtilisin nattokinase by site-directed mutagenesis and molecular dynamics simulation. (2006) https://pubmed.ncbi.nlm.nih.gov/16411898/ DOI: 10.1042/BJ20050772
    route
    In vitro
    tissue
    Enzyme kinetics with molecular dynamics and free-energy perturbation
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Nattokinase: what the purified enzyme cleaves, what survives being eaten, and the gap between the two (2026-09-23) · lines 70–70

    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 · Recombinant subtilisin NK mutants · source_derived_draft · unverified_draft

    Alanine substitution at Ser33, Asp60, Ser62 or Thr220 raised the free energy of the transition state and lowered kcat.
    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