{"id":"6c4eea43-864e-5e84-a690-6c6cc56fd787","stable_key":"88eb7407-f147-558b-889b-0c89c4e0aa4a:spermidine-dohh-oxygen","predicate":"forms_peroxo_intermediate_in","statement":"Human DOHH structures resolved a peroxo-diiron intermediate involved in hydroxylating deoxyhypusine-eIF5A.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"bc9bdce5-d492-5564-94a7-05aac3e13ba2","mechanism_event_label":"Oxygen chemistry completes the protein modification.","subject":{"id":"899c7ab0-6f81-5b38-a6bd-fbb33d66ac8d","slug":"oxygen","display_name":"Molecular oxygen","entity_type_key":"small_molecule"},"object":{"id":"185dae5b-798b-5fd2-b28d-57b640045a0f","slug":"dohh","display_name":"DOHH","entity_type_key":"protein"},"evidence_count":1,"mechanism_event":{"id":"bc9bdce5-d492-5564-94a7-05aac3e13ba2","stable_key":"88eb7407-f147-558b-889b-0c89c4e0aa4a:spermidine-dohh-oxygen-event","event_type":"observed_relationship","label":"Oxygen chemistry completes the protein modification.","description":"Human DOHH structures resolved a peroxo-diiron intermediate involved in hydroxylating deoxyhypusine-eIF5A.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"899c7ab0-6f81-5b38-a6bd-fbb33d66ac8d","slug":"oxygen","display_name":"Molecular oxygen","entity_type_key":"small_molecule"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"185dae5b-798b-5fd2-b28d-57b640045a0f","slug":"dohh","display_name":"DOHH","entity_type_key":"protein"},"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":"fd7586aa-2477-5fbf-b715-1fd83e0c5483","slug":"eif5a1-hypusine","display_name":"eIF5A1 with hypusine at residue 50","entity_type_key":"protein_state"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""},{"entity":{"id":"59d6d1cd-df32-5b58-b950-3188bc7b95d6","slug":"iron-ii","display_name":"Ferrous iron","entity_type_key":"ion"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":4,"notes":""}]},"contexts":[{"dimension":"evidence_access","value_text":"Primary abstract","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Human enzyme; 1.7-angstrom structures and spectroscopy.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"DOHH is not a collagen-type 2-oxoglutarate hydroxylase; do not infer the same vitamin C requirement.","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":"Oxygen chemistry completes the protein modification.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"Crystal Structure of the Peroxo-diiron(III) Intermediate of Deoxyhypusine Hydroxylase, an Oxygenase Involved in Hypusination. · 2015 · https://pubmed.ncbi.nlm.nih.gov/25865244/ · DOI 10.1016/j.str.2015.03.002","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"66e1582a-a323-5b3f-ae11-7b4037bb95e7","evidence_kind":"source_excerpt","locator":"Lines 62-68","start_line":62,"end_line":68,"excerpt":"## spermidine-dohh-oxygen\nOxygen chemistry completes the protein modification.\nHuman DOHH structures resolved a peroxo-diiron intermediate involved in hydroxylating deoxyhypusine-eIF5A.\nModel: Human enzyme; 1.7-angstrom structures and spectroscopy.\nLimitations: DOHH is not a collagen-type 2-oxoglutarate hydroxylase; do not infer the same vitamin C requirement.\nEvidence access: Primary abstract\nCrystal Structure of the Peroxo-diiron(III) Intermediate of Deoxyhypusine Hydroxylase, an Oxygenase Involved in Hypusination. · 2015 · https://pubmed.ncbi.nlm.nih.gov/25865244/ · DOI 10.1016/j.str.2015.03.002","model_system":"Human enzyme; 1.7-angstrom structures and spectroscopy.","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. 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