{"id":"9aa0a561-e07a-5db1-bb75-55187990ef5a","stable_key":"db0fc92e-b5ef-5667-a4c5-3ef257edbc9b:glutathione-bso-gcl","predicate":"inhibits","statement":"The bound BSO inhibitory species was phosphorylated on its sulfoximine nitrogen.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"dcbcb38e-3b0d-514c-8338-6effdf938f33","mechanism_event_label":"The inhibitor is chemically activated at the enzyme.","subject":{"id":"522ac38a-0bc1-57fb-a1e5-45ca2c14515c","slug":"buthionine-sulfoximine","display_name":"L-Buthionine-S-sulfoximine / BSO","entity_type_key":"small_molecule"},"object":{"id":"782a89cb-b15e-5b88-85e3-87ec8036ac1a","slug":"yeast-gsh1","display_name":"Saccharomyces cerevisiae glutamate-cysteine ligase Gsh1","entity_type_key":"protein"},"evidence_count":1,"mechanism_event":{"id":"dcbcb38e-3b0d-514c-8338-6effdf938f33","stable_key":"db0fc92e-b5ef-5667-a4c5-3ef257edbc9b:glutathione-bso-gcl-event","event_type":"biochemical_relationship","label":"The inhibitor is chemically activated at the enzyme.","description":"The bound BSO inhibitory species was phosphorylated on its sulfoximine nitrogen.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"522ac38a-0bc1-57fb-a1e5-45ca2c14515c","slug":"buthionine-sulfoximine","display_name":"L-Buthionine-S-sulfoximine / BSO","entity_type_key":"small_molecule"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"782a89cb-b15e-5b88-85e3-87ec8036ac1a","slug":"yeast-gsh1","display_name":"Saccharomyces cerevisiae glutamate-cysteine ligase Gsh1","entity_type_key":"protein"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""}]},"contexts":[{"dimension":"availability_state","value_text":"machinery_impairment","comparator":null,"unit":null,"notes":"Imported condition classification; unverified.","entity":null},{"dimension":"evidence_span","value_text":"{\"source_cache\": \"artifacts/glutathione-research/20220146.abstract.txt\", \"locator\": \"Primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"c456343cb9386a797d12af2169106d7f3b8033a5fa3882034609d3bbc26ae478\", \"start_char\": 0, \"end_char\": 1382, \"text_sha256\": \"c456343cb9386a797d12af2169106d7f3b8033a5fa3882034609d3bbc26ae478\"}","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Inhibited-enzyme crystallography","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"GSH and BSO-bound structures","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Binding geometry is species-specific; BSO is an experimental inhibitor, not dietary depletion.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"Glutathione research collection; topical membership is not evidence of a direct dietary effect.","comparator":null,"unit":null,"notes":"","entity":{"slug":"glutathione","display_name":"GSH","entity_type_key":"small_molecule"}},{"dimension":"organism","value_text":"Saccharomyces cerevisiae","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"The inhibitor is chemically activated at the enzyme.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[glutathione-p20220146] Structural basis for feedback and pharmacological inhibition of Saccharomyces cerevisiae glutamate cysteine ligase. (2010). https://pubmed.ncbi.nlm.nih.gov/20220146/ DOI: 10.1074/jbc.m110.104802","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Purified Gsh1","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"trigger_kind","value_text":"machinery_impairment","comparator":null,"unit":null,"notes":"Imported condition classification; unverified.","entity":null}],"evidence":[{"id":"ccbf35a3-6ec1-5f20-bfab-197af62b730c","evidence_kind":"source_excerpt","locator":"Lines 372-383","start_line":372,"end_line":383,"excerpt":"### glutathione-bso-gcl\nThe bound BSO inhibitory species was phosphorylated on its sulfoximine nitrogen.\nCondition category: machinery_impairment\nnutrient_topic: Glutathione research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: The inhibitor is chemically activated at the enzyme.\norganism: Saccharomyces cerevisiae\ntissue_or_cell_type: Purified Gsh1\nexperimental_model: Inhibited-enzyme crystallography\nlimitations: Binding geometry is species-specific; BSO is an experimental inhibitor, not dietary depletion.\nexposure: GSH and BSO-bound structures\nevidence_span: {\"source_cache\": \"artifacts/glutathione-research/20220146.abstract.txt\", \"locator\": \"Primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"c456343cb9386a797d12af2169106d7f3b8033a5fa3882034609d3bbc26ae478\", \"start_char\": 0, \"end_char\": 1382, \"text_sha256\": \"c456343cb9386a797d12af2169106d7f3b8033a5fa3882034609d3bbc26ae478\"}\n[glutathione-p20220146] Structural basis for feedback and pharmacological inhibition of Saccharomyces cerevisiae glutamate cysteine ligase. 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