{"id":"821fe070-6211-55bc-9cf9-e0e574bb7490","stable_key":"33bef151-bdc7-5892-aff6-0345ab149739:nattokinase-cleaves-the-von-willebrand-factor-a2-domain","predicate":"proteolyzes","statement":"Nattokinase directly cleaved the folded von Willebrand factor A2 domain and the unstructured vWF73 peptide under static conditions, with Thr1608-Gly1609 as the primary site.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"negative","is_public":true,"mechanism_event_id":"b5d4edd2-7d53-5c15-8e34-be18c3fade43","mechanism_event_label":"Nattokinase directly cleaved the folded von Willebrand factor A2 domain and the unstructured vWF73 peptide under static conditions, with Thr1608-Gly1609 as the primary site.","subject":{"id":"6b03a125-209a-5060-8b35-ec9e0e54033c","slug":"nattokinase","display_name":"Nattokinase / subtilisin NAT","entity_type_key":"peptide"},"object":{"id":"d1c324a6-f2c0-550e-ad72-f3fa04a924f8","slug":"vwf","display_name":"Human von Willebrand factor / VWF","entity_type_key":"protein"},"evidence_count":1,"mechanism_event":{"id":"b5d4edd2-7d53-5c15-8e34-be18c3fade43","stable_key":"33bef151-bdc7-5892-aff6-0345ab149739:nattokinase-cleaves-the-von-willebrand-factor-a2-domain-event","event_type":"biochemical_relationship","label":"Nattokinase directly cleaved the folded von Willebrand factor A2 domain and the unstructured vWF73 peptide under static conditions, with Thr1608-Gly1609 as the primary site.","description":"In vitro enzymology with mass spectrometry","status":"provisional","compartment":null,"participants":[{"entity":{"id":"6b03a125-209a-5060-8b35-ec9e0e54033c","slug":"nattokinase","display_name":"Nattokinase / subtilisin NAT","entity_type_key":"peptide"},"role":"acting component","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"d1c324a6-f2c0-550e-ad72-f3fa04a924f8","slug":"vwf","display_name":"Human von Willebrand factor / VWF","entity_type_key":"protein"},"role":"component the finding is about","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""}]},"contexts":[{"dimension":"duration","value_text":"Not stated here","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"evidence_access","value_text":"Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Purified human von Willebrand factor constructs","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"Purified nattokinase","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"A purified-substrate system. The cleaved bond sits three residues downstream of the ADAMTS13 site Tyr1605-Met1606. No multimer endpoint and no human oral exposure were measured.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"organism","value_text":"Purified human von Willebrand factor constructs","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"Nattokinase directly cleaved the folded von Willebrand factor A2 domain and the unstructured vWF73 peptide under static conditions, with Thr1608-Gly1609 as the primary site.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"Degradation mechanism of the von Willebrand factor A2 domain by nattokinase. (2026) https://pubmed.ncbi.nlm.nih.gov/42163571/ DOI: 10.1002/1873-3468.70366","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"route","value_text":"In vitro","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue","value_text":"In vitro enzymology with mass spectrometry","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"b6725aa3-6be8-5324-921e-760f398c53f2","evidence_kind":"source_excerpt","locator":"Lines 169-169","start_line":169,"end_line":169,"excerpt":"Nattokinase directly cleaved the folded von Willebrand factor A2 domain and the unstructured vWF73 peptide under static conditions, with Thr1608-Gly1609 as the primary site.","model_system":"Purified human von Willebrand factor constructs","directness":"reported_statement","verification_status":"source_derived_draft","notes":"","relationship":"supports","weight":1.0,"link_notes":"","source":{"id":"41cb127c-1c23-53aa-b7d0-5ec7f6fa3c99","stable_key":"import-33bef151-bdc7-5892-aff6-0345ab149739","title":"Nattokinase: what the purified enzyme cleaves, what survives being eaten, and the gap between the two (2026-09-23)","document_type":"imported_text","citation_label":"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.","file_path":"","sha256":"34fc46e0e849d06bfa13cb099a79b50679dd6fd0de8a5a0575326afdde3259c1","revision_id":"efd063e6-e982-5f6e-a4b8-6f2ffe4185ce","review_status":"unverified_draft","notes":""}}],"relations":[{"id":"cd56b912-a00b-5e24-9ab5-eea5d3b1291f","relation_type":"limits_translation_of","notes":"The A2 cleavage is the strongest new molecular result here and has no human exposure bridge behind it.","source_claim_id":"140e1014-8105-56ca-b13a-76fe0d42e8d9","source_claim_key":"33bef151-bdc7-5892-aff6-0345ab149739:efsa-could-not-conclude-on-absorption-of-the-active-enzyme","source_statement":"EFSA concluded that the information provided on absorption, distribution, metabolism and excretion did not allow conclusions to be drawn on the absorption of active nattokinase or any functional metabolites derived from it.","target_claim_id":"821fe070-6211-55bc-9cf9-e0e574bb7490","target_claim_key":"33bef151-bdc7-5892-aff6-0345ab149739:nattokinase-cleaves-the-von-willebrand-factor-a2-domain","target_statement":"Nattokinase directly cleaved the folded von Willebrand factor A2 domain and the unstructured vWF73 peptide under static conditions, with Thr1608-Gly1609 as the primary site."}],"conflicts":[],"corrections":[],"research":null}