{"id":"03417d53-edb0-56f7-bae0-2c24dbc105a7","stable_key":"59b18080-c560-563d-abc5-bac4ee82a27c:ergothioneine-egte-sulfenic","predicate":"converts","statement":"Biochemical characterization of Mycobacterium smegmatis EgtE supported sulfoxide substrate processing through a sulfenic-acid intermediate toward ergothioneine.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"d2e84f0e-c2ce-5810-b1c6-1f0f0b95644d","mechanism_event_label":"Sulfur is retained while the cysteine carbon scaffold is removed.","subject":{"id":"dc1ac837-e506-5809-9dfe-21aece031fcf","slug":"mycobacterium-smegmatis-egte","display_name":"Mycobacterium smegmatis EgtE","entity_type_key":"protein"},"object":{"id":"f7086495-5e10-536b-81b3-e63590cf156d","slug":"hercynylcysteine-sulfoxide","display_name":"Hercynylcysteine sulfoxide","entity_type_key":"small_molecule"},"evidence_count":1,"mechanism_event":{"id":"d2e84f0e-c2ce-5810-b1c6-1f0f0b95644d","stable_key":"59b18080-c560-563d-abc5-bac4ee82a27c:ergothioneine-egte-sulfenic-event","event_type":"observed_relationship","label":"Sulfur is retained while the cysteine carbon scaffold is removed.","description":"Biochemical characterization of Mycobacterium smegmatis EgtE supported sulfoxide substrate processing through a sulfenic-acid intermediate toward ergothioneine.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"dc1ac837-e506-5809-9dfe-21aece031fcf","slug":"mycobacterium-smegmatis-egte","display_name":"Mycobacterium smegmatis EgtE","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"f7086495-5e10-536b-81b3-e63590cf156d","slug":"hercynylcysteine-sulfoxide","display_name":"Hercynylcysteine sulfoxide","entity_type_key":"small_molecule"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"939c92c3-50ea-5a4a-9654-8e3b94448132","slug":"ergothioneine","display_name":"L-Ergothioneine","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""}]},"contexts":[{"dimension":"evidence_access","value_text":"Primary abstract","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"In vitro enzyme characterization.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Intermediate assignment is mechanistically supported; full intracellular flux was not measured.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"Ergothioneine collection; molecular form, preparation, species, exposure and manipulation remain explicit.","comparator":null,"unit":null,"notes":"","entity":{"slug":"ergothioneine","display_name":"L-Ergothioneine","entity_type_key":"small_molecule"}},{"dimension":"plain_language","value_text":"Sulfur is retained while the cysteine carbon scaffold is removed.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"Mechanistic studies of a novel C-S lyase in ergothioneine biosynthesis: the involvement of a sulfenic acid intermediate. · 2015 · https://pubmed.ncbi.nlm.nih.gov/26149121/ · DOI 10.1038/srep11870","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"28fc8fd1-4302-5266-8b5e-199cb67fbf59","evidence_kind":"source_excerpt","locator":"Lines 208-214","start_line":208,"end_line":214,"excerpt":"## ergothioneine-egte-sulfenic\nSulfur is retained while the cysteine carbon scaffold is removed.\nBiochemical characterization of Mycobacterium smegmatis EgtE supported sulfoxide substrate processing through a sulfenic-acid intermediate toward ergothioneine.\nModel: In vitro enzyme characterization.\nLimitations: Intermediate assignment is mechanistically supported; full intracellular flux was not measured.\nEvidence access: Primary abstract\nMechanistic studies of a novel C-S lyase in ergothioneine biosynthesis: the involvement of a sulfenic acid intermediate. · 2015 · https://pubmed.ncbi.nlm.nih.gov/26149121/ · DOI 10.1038/srep11870","model_system":"In vitro enzyme characterization.","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":"2f037d98-f3d0-5dbe-80d8-90b738f130d6","stable_key":"import-59b18080-c560-563d-abc5-bac4ee82a27c","title":"Ergothioneine: transport, redox chemistry 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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