{"id":"2a15bc8a-db23-5a43-a4e8-d2059cb97079","stable_key":"b7798a90-72a3-5454-a321-c4be88bf0cc4:lithium-bpnt1-substrate","predicate":"hydrolyzes","statement":"Cloned rat RnPIP hydrolyzed PAP and Ins(1,4)P2 in magnesium-dependent reactions.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"35138c67-355c-5a90-869a-475c0326289c","mechanism_event_label":"Clearing a sulfur-pathway by-product uses another metal-dependent enzyme.","subject":{"id":"205b1d9e-7bfc-58ac-8a4f-1b4942ae521f","slug":"rat-bpnt1","display_name":"Rat bisphosphate nucleotidase 1 / RnPIP","entity_type_key":"protein"},"object":{"id":"c056d2b3-6cf8-500a-a641-1f19dd82cfd4","slug":"pap","display_name":"3-prime-Phosphoadenosine-5-prime-phosphate / PAP","entity_type_key":"small_molecule"},"evidence_count":1,"mechanism_event":{"id":"35138c67-355c-5a90-869a-475c0326289c","stable_key":"b7798a90-72a3-5454-a321-c4be88bf0cc4:lithium-bpnt1-substrate-event","event_type":"observed_relationship","label":"Clearing a sulfur-pathway by-product uses another metal-dependent enzyme.","description":"Cloned rat RnPIP hydrolyzed PAP and Ins(1,4)P2 in magnesium-dependent reactions.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"205b1d9e-7bfc-58ac-8a4f-1b4942ae521f","slug":"rat-bpnt1","display_name":"Rat bisphosphate nucleotidase 1 / RnPIP","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"c056d2b3-6cf8-500a-a641-1f19dd82cfd4","slug":"pap","display_name":"3-prime-Phosphoadenosine-5-prime-phosphate / PAP","entity_type_key":"small_molecule"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"8e2e3902-5e26-52e3-9c85-1d7c0ace1637","slug":"lithium","display_name":"Lithium","entity_type_key":"nutrient_element"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""},{"entity":{"id":"13b4b09c-4581-58f6-9792-9a78125963e8","slug":"lithium-ion","display_name":"Lithium ion (Li+)","entity_type_key":"ion"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""},{"entity":{"id":"bff427ab-35f9-59c2-bb24-fd5953bbaec2","slug":"magnesium-ion","display_name":"Mg2+","entity_type_key":"ion"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":4,"notes":""},{"entity":{"id":"5b09f2d6-d3ce-50ee-80d7-a77680b379a2","slug":"inositol-1-4-bisphosphate","display_name":"Myo-inositol 1,4-bisphosphate","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":5,"notes":""},{"entity":{"id":"44432084-b8c5-5d59-a682-6bc790ebbb6d","slug":"paps","display_name":"3-prime-Phosphoadenosine-5-prime-phosphosulfate / PAPS","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":6,"notes":""}]},"contexts":[{"dimension":"evidence_access","value_text":"Primary abstract","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Cloned rat enzyme; biochemical substrate assays.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"The paper proposes consequences for sulfotransferases/RNA processing; those downstream effects were not all tested.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"Lithium collection; molecular form, preparation, species, exposure and manipulation remain explicit.","comparator":null,"unit":null,"notes":"","entity":{"slug":"lithium","display_name":"Lithium","entity_type_key":"nutrient_element"}},{"dimension":"plain_language","value_text":"Clearing a sulfur-pathway by-product uses another metal-dependent enzyme.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"A novel mammalian lithium-sensitive enzyme with a dual enzymatic activity, 3'-phosphoadenosine 5'-phosphate phosphatase and inositol-polyphosphate 1-phosphatase. · 1999 · https://pubmed.ncbi.nlm.nih.gov/10347153/ · DOI 10.1074/jbc.274.23.16034","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"3503a47f-cf17-50bc-aaaa-f1ce286b891c","evidence_kind":"source_excerpt","locator":"Lines 112-118","start_line":112,"end_line":118,"excerpt":"## lithium-bpnt1-substrate\nClearing a sulfur-pathway by-product uses another metal-dependent enzyme.\nCloned rat RnPIP hydrolyzed PAP and Ins(1,4)P2 in magnesium-dependent reactions.\nModel: Cloned rat enzyme; biochemical substrate assays.\nLimitations: The paper proposes consequences for sulfotransferases/RNA processing; those downstream effects were not all tested.\nEvidence access: Primary abstract\nA novel mammalian lithium-sensitive enzyme with a dual enzymatic activity, 3'-phosphoadenosine 5'-phosphate phosphatase and inositol-polyphosphate 1-phosphatase. · 1999 · https://pubmed.ncbi.nlm.nih.gov/10347153/ · DOI 10.1074/jbc.274.23.16034","model_system":"Cloned rat enzyme; biochemical substrate assays.","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":"b2dd2f3c-5c4c-5a12-9a0d-91b521ffcf98","stable_key":"import-b7798a90-72a3-5454-a321-c4be88bf0cc4","title":"Lithium: metal-sensitive enzymes, transport 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. 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