{"id":"f696af96-645b-58ee-b879-997ffe867ee1","stable_key":"dc8975b1-95ff-5d9b-be17-a1c04610cca7:mo-marc-no-terminal-sulfur","predicate":"reconstitutes_without_terminal_sulfuration","statement":"Active mARC1 and mARC2 were reconstituted with Moco without the terminal sulfuration needed by the XOR enzyme family.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"10c78133-9eb4-54d3-97c4-0979da0c9f42","mechanism_event_label":"mARC does not require the extra sulfur-activation step used by XDH and AOX1.","subject":{"id":"ac4bcc03-66fb-52c1-b191-9ecb2124659f","slug":"molybdenum-cofactor","display_name":"Molybdenum cofactor / Moco","entity_type_key":"small_molecule"},"object":{"id":"cd629c45-47a6-555e-9ad9-9abb93a04e7f","slug":"mtarc1","display_name":"Human mitochondrial amidoxime-reducing component 1 / MTARC1","entity_type_key":"protein"},"evidence_count":1,"mechanism_event":{"id":"10c78133-9eb4-54d3-97c4-0979da0c9f42","stable_key":"dc8975b1-95ff-5d9b-be17-a1c04610cca7:mo-marc-no-terminal-sulfur-event","event_type":"biochemical_relationship","label":"mARC does not require the extra sulfur-activation step used by XDH and AOX1.","description":"Active mARC1 and mARC2 were reconstituted with Moco without the terminal sulfuration needed by the XOR enzyme family.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"c3c9e014-7930-5cfc-b7ce-a142dcdb3dd0","slug":"mtarc2","display_name":"Human mitochondrial amidoxime-reducing component 2 / MTARC2","entity_type_key":"protein"},"role":"parallel enzyme","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"e8016ea8-2237-5618-85b2-199710521dc6","slug":"mocos","display_name":"Human molybdenum cofactor sulfurase / MOCOS","entity_type_key":"protein"},"role":"comparison pathway","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"ac4bcc03-66fb-52c1-b191-9ecb2124659f","slug":"molybdenum-cofactor","display_name":"Molybdenum cofactor / Moco","entity_type_key":"small_molecule"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""},{"entity":{"id":"cd629c45-47a6-555e-9ad9-9abb93a04e7f","slug":"mtarc1","display_name":"Human mitochondrial amidoxime-reducing component 1 / MTARC1","entity_type_key":"protein"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""}]},"contexts":[{"dimension":"evidence_span","value_text":"{\"source_cache\": \"artifacts/molybdenum-research/20861021.abstract.txt\", \"locator\": \"Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"0f430936dcc4701e5d57040edcab4b0418e3c49c59620e0f7d5f54aff41e7877\", \"start_char\": 0, \"end_char\": 1557, \"text_sha256\": \"0f430936dcc4701e5d57040edcab4b0418e3c49c59620e0f7d5f54aff41e7877\"}","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Recombinant human mARC1/mARC2 biochemical and spectroscopic reconstitution","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"N-hydroxylated substrates; cofactor reconstitution","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"The 2010 paper could not identify the Mo-ligating cysteine; later structural/mutagenesis work resolves that point. Its earlier inference is not imported as current fact.","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":"mARC does not require the extra sulfur-activation step used by XDH and AOX1.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[mo-p20861021] Biochemical and spectroscopic characterization of the human mitochondrial amidoxime reducing components hmARC-1 and hmARC-2 suggests the existence of a new molybdenum enzyme family in eukaryotes. (2010). https://pubmed.ncbi.nlm.nih.gov/20861021/ DOI: 10.1074/jbc.m110.169532","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Purified enzyme system","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"078203f9-6b40-525c-8a37-60bd38e9534c","evidence_kind":"source_excerpt","locator":"Lines 976-987","start_line":976,"end_line":987,"excerpt":"### mo-marc-no-terminal-sulfur\nActive mARC1 and mARC2 were reconstituted with Moco without the terminal sulfuration needed by the XOR enzyme family.\nCondition category: normal\nnutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: mARC does not require the extra sulfur-activation step used by XDH and AOX1.\norganism: Human proteins expressed in Escherichia coli\ntissue_or_cell_type: Purified enzyme system\nexperimental_model: Recombinant human mARC1/mARC2 biochemical and spectroscopic reconstitution\nlimitations: The 2010 paper could not identify the Mo-ligating cysteine; later structural/mutagenesis work resolves that point. Its earlier inference is not imported as current fact.\nexposure: N-hydroxylated substrates; cofactor reconstitution\nevidence_span: {\"source_cache\": \"artifacts/molybdenum-research/20861021.abstract.txt\", \"locator\": \"Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"0f430936dcc4701e5d57040edcab4b0418e3c49c59620e0f7d5f54aff41e7877\", \"start_char\": 0, \"end_char\": 1557, \"text_sha256\": \"0f430936dcc4701e5d57040edcab4b0418e3c49c59620e0f7d5f54aff41e7877\"}\n[mo-p20861021] Biochemical and spectroscopic characterization of the human mitochondrial amidoxime reducing components hmARC-1 and hmARC-2 suggests the existence of a new molybdenum enzyme family in eukaryotes. (2010). https://pubmed.ncbi.nlm.nih.gov/20861021/ DOI: 10.1074/jbc.m110.169532","model_system":"Recombinant human mARC1/mARC2 biochemical and spectroscopic reconstitution","directness":"author_interpretation","verification_status":"source_derived_draft","notes":"Exact curation-document quotation, not publisher quotation. Study references: [mo-p20861021] Biochemical and spectroscopic characterization of the human mitochondrial amidoxime reducing components hmARC-1 and hmARC-2 suggests the existence of a new molybdenum enzyme family in eukaryotes. 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