{"id":"b408c423-497a-545c-b37e-81e12e4da310","stable_key":"a9dd23c6-978a-5755-8bd8-f29bd1fe0cda:b3-cons-sirt2-reaction","predicate":"deacetylates","statement":"Human SIRT2 deacetylated monoacetylated histone peptides in the NAD-consuming reaction producing nicotinamide and O-acetyl-ADP-ribose.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"positive","is_public":true,"mechanism_event_id":"75586117-e3a7-5cd0-9f9e-bc7309e7f70c","mechanism_event_label":"SIRT2 consumes NAD while removing acetyl groups from histone peptides.","subject":{"id":"7b80e703-0dd4-5086-a477-75e1ee24a85e","slug":"sirt2","display_name":"Human SIRT2","entity_type_key":"protein"},"object":{"id":"5c61138c-a222-59a0-8cbb-68996fbfda2f","slug":"histone-acetylated-peptides","display_name":"Monoacetylated histone H3/H4 assay peptides","entity_type_key":"protein_state"},"evidence_count":1,"mechanism_event":{"id":"75586117-e3a7-5cd0-9f9e-bc7309e7f70c","stable_key":"a9dd23c6-978a-5755-8bd8-f29bd1fe0cda:b3-cons-sirt2-reaction-event","event_type":"biochemical_relationship","label":"SIRT2 consumes NAD while removing acetyl groups from histone peptides.","description":"Human SIRT2 deacetylated monoacetylated histone peptides in the NAD-consuming reaction producing nicotinamide and O-acetyl-ADP-ribose.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"7b80e703-0dd4-5086-a477-75e1ee24a85e","slug":"sirt2","display_name":"Human SIRT2","entity_type_key":"protein"},"role":"enzyme","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"283ed24b-06a1-50aa-9281-df3bac6ce37e","slug":"nad-plus","display_name":"NAD+","entity_type_key":"small_molecule"},"role":"cosubstrate","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"5c61138c-a222-59a0-8cbb-68996fbfda2f","slug":"histone-acetylated-peptides","display_name":"Monoacetylated histone H3/H4 assay peptides","entity_type_key":"protein_state"},"role":"substrate","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""},{"entity":{"id":"95a9ecc1-717b-59b8-a50b-0a48d7705aa2","slug":"histone-deacetylated-peptides","display_name":"Deacetylated histone assay peptides","entity_type_key":"protein_state"},"role":"product","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""},{"entity":{"id":"08c27a3f-552e-5c92-8688-321a9b64a0d6","slug":"nicotinamide","display_name":"Nicotinamide","entity_type_key":"small_molecule"},"role":"coproduct","stoichiometry":null,"state_label":"","sequence_order":4,"notes":""},{"entity":{"id":"e51e5546-5ace-5717-a7c1-64f3adaed6d9","slug":"o-acetyl-adp-ribose","display_name":"O-Acetyl-ADP-ribose","entity_type_key":"small_molecule"},"role":"coproduct","stoichiometry":null,"state_label":"","sequence_order":5,"notes":""}]},"contexts":[{"dimension":"cross_nutrient","value_text":"false","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"evidence_span","value_text":"{\"source_cache\": \"artifacts/niacin-consumption-sources/sirt22004.abstract.txt\", \"locator\": \"Indexed abstract\", \"start_char\": 0, \"end_char\": 1423, \"file_sha256\": \"a84f7d25c6e518d3317d4b0a41df8d8ac447cd3ef2966815c9818ca63116ef7f\", \"text_sha256\": \"a84f7d25c6e518d3317d4b0a41df8d8ac447cd3ef2966815c9818ca63116ef7f\"}","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Recombinant enzyme and monoacetylated histone H3/H4 peptide assays","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"Human SIRT2; yeast Sir2/Hst2 were also studied separately","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Indexed abstract; rapid-kinetic details are not assigned to human SIRT2 individually. No dietary or longevity inference.","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":"Human","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"SIRT2 consumes NAD while removing acetyl groups from histone peptides.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[b3-cons-sirt22004] Substrate specificity and kinetic mechanism of the Sir2 family of NAD+-dependent histone/protein deacetylases. (2004). https://pubmed.ncbi.nlm.nih.gov/15274642/ DOI: 10.1021/bi049592e","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Cell-free assay","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"afbdd775-de86-5fe2-954b-77a70b99b01f","evidence_kind":"source_excerpt","locator":"Lines 551-563","start_line":551,"end_line":563,"excerpt":"### b3-cons-sirt2-reaction\nHuman SIRT2 deacetylated monoacetylated histone peptides in the NAD-consuming reaction producing nicotinamide and O-acetyl-ADP-ribose.\nCondition category: normal\nnutrient_topic: Niacin research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: SIRT2 consumes NAD while removing acetyl groups from histone peptides.\norganism: Human\ntissue_or_cell_type: Cell-free assay\nexperimental_model: Recombinant enzyme and monoacetylated histone H3/H4 peptide assays\nlimitations: Indexed abstract; rapid-kinetic details are not assigned to human SIRT2 individually. No dietary or longevity inference.\nexposure: Human SIRT2; yeast Sir2/Hst2 were also studied separately\ncross_nutrient: false\nevidence_span: {\"source_cache\": \"artifacts/niacin-consumption-sources/sirt22004.abstract.txt\", \"locator\": \"Indexed abstract\", \"start_char\": 0, \"end_char\": 1423, \"file_sha256\": \"a84f7d25c6e518d3317d4b0a41df8d8ac447cd3ef2966815c9818ca63116ef7f\", \"text_sha256\": \"a84f7d25c6e518d3317d4b0a41df8d8ac447cd3ef2966815c9818ca63116ef7f\"}\n[b3-cons-sirt22004] Substrate specificity and kinetic mechanism of the Sir2 family of NAD+-dependent histone/protein deacetylases. (2004). https://pubmed.ncbi.nlm.nih.gov/15274642/ DOI: 10.1021/bi049592e","model_system":"Recombinant enzyme and monoacetylated histone H3/H4 peptide assays","directness":"author_interpretation","verification_status":"source_derived_draft","notes":"Exact curation-document quotation, not publisher quotation. Study references: [b3-cons-sirt22004] Substrate specificity and kinetic mechanism of the Sir2 family of NAD+-dependent histone/protein deacetylases. (2004). https://pubmed.ncbi.nlm.nih.gov/15274642/ DOI: 10.1021/bi049592e","relationship":"supports","weight":1.0,"link_notes":"","source":{"id":"a62b7b5b-786a-57e9-85e9-67c6912a5054","stable_key":"import-a9dd23c6-978a-5755-8bd8-f29bd1fe0cda","title":"Niacin: NAD metabolism, deficiency 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":"a8cac59639322f74812ce12eef338c2f6c385c04cc4af6ab511fc7c972f0c2e6","revision_id":"bec8fc45-12e7-5f75-a814-5d72ed015d01","review_status":"unverified_draft","notes":""}}],"relations":[],"conflicts":[],"corrections":[],"research":null}