{"id":"4e3e6b64-5ea7-5746-a846-95528107f2f3","stable_key":"335be270-ea4a-5c8e-ad04-964fd22a439e:vanadium-ptp-competitive","predicate":"competitively_inhibits","statement":"Vanadate competitively inhibited PTP1B with a reported Ki of 0.38 ± 0.02 micromolar.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"negative","is_public":true,"mechanism_event_id":"402de4d5-a4e7-5451-9b93-b62278ea76b1","mechanism_event_label":"A phosphate-like inhibitor can occupy a phosphatase’s catalytic machinery.","subject":{"id":"bef86a6e-28a0-5df9-9306-3f05991aa159","slug":"vanadate-v","display_name":"Vanadate(V), protonation/speciation dependent","entity_type_key":"chemical_species"},"object":{"id":"58af4c7b-a5f4-540c-85eb-28a6161d45e7","slug":"ptp1b-1997-assay-preparation","display_name":"PTP1B preparation in the 1997 vanadate inhibition study","entity_type_key":"protein"},"evidence_count":1,"mechanism_event":{"id":"402de4d5-a4e7-5451-9b93-b62278ea76b1","stable_key":"335be270-ea4a-5c8e-ad04-964fd22a439e:vanadium-ptp-competitive-event","event_type":"observed_relationship","label":"A phosphate-like inhibitor can occupy a phosphatase’s catalytic machinery.","description":"Vanadate competitively inhibited PTP1B with a reported Ki of 0.38 ± 0.02 micromolar.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"bef86a6e-28a0-5df9-9306-3f05991aa159","slug":"vanadate-v","display_name":"Vanadate(V), protonation/speciation dependent","entity_type_key":"chemical_species"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"58af4c7b-a5f4-540c-85eb-28a6161d45e7","slug":"ptp1b-1997-assay-preparation","display_name":"PTP1B preparation in the 1997 vanadate inhibition study","entity_type_key":"protein"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"c5cbad45-22c6-594b-ab6b-71880dab1b24","slug":"vanadium","display_name":"Vanadium","entity_type_key":"nutrient_element"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""},{"entity":{"id":"b28dfc54-a5ef-5f9e-ac1f-890b68e58dc3","slug":"inorganic-phosphate","display_name":"Inorganic phosphate","entity_type_key":"chemical_species"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""}]},"contexts":[{"dimension":"evidence_access","value_text":"Primary abstract","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Recombinant-enzyme kinetic study; construct species not resolved from accessed primary abstract.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Assay affinity is not a dietary threshold, and PTP1B is not the only phosphatase inhibited.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit.","comparator":null,"unit":null,"notes":"","entity":{"slug":"vanadium","display_name":"Vanadium","entity_type_key":"nutrient_element"}},{"dimension":"plain_language","value_text":"A phosphate-like inhibitor can occupy a phosphatase’s catalytic machinery.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"Mechanism of inhibition of protein-tyrosine phosphatases by vanadate and pervanadate. · 1997 · https://pubmed.ncbi.nlm.nih.gov/8995372/ · DOI 10.1074/jbc.272.2.843","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"53d14130-adc5-5fe5-bb21-f9fe196034bf","evidence_kind":"source_excerpt","locator":"Lines 14-20","start_line":14,"end_line":20,"excerpt":"## vanadium-ptp-competitive\nA phosphate-like inhibitor can occupy a phosphatase’s catalytic machinery.\nVanadate competitively inhibited PTP1B with a reported Ki of 0.38 ± 0.02 micromolar.\nModel: Recombinant-enzyme kinetic study; construct species not resolved from accessed primary abstract.\nLimitations: Assay affinity is not a dietary threshold, and PTP1B is not the only phosphatase inhibited.\nEvidence access: Primary abstract\nMechanism of inhibition of protein-tyrosine phosphatases by vanadate and pervanadate. · 1997 · https://pubmed.ncbi.nlm.nih.gov/8995372/ · DOI 10.1074/jbc.272.2.843","model_system":"Recombinant-enzyme kinetic study; construct species not resolved from accessed primary abstract.","directness":"reported_statement","verification_status":"source_derived_draft","notes":"Original curation paraphrase; evidence access and experimental limitations specified.","relationship":"supports","weight":1.0,"link_notes":"","source":{"id":"e4d5d0ba-529b-540f-96ed-e719d116ccfd","stable_key":"import-335be270-ea4a-5c8e-ad04-964fd22a439e","title":"Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19)","document_type":"imported_text","citation_label":"AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text.","file_path":"","sha256":"d36b30d972e756ca4d19b66f976980e206c65025bd4bbf4c127c17320bd019c2","revision_id":"70d42967-8032-5627-8670-f59841735e89","review_status":"unverified_draft","notes":""}}],"relations":[],"conflicts":[],"corrections":[],"research":null}