{"id":"7d9e8b5e-17bf-51b9-b2e7-270db1028f6d","stable_key":"44eaeae5-557a-552b-8998-884f30462e2a:sulforaphane-gss-second-step","predicate":"catalyzes_formation_of","statement":"Human GSS joins gamma-glutamylcysteine and glycine in an ATP-dependent reaction to form glutathione.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"ef6c773f-ccf1-545a-9d48-e1d381593f00","mechanism_event_label":"A second enzyme, glycine and energy complete the molecule.","subject":{"id":"4f530f0d-22df-58fb-82a8-976e76f875cb","slug":"gss","display_name":"Human glutathione synthetase / GSS","entity_type_key":"protein"},"object":{"id":"b44c9e27-4bbb-52d3-a022-14cddded5073","slug":"glutathione","display_name":"GSH","entity_type_key":"small_molecule"},"evidence_count":1,"mechanism_event":{"id":"ef6c773f-ccf1-545a-9d48-e1d381593f00","stable_key":"44eaeae5-557a-552b-8998-884f30462e2a:sulforaphane-gss-second-step-event","event_type":"biochemical_relationship","label":"A second enzyme, glycine and energy complete the molecule.","description":"Human GSS joins gamma-glutamylcysteine and glycine in an ATP-dependent reaction to form glutathione.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"d47d2006-2fb8-56ea-a76a-7919171f66ce","slug":"gamma-glutamylcysteine","display_name":"Gamma-glutamylcysteine","entity_type_key":"small_molecule"},"role":"substrate","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"2b507258-430c-51fe-9fd2-e510c2c197a9","slug":"glycine","display_name":"Glycine","entity_type_key":"small_molecule"},"role":"substrate","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"58b974f1-d389-5bf6-81cd-889c44442c42","slug":"atp","display_name":"ATP","entity_type_key":"small_molecule"},"role":"energy_substrate","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""},{"entity":{"id":"4f530f0d-22df-58fb-82a8-976e76f875cb","slug":"gss","display_name":"Human glutathione synthetase / GSS","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""},{"entity":{"id":"b44c9e27-4bbb-52d3-a022-14cddded5073","slug":"glutathione","display_name":"GSH","entity_type_key":"small_molecule"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":4,"notes":""}]},"contexts":[{"dimension":"evidence_span","value_text":"{\"source_cache\": \"artifacts/sulforaphane-research/30581542.fulltext.txt\", \"locator\": \"Primary full-text span; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"77cf6674cf9b9bc140a228588a53c937966fd3a67397c1c4970221c5cc58a0b1\", \"start_char\": 923, \"end_char\": 1092, \"text_sha256\": \"bed9ef1323b513b1e31b65277f28b935ddf0c9b0c83cbe9ee9f827f97806846c\"}","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Human enzyme mutagenesis, kinetics and molecular dynamics","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"S-loop variants; established biosynthetic reactions described in the introduction","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Reaction descriptions are background chemistry in a primary enzyme paper, not evidence that sulforaphane corrects inherited GSS deficiency.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"Sulforaphane research collection; topical membership is not evidence of a direct dietary effect.","comparator":null,"unit":null,"notes":"","entity":{"slug":"sulforaphane","display_name":"Sulforaphane / SFN, stereochemistry specified per study","entity_type_key":"small_molecule"}},{"dimension":"organism","value_text":"Human GSS","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"A second enzyme, glycine and energy complete the molecule.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[sulforaphane-p30581542] Genetic Mutations in the S-loop of Human Glutathione Synthetase: Links Between Substrate Binding, Active Site Structure and Allostery. (2019). https://pubmed.ncbi.nlm.nih.gov/30581542/ DOI: 10.1016/j.csbj.2018.11.008","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Glutathione synthesis and substrate binding","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"38affbf2-171a-5a3d-a286-63a975e06019","evidence_kind":"source_excerpt","locator":"Lines 853-864","start_line":853,"end_line":864,"excerpt":"### sulforaphane-gss-second-step\nHuman GSS joins gamma-glutamylcysteine and glycine in an ATP-dependent reaction to form glutathione.\nCondition category: normal\nnutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: A second enzyme, glycine and energy complete the molecule.\norganism: Human GSS\ntissue_or_cell_type: Glutathione synthesis and substrate binding\nexperimental_model: Human enzyme mutagenesis, kinetics and molecular dynamics\nlimitations: Reaction descriptions are background chemistry in a primary enzyme paper, not evidence that sulforaphane corrects inherited GSS deficiency.\nexposure: S-loop variants; established biosynthetic reactions described in the introduction\nevidence_span: {\"source_cache\": \"artifacts/sulforaphane-research/30581542.fulltext.txt\", \"locator\": \"Primary full-text span; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"77cf6674cf9b9bc140a228588a53c937966fd3a67397c1c4970221c5cc58a0b1\", \"start_char\": 923, \"end_char\": 1092, \"text_sha256\": \"bed9ef1323b513b1e31b65277f28b935ddf0c9b0c83cbe9ee9f827f97806846c\"}\n[sulforaphane-p30581542] Genetic Mutations in the S-loop of Human Glutathione Synthetase: Links Between Substrate Binding, Active Site Structure and Allostery. (2019). https://pubmed.ncbi.nlm.nih.gov/30581542/ DOI: 10.1016/j.csbj.2018.11.008","model_system":"Human enzyme mutagenesis, kinetics and molecular dynamics","directness":"author_interpretation","verification_status":"source_derived_draft","notes":"Exact curation-document quotation, not publisher quotation. Study references: [sulforaphane-p30581542] Genetic Mutations in the S-loop of Human Glutathione Synthetase: Links Between Substrate Binding, Active Site Structure and Allostery. (2019). https://pubmed.ncbi.nlm.nih.gov/30581542/ DOI: 10.1016/j.csbj.2018.11.008","relationship":"supports","weight":1.0,"link_notes":"","source":{"id":"a4bafbf7-f117-53c9-a6d7-8fb25e4aca72","stable_key":"import-44eaeae5-557a-552b-8998-884f30462e2a","title":"Sulforaphane: formation, electrophile sensing 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":"f355c492a6c35673d8260b1328667fe206e5315b9fcaa5aeff53d80373c7ef97","revision_id":"f2c47d71-34cd-5160-8e92-fe196b576707","review_status":"unverified_draft","notes":""}}],"relations":[],"conflicts":[],"corrections":[],"research":null}