{"id":"fa229ea5-1311-57c0-9c32-668506112115","stable_key":"c3df3634-4c3a-5099-a5d9-e4f6344c1084:dohh-eif5a-hypusine","predicate":"hydroxylates","statement":"DOHH hydroxylates deoxyhypusine-eIF5A to hypusine-eIF5A using its oxygen-activating diiron center.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"9628bf46-2143-5f93-ad3b-d929896ba13b","mechanism_event_label":"A second enzyme completes the special modification.","subject":{"id":"185dae5b-798b-5fd2-b28d-57b640045a0f","slug":"dohh","display_name":"DOHH","entity_type_key":"protein"},"object":{"id":"a4d54591-b5a7-5e54-a52c-7011ace70819","slug":"eif5a1-deoxyhypusine","display_name":"eIF5A1 with deoxyhypusine at residue 50","entity_type_key":"protein_state"},"evidence_count":1,"mechanism_event":{"id":"9628bf46-2143-5f93-ad3b-d929896ba13b","stable_key":"c3df3634-4c3a-5099-a5d9-e4f6344c1084:dohh-eif5a-hypusine-event","event_type":"biochemical_relationship","label":"A second enzyme completes the special modification.","description":"DOHH hydroxylates deoxyhypusine-eIF5A to hypusine-eIF5A using its oxygen-activating diiron center.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"185dae5b-798b-5fd2-b28d-57b640045a0f","slug":"dohh","display_name":"DOHH","entity_type_key":"protein"},"role":"enzyme","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"a4d54591-b5a7-5e54-a52c-7011ace70819","slug":"eif5a1-deoxyhypusine","display_name":"eIF5A1 with deoxyhypusine at residue 50","entity_type_key":"protein_state"},"role":"substrate","stoichiometry":null,"state_label":"","sequence_order":1,"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":"product","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""},{"entity":{"id":"59d6d1cd-df32-5b58-b950-3188bc7b95d6","slug":"iron-ii","display_name":"Ferrous iron","entity_type_key":"ion"},"role":"catalytic_metal","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""},{"entity":{"id":"899c7ab0-6f81-5b38-a6bd-fbb33d66ac8d","slug":"oxygen","display_name":"Molecular oxygen","entity_type_key":"small_molecule"},"role":"cosubstrate","stoichiometry":null,"state_label":"","sequence_order":4,"notes":""}]},"contexts":[{"dimension":"experimental_model","value_text":"Human DOHH structures and spectroscopy.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"DOHH is a diiron enzyme, not a 2-oxoglutarate-dependent hydroxylase. This reaction modifies lysine already in a protein. It does not show that extra oral lysine increases the reaction or improves a clinical outcome.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"organism","value_text":"Human","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"A second enzyme completes the special modification.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[dohh-2015] 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},{"dimension":"tissue_or_cell_type","value_text":"Not specified as a whole tissue; see experimental model.","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"abba22e0-d538-5138-a1a8-88c39c723682","evidence_kind":"source_excerpt","locator":"Lines 588-596","start_line":588,"end_line":596,"excerpt":"### dohh-eif5a-hypusine\nDOHH hydroxylates deoxyhypusine-eIF5A to hypusine-eIF5A using its oxygen-activating diiron center.\nPlain language: A second enzyme completes the special modification.\nCondition category: normal\norganism: Human\ntissue_or_cell_type: Not specified as a whole tissue; see experimental model.\nexperimental_model: Human DOHH structures and spectroscopy.\nlimitations: DOHH is a diiron enzyme, not a 2-oxoglutarate-dependent hydroxylase. This reaction modifies lysine already in a protein. It does not show that extra oral lysine increases the reaction or improves a clinical outcome.\n[dohh-2015] 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","model_system":"Human DOHH structures and spectroscopy.","directness":"author_interpretation","verification_status":"source_derived_draft","notes":"Exact quote from the accompanying curation document, not from publisher text. Original study references: [dohh-2015] 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","relationship":"supports","weight":1.0,"link_notes":"","source":{"id":"7633bde7-dcc9-5086-91c6-a45eb96857f3","stable_key":"import-c3df3634-4c3a-5099-a5d9-e4f6344c1084","title":"L-Lysine: mechanism-first literature curation (2026-09-17)","document_type":"imported_text","citation_label":"AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text.","file_path":"","sha256":"93998d47c21525409ba82f1c82ededf2893dff15fbe61c7deffc175b0e298e97","revision_id":"3897e31f-6624-59e1-a053-8a81b7361632","review_status":"unverified_draft","notes":""}}],"relations":[],"conflicts":[],"corrections":[],"research":null}