{"id":"5047dcb7-5d35-56e8-91aa-b593779e3cae","stable_key":"88eb7407-f147-558b-889b-0c89c4e0aa4a:spermidine-paox-acetylspermine","predicate":"oxidizes","statement":"Human PAOX oxidized N1-acetylspermine with Km 0.85 micromolar and kcat 31.7 per second.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"f49eed38-719e-5380-96e0-3568362a607a","mechanism_event_label":"Back-conversion depends on which polyamine was acetylated.","subject":{"id":"80b7a4f6-c2c5-5ee1-8fab-c3500bb5c79c","slug":"paox","display_name":"Human N1-acetylpolyamine oxidase / PAOX","entity_type_key":"protein"},"object":{"id":"6ebd5e63-4e9d-5268-97ea-587dec320835","slug":"n1-acetylspermine","display_name":"N1-Acetylspermine","entity_type_key":"small_molecule"},"evidence_count":1,"mechanism_event":{"id":"f49eed38-719e-5380-96e0-3568362a607a","stable_key":"88eb7407-f147-558b-889b-0c89c4e0aa4a:spermidine-paox-acetylspermine-event","event_type":"observed_relationship","label":"Back-conversion depends on which polyamine was acetylated.","description":"Human PAOX oxidized N1-acetylspermine with Km 0.85 micromolar and kcat 31.7 per second.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"80b7a4f6-c2c5-5ee1-8fab-c3500bb5c79c","slug":"paox","display_name":"Human N1-acetylpolyamine oxidase / PAOX","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"6ebd5e63-4e9d-5268-97ea-587dec320835","slug":"n1-acetylspermine","display_name":"N1-Acetylspermine","entity_type_key":"small_molecule"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"7014993c-468f-5c6b-ab04-80c87f9dfd9f","slug":"spermidine","display_name":"Spermidine","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""},{"entity":{"id":"ded80d0b-9076-5034-9e87-cd38f7dafae5","slug":"spermine","display_name":"Spermine","entity_type_key":"small_molecule"},"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":"Purified human enzyme.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Substrate specificity differs from SMOX; enzyme turnover is not whole-body turnover.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"Spermidine collection; molecular form, preparation, species, exposure and manipulation remain explicit.","comparator":null,"unit":null,"notes":"","entity":{"slug":"spermidine","display_name":"Spermidine","entity_type_key":"small_molecule"}},{"dimension":"plain_language","value_text":"Back-conversion depends on which polyamine was acetylated.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"Properties of recombinant human N1-acetylpolyamine oxidase (hPAO): potential role in determining drug sensitivity. · 2005 · https://pubmed.ncbi.nlm.nih.gov/15791459/ · DOI 10.1007/s00280-004-0936-5","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"5b3c6143-7f95-5f8e-b961-8ac1a4c961a8","evidence_kind":"source_excerpt","locator":"Lines 102-108","start_line":102,"end_line":108,"excerpt":"## spermidine-paox-acetylspermine\nBack-conversion depends on which polyamine was acetylated.\nHuman PAOX oxidized N1-acetylspermine with Km 0.85 micromolar and kcat 31.7 per second.\nModel: Purified human enzyme.\nLimitations: Substrate specificity differs from SMOX; enzyme turnover is not whole-body turnover.\nEvidence access: Primary abstract\nProperties of recombinant human N1-acetylpolyamine oxidase (hPAO): potential role in determining drug sensitivity. · 2005 · https://pubmed.ncbi.nlm.nih.gov/15791459/ · DOI 10.1007/s00280-004-0936-5","model_system":"Purified human enzyme.","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":"4348f3f8-0180-58a3-b61c-55d03bb322d2","stable_key":"import-88eb7407-f147-558b-889b-0c89c4e0aa4a","title":"Spermidine: biosynthesis, hypusination, 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. Not publisher full text.","file_path":"","sha256":"8eec8784bc2bd0384cfd53c6603c4ced8e53c227d9ab29ed85594c43e34c68ef","revision_id":"7c421a18-4526-59f6-b84e-4be533bc35ac","review_status":"unverified_draft","notes":""}}],"relations":[],"conflicts":[],"corrections":[],"research":null}