{"id":"8d746837-56b7-5aab-b371-4847b5a544c5","stable_key":"dc8975b1-95ff-5d9b-be17-a1c04610cca7:mo-nfs1-sulfur","predicate":"mobilizes_sulfur_from","statement":"Human NFS1 transferred sulfur from L-cysteine through an NFS1-bound persulfide intermediate to the rhodanese-like domain of MOCS3.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"cc7a1a89-5903-5cce-9f84-c2a1574de190","mechanism_event_label":"Cysteine supplies sulfur that becomes part of the molybdenum cofactor.","subject":{"id":"9838e184-216a-5a26-a8c5-1777b9dd2d90","slug":"nfs1","display_name":"Human cysteine desulfurase / NFS1","entity_type_key":"protein"},"object":{"id":"ca899f13-50ad-55e5-ab99-329ae0038c74","slug":"l-cysteine","display_name":"L-Cysteine","entity_type_key":"small_molecule"},"evidence_count":1,"mechanism_event":{"id":"cc7a1a89-5903-5cce-9f84-c2a1574de190","stable_key":"dc8975b1-95ff-5d9b-be17-a1c04610cca7:mo-nfs1-sulfur-event","event_type":"biochemical_relationship","label":"Cysteine supplies sulfur that becomes part of the molybdenum cofactor.","description":"Human NFS1 transferred sulfur from L-cysteine through an NFS1-bound persulfide intermediate to the rhodanese-like domain of MOCS3.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"6fec6f2a-0e68-575d-9307-e509e69d4ae1","slug":"nfs1-persulfide","display_name":"Human NFS1 sulfur-loaded persulfide state","entity_type_key":"protein_state"},"role":"intermediate","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"c9f482f8-899b-5a59-9745-05a8709d91a2","slug":"mocs3","display_name":"Human adenylyltransferase and sulfurtransferase / MOCS3","entity_type_key":"protein"},"role":"acceptor","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"465f4f2d-1739-5e2b-b6be-fbf625620555","slug":"mocs3-persulfide","display_name":"Human MOCS3 sulfur-loaded persulfide state","entity_type_key":"protein_state"},"role":"product","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""},{"entity":{"id":"c78d3c3c-59b9-5192-b7ec-498124752c92","slug":"lyrm4","display_name":"Human ISD11 / LYRM4","entity_type_key":"protein"},"role":"stabilizing partner","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""},{"entity":{"id":"9838e184-216a-5a26-a8c5-1777b9dd2d90","slug":"nfs1","display_name":"Human cysteine desulfurase / NFS1","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":4,"notes":""},{"entity":{"id":"ca899f13-50ad-55e5-ab99-329ae0038c74","slug":"l-cysteine","display_name":"L-Cysteine","entity_type_key":"small_molecule"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":5,"notes":""}]},"contexts":[{"dimension":"evidence_span","value_text":"{\"source_cache\": \"artifacts/molybdenum-research/18650437.abstract.txt\", \"locator\": \"Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"8180bd148722e8980ef5acbd4ae4c29a0d9d13da56bbccb91165a5eed4ab6f50\", \"start_char\": 0, \"end_char\": 1547, \"text_sha256\": \"8180bd148722e8980ef5acbd4ae4c29a0d9d13da56bbccb91165a5eed4ab6f50\"}","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Purified human NFS1/ISD11 and MOCS3 rhodanese-domain interaction and sulfur-transfer assays","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"L-cysteine sulfur-donor assays","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Truncated and heterologously expressed proteins; cell localization was investigated independently in 2013.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"Molybdenum research collection; topical membership is not evidence of a direct dietary effect.","comparator":null,"unit":null,"notes":"","entity":{"slug":"molybdenum","display_name":"Molybdenum","entity_type_key":"nutrient_element"}},{"dimension":"organism","value_text":"Human proteins expressed in Escherichia coli","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"Cysteine supplies sulfur that becomes part of the molybdenum cofactor.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[mo-p18650437] A novel role for human Nfs1 in the cytoplasm: Nfs1 acts as a sulfur donor for MOCS3, a protein involved in molybdenum cofactor biosynthesis. (2008). https://pubmed.ncbi.nlm.nih.gov/18650437/ DOI: 10.1074/jbc.m804064200","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Purified proteins","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"d63d21e5-287b-5780-bbc3-44d5dcab9680","evidence_kind":"source_excerpt","locator":"Lines 352-363","start_line":352,"end_line":363,"excerpt":"### mo-nfs1-sulfur\nHuman NFS1 transferred sulfur from L-cysteine through an NFS1-bound persulfide intermediate to the rhodanese-like domain of MOCS3.\nCondition category: normal\nnutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: Cysteine supplies sulfur that becomes part of the molybdenum cofactor.\norganism: Human proteins expressed in Escherichia coli\ntissue_or_cell_type: Purified proteins\nexperimental_model: Purified human NFS1/ISD11 and MOCS3 rhodanese-domain interaction and sulfur-transfer assays\nlimitations: Truncated and heterologously expressed proteins; cell localization was investigated independently in 2013.\nexposure: L-cysteine sulfur-donor assays\nevidence_span: {\"source_cache\": \"artifacts/molybdenum-research/18650437.abstract.txt\", \"locator\": \"Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"8180bd148722e8980ef5acbd4ae4c29a0d9d13da56bbccb91165a5eed4ab6f50\", \"start_char\": 0, \"end_char\": 1547, \"text_sha256\": \"8180bd148722e8980ef5acbd4ae4c29a0d9d13da56bbccb91165a5eed4ab6f50\"}\n[mo-p18650437] A novel role for human Nfs1 in the cytoplasm: Nfs1 acts as a sulfur donor for MOCS3, a protein involved in molybdenum cofactor biosynthesis. (2008). https://pubmed.ncbi.nlm.nih.gov/18650437/ DOI: 10.1074/jbc.m804064200","model_system":"Purified human NFS1/ISD11 and MOCS3 rhodanese-domain interaction and sulfur-transfer assays","directness":"author_interpretation","verification_status":"source_derived_draft","notes":"Exact curation-document quotation, not publisher quotation. Study references: [mo-p18650437] A novel role for human Nfs1 in the cytoplasm: Nfs1 acts as a sulfur donor for MOCS3, a protein involved in molybdenum cofactor biosynthesis. (2008). https://pubmed.ncbi.nlm.nih.gov/18650437/ DOI: 10.1074/jbc.m804064200","relationship":"supports","weight":1.0,"link_notes":"","source":{"id":"1aa6da60-8284-5252-8dd9-ac2250d5ced5","stable_key":"import-dc8975b1-95ff-5d9b-be17-a1c04610cca7","title":"Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (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":"143147eb9ac7fe750bdd33bb50d7773bc0cd49cc94faf219aebce3c3d760dd8f","revision_id":"90c2239d-290b-5e16-815a-f94d30569ebd","review_status":"unverified_draft","notes":""}}],"relations":[],"conflicts":[],"corrections":[],"research":null}