{"id":"036f9550-5fda-5626-b23f-fd545ae13da8","stable_key":"db0fc92e-b5ef-5667-a4c5-3ef257edbc9b:glutathione-glo1-methylglyoxal","predicate":"supports_glutathione_dependent_clearance_of","statement":"Human GLO1 catalyzes glutathione-dependent methylglyoxal inactivation.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"f99bf8f9-aad2-5fca-b29d-c6d7468b4752","mechanism_event_label":"Glutathione also participates in handling a reactive carbonyl compound.","subject":{"id":"6874ce5e-d0bf-5a34-b8e9-e3e9516be255","slug":"glo1","display_name":"Human glyoxalase I / GLO1","entity_type_key":"protein"},"object":{"id":"55c17a25-868a-5496-a200-88d9ec014558","slug":"methylglyoxal","display_name":"Methylglyoxal","entity_type_key":"small_molecule"},"evidence_count":1,"mechanism_event":{"id":"f99bf8f9-aad2-5fca-b29d-c6d7468b4752","stable_key":"db0fc92e-b5ef-5667-a4c5-3ef257edbc9b:glutathione-glo1-methylglyoxal-event","event_type":"biochemical_relationship","label":"Glutathione also participates in handling a reactive carbonyl compound.","description":"Human GLO1 catalyzes glutathione-dependent methylglyoxal inactivation.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"b44c9e27-4bbb-52d3-a022-14cddded5073","slug":"glutathione","display_name":"GSH","entity_type_key":"small_molecule"},"role":"reaction_partner","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"6874ce5e-d0bf-5a34-b8e9-e3e9516be255","slug":"glo1","display_name":"Human glyoxalase I / GLO1","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"55c17a25-868a-5496-a200-88d9ec014558","slug":"methylglyoxal","display_name":"Methylglyoxal","entity_type_key":"small_molecule"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""}]},"contexts":[{"dimension":"evidence_span","value_text":"{\"source_cache\": \"artifacts/glutathione-research/9218781.abstract.txt\", \"locator\": \"Primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"e00867a8f693a2a0e6506a87d162a52ce4aa75ac846c7b0495dcf6ad7c9330e1\", \"start_char\": 0, \"end_char\": 1251, \"text_sha256\": \"e00867a8f693a2a0e6506a87d162a52ce4aa75ac846c7b0495dcf6ad7c9330e1\"}","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Human GLO1 crystal structure","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"S-benzyl-GSH complex","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"The essential zinc site is biochemical evidence; neither zinc nor GSH supplementation was tested.","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":"Human","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"Glutathione also participates in handling a reactive carbonyl compound.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[glutathione-p9218781] Crystal structure of human glyoxalase I--evidence for gene duplication and 3D domain swapping. 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