{"id":"2d216f02-e167-53b5-a030-ac2a11a4a96b","stable_key":"db0fc92e-b5ef-5667-a4c5-3ef257edbc9b:glutathione-glrx2-deglutathionylation","predicate":"catalyzes","statement":"GLRX2 reduced glutathionylated substrates with lower rate but higher affinity than GLRX1, giving similar catalytic efficiency.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"b2d6deca-dd57-516b-901d-ab70b7b7d8da","mechanism_event_label":"Glutathione attached to a protein can be removed enzymatically.","subject":{"id":"4e5c4de6-8387-5f52-8dc1-dad3395221ad","slug":"glrx2","display_name":"Human glutaredoxin 2 / GLRX2","entity_type_key":"protein"},"object":{"id":"29df1b2e-5e9e-51a0-ab8a-2039e8a6a59c","slug":"glrx2-deglutathionylation","display_name":"Human GLRX2-mediated protein deglutathionylation","entity_type_key":"cellular_process"},"evidence_count":1,"mechanism_event":{"id":"b2d6deca-dd57-516b-901d-ab70b7b7d8da","stable_key":"db0fc92e-b5ef-5667-a4c5-3ef257edbc9b:glutathione-glrx2-deglutathionylation-event","event_type":"biochemical_relationship","label":"Glutathione attached to a protein can be removed enzymatically.","description":"GLRX2 reduced glutathionylated substrates with lower rate but higher affinity than GLRX1, giving similar catalytic efficiency.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"bd4266e7-f9ac-569f-af1d-a210d497d2ac","slug":"protein-glutathione-mixed-disulfides","display_name":"Protein-glutathione mixed disulfides / protein S-glutathionylation","entity_type_key":"protein_state"},"role":"substrate","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"b44c9e27-4bbb-52d3-a022-14cddded5073","slug":"glutathione","display_name":"GSH","entity_type_key":"small_molecule"},"role":"electron_donor","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"4e5c4de6-8387-5f52-8dc1-dad3395221ad","slug":"glrx2","display_name":"Human glutaredoxin 2 / GLRX2","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""},{"entity":{"id":"29df1b2e-5e9e-51a0-ab8a-2039e8a6a59c","slug":"glrx2-deglutathionylation","display_name":"Human GLRX2-mediated protein deglutathionylation","entity_type_key":"cellular_process"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""}]},"contexts":[{"dimension":"evidence_span","value_text":"{\"source_cache\": \"artifacts/glutathione-research/14676218.abstract.txt\", \"locator\": \"Primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"a7399b7d035bd3815c30362449b7986dea08873c824e05506d7db627a71daa84\", \"start_char\": 0, \"end_char\": 1398, \"text_sha256\": \"a7399b7d035bd3815c30362449b7986dea08873c824e05506d7db627a71daa84\"}","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Purified human glutaredoxin kinetics and mutants","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"GSH or NADPH/thioredoxin-reductase donor systems","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Biochemical electron-donor alternatives; no claim that all cellular GLRX2 uses one route.","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 GLRX1/GLRX2","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"Glutathione attached to a protein can be removed enzymatically.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[glutathione-p14676218] Human mitochondrial glutaredoxin reduces S-glutathionylated proteins with high affinity accepting electrons from either glutathione or thioredoxin reductase. (2004). https://pubmed.ncbi.nlm.nih.gov/14676218/ DOI: 10.1074/jbc.m312719200","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Glutathionylated substrates","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"722d6598-846d-5513-a28a-3e2709a48541","evidence_kind":"source_excerpt","locator":"Lines 814-825","start_line":814,"end_line":825,"excerpt":"### glutathione-glrx2-deglutathionylation\nGLRX2 reduced glutathionylated substrates with lower rate but higher affinity than GLRX1, giving similar catalytic efficiency.\nCondition category: normal\nnutrient_topic: Glutathione research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: Glutathione attached to a protein can be removed enzymatically.\norganism: Human GLRX1/GLRX2\ntissue_or_cell_type: Glutathionylated substrates\nexperimental_model: Purified human glutaredoxin kinetics and mutants\nlimitations: Biochemical electron-donor alternatives; no claim that all cellular GLRX2 uses one route.\nexposure: GSH or NADPH/thioredoxin-reductase donor systems\nevidence_span: {\"source_cache\": \"artifacts/glutathione-research/14676218.abstract.txt\", \"locator\": \"Primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"a7399b7d035bd3815c30362449b7986dea08873c824e05506d7db627a71daa84\", \"start_char\": 0, \"end_char\": 1398, \"text_sha256\": \"a7399b7d035bd3815c30362449b7986dea08873c824e05506d7db627a71daa84\"}\n[glutathione-p14676218] Human mitochondrial glutaredoxin reduces S-glutathionylated proteins with high affinity accepting electrons from either glutathione or thioredoxin reductase. (2004). https://pubmed.ncbi.nlm.nih.gov/14676218/ DOI: 10.1074/jbc.m312719200","model_system":"Purified human glutaredoxin kinetics and mutants","directness":"author_interpretation","verification_status":"source_derived_draft","notes":"Exact curation-document quotation, not publisher quotation. Study references: [glutathione-p14676218] Human mitochondrial glutaredoxin reduces S-glutathionylated proteins with high affinity accepting electrons from either glutathione or thioredoxin reductase. (2004). https://pubmed.ncbi.nlm.nih.gov/14676218/ DOI: 10.1074/jbc.m312719200","relationship":"supports","weight":1.0,"link_notes":"","source":{"id":"9b7417fd-059d-5683-b452-71d1e3cf82d0","stable_key":"import-db0fc92e-b5ef-5667-a4c5-3ef257edbc9b","title":"Glutathione: metabolism, signaling and nutrient connections (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":"2a5740c4a7e770aafe883fea47909b18bf5e174f211749935130a50f9dea2753","revision_id":"a64016dd-4b72-5954-a72d-0e61de854073","review_status":"unverified_draft","notes":""}}],"relations":[],"conflicts":[],"corrections":[],"research":null}