{"id":"f84c754d-9bea-5535-870c-d78b5e6cb791","stable_key":"a9dd23c6-978a-5755-8bd8-f29bd1fe0cda:b3-pre-nmnat2-namn","predicate":"catalyzes-production-of","statement":"Purified recombinant human NMNAT2 has adenylyltransferase activity toward nicotinic acid mononucleotide, supporting NaAD formation.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"positive","is_public":true,"mechanism_event_id":"11701645-f88d-50f9-a5b8-43c1483d5f6f","mechanism_event_label":"The same human isozyme processes either the amidated or deamidated mononucleotide.","subject":{"id":"11ea02c9-58ec-54d8-948f-f89eff2c2bd9","slug":"nmnat2","display_name":"Human nicotinamide mononucleotide adenylyltransferase 2 / NMNAT2","entity_type_key":"protein"},"object":{"id":"4be03515-1913-50d7-a676-dbbb49a0809d","slug":"nicotinic-acid-adenine-dinucleotide","display_name":"Nicotinic acid adenine dinucleotide","entity_type_key":"small_molecule"},"evidence_count":1,"mechanism_event":{"id":"11701645-f88d-50f9-a5b8-43c1483d5f6f","stable_key":"a9dd23c6-978a-5755-8bd8-f29bd1fe0cda:b3-pre-nmnat2-namn-event","event_type":"biochemical_relationship","label":"The same human isozyme processes either the amidated or deamidated mononucleotide.","description":"Purified recombinant human NMNAT2 has adenylyltransferase activity toward nicotinic acid mononucleotide, supporting NaAD formation.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"11ea02c9-58ec-54d8-948f-f89eff2c2bd9","slug":"nmnat2","display_name":"Human nicotinamide mononucleotide adenylyltransferase 2 / NMNAT2","entity_type_key":"protein"},"role":"enzyme","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"a17c536e-82bd-5613-8114-79bb35ec8039","slug":"nicotinic-acid-mononucleotide","display_name":"Nicotinic acid mononucleotide","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":"adenylyl donor","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""},{"entity":{"id":"4be03515-1913-50d7-a676-dbbb49a0809d","slug":"nicotinic-acid-adenine-dinucleotide","display_name":"Nicotinic acid adenine dinucleotide","entity_type_key":"small_molecule"},"role":"product","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""}]},"contexts":[{"dimension":"evidence_span","value_text":"{\"source_cache\": \"artifacts/niacin-precursors-sources/nmnat2002.abstract.txt\", \"locator\": \"Indexed primary abstract\", \"start_char\": 0, \"end_char\": 826, \"file_sha256\": \"5064cc6a7b31875eeaea8def5544c3cce75a971f73aa74f332d89e06c3c54477\", \"text_sha256\": \"5064cc6a7b31875eeaea8def5544c3cce75a971f73aa74f332d89e06c3c54477\"}","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Cloned, expressed and purified recombinant human NMNAT2","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"Biochemical or structural assay; no dietary intervention","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Purified-enzyme evidence does not establish dietary intake requirements or clinical outcomes.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"Niacin research collection; topical membership is not evidence of a direct dietary effect.","comparator":null,"unit":null,"notes":"","entity":{"slug":"niacin","display_name":"Niacin (vitamin B3)","entity_type_key":"nutrient_element"}},{"dimension":"organism","value_text":"Homo sapiens","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"The same human isozyme processes either the amidated or deamidated mononucleotide.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[b3-pre-nmnat2002] Identification of a novel human nicotinamide mononucleotide adenylyltransferase. (2002). https://pubmed.ncbi.nlm.nih.gov/12359228/ DOI: 10.1016/s0006-291x(02)02285-4","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Purified recombinant protein; no intact tissue","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"9dfef585-ac39-5797-8328-b216b2baeb92","evidence_kind":"source_excerpt","locator":"Lines 315-326","start_line":315,"end_line":326,"excerpt":"### b3-pre-nmnat2-namn\nPurified recombinant human NMNAT2 has adenylyltransferase activity toward nicotinic acid mononucleotide, supporting NaAD formation.\nCondition category: normal\nnutrient_topic: Niacin research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: The same human isozyme processes either the amidated or deamidated mononucleotide.\norganism: Homo sapiens\ntissue_or_cell_type: Purified recombinant protein; no intact tissue\nexperimental_model: Cloned, expressed and purified recombinant human NMNAT2\nlimitations: Purified-enzyme evidence does not establish dietary intake requirements or clinical outcomes.\nexposure: Biochemical or structural assay; no dietary intervention\nevidence_span: {\"source_cache\": \"artifacts/niacin-precursors-sources/nmnat2002.abstract.txt\", \"locator\": \"Indexed primary abstract\", \"start_char\": 0, \"end_char\": 826, \"file_sha256\": \"5064cc6a7b31875eeaea8def5544c3cce75a971f73aa74f332d89e06c3c54477\", \"text_sha256\": \"5064cc6a7b31875eeaea8def5544c3cce75a971f73aa74f332d89e06c3c54477\"}\n[b3-pre-nmnat2002] Identification of a novel human nicotinamide mononucleotide adenylyltransferase. 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