{"id":"d7d55a4e-4e53-5c01-9fb6-36930e0fd6a2","stable_key":"00c24cfe-6189-5244-b81f-5d693e4e177d:chlorogenic_acid-human-comt-sam","predicate":"binds","statement":"Human soluble COMT structures resolve bound SAM.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"8ffceebe-3c47-5617-8fd2-0983a50b872d","mechanism_event_label":"The shared methyl donor links COMT to methionine-cycle metabolism.","subject":{"id":"936e1fd4-e862-5e32-b7dc-35b946294e43","slug":"comt","display_name":"Human catechol O-methyltransferase / COMT","entity_type_key":"protein"},"object":{"id":"825f2da2-01bc-5874-a3c6-64f5ac867db5","slug":"s-adenosylmethionine","display_name":"S-Adenosyl-L-methionine","entity_type_key":"small_molecule"},"evidence_count":1,"mechanism_event":{"id":"8ffceebe-3c47-5617-8fd2-0983a50b872d","stable_key":"00c24cfe-6189-5244-b81f-5d693e4e177d:chlorogenic_acid-human-comt-sam-event","event_type":"biochemical_relationship","label":"The shared methyl donor links COMT to methionine-cycle metabolism.","description":"Human soluble COMT structures resolve bound SAM.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"936e1fd4-e862-5e32-b7dc-35b946294e43","slug":"comt","display_name":"Human catechol O-methyltransferase / COMT","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"825f2da2-01bc-5874-a3c6-64f5ac867db5","slug":"s-adenosylmethionine","display_name":"S-Adenosyl-L-methionine","entity_type_key":"small_molecule"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""}]},"contexts":[{"dimension":"evidence_span","value_text":"{\"source_cache\": \"artifacts/chlorogenic_acid-research/18486144.abstract.txt\", \"locator\": \"Primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"9cafbfc9353f49fab9919bc64608f21f445ace4b190771e44088a5a746e5a6e3\", \"start_char\": 0, \"end_char\": 1961, \"text_sha256\": \"9cafbfc9353f49fab9919bc64608f21f445ace4b190771e44088a5a746e5a6e3\"}","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Human soluble COMT crystallography and deposited structure 3BWM","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"SAM and 3,5-dinitrocatechol-bound crystals; deposited Mg ion","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Structural cofactor connection, not a CGA-magnesium supplementation trial. Human and rat COMT specificity differs; deposition includes an inhibitor analog rather than CGA.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"Chlorogenic acid research collection; topical membership is not evidence of a direct dietary effect.","comparator":null,"unit":null,"notes":"","entity":{"slug":"chlorogenic-acid","display_name":"Chlorogenic acid / 5-O-caffeoylquinic acid","entity_type_key":"small_molecule"}},{"dimension":"organism","value_text":"Homo sapiens","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"The shared methyl donor links COMT to methionine-cycle metabolism.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[chlorogenic_acid-p18486144] Crystal structures of human 108V and 108M catechol O-methyltransferase. (2008). https://pubmed.ncbi.nlm.nih.gov/18486144/ DOI: 10.1016/j.jmb.2008.04.040","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Purified soluble COMT","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"b20618d2-1d9a-5900-85be-f6380e49f6e0","evidence_kind":"source_excerpt","locator":"Lines 841-852","start_line":841,"end_line":852,"excerpt":"### chlorogenic_acid-human-comt-sam\nHuman soluble COMT structures resolve bound SAM.\nCondition category: normal\nnutrient_topic: Chlorogenic acid research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: The shared methyl donor links COMT to methionine-cycle metabolism.\norganism: Homo sapiens\ntissue_or_cell_type: Purified soluble COMT\nexperimental_model: Human soluble COMT crystallography and deposited structure 3BWM\nlimitations: Structural cofactor connection, not a CGA-magnesium supplementation trial. Human and rat COMT specificity differs; deposition includes an inhibitor analog rather than CGA.\nexposure: SAM and 3,5-dinitrocatechol-bound crystals; deposited Mg ion\nevidence_span: {\"source_cache\": \"artifacts/chlorogenic_acid-research/18486144.abstract.txt\", \"locator\": \"Primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"9cafbfc9353f49fab9919bc64608f21f445ace4b190771e44088a5a746e5a6e3\", \"start_char\": 0, \"end_char\": 1961, \"text_sha256\": \"9cafbfc9353f49fab9919bc64608f21f445ace4b190771e44088a5a746e5a6e3\"}\n[chlorogenic_acid-p18486144] Crystal structures of human 108V and 108M catechol O-methyltransferase. (2008). https://pubmed.ncbi.nlm.nih.gov/18486144/ DOI: 10.1016/j.jmb.2008.04.040","model_system":"Human soluble COMT crystallography and deposited structure 3BWM","directness":"author_interpretation","verification_status":"source_derived_draft","notes":"Exact curation-document quotation, not publisher quotation. Study references: [chlorogenic_acid-p18486144] Crystal structures of human 108V and 108M catechol O-methyltransferase. (2008). https://pubmed.ncbi.nlm.nih.gov/18486144/ DOI: 10.1016/j.jmb.2008.04.040","relationship":"supports","weight":1.0,"link_notes":"","source":{"id":"98a7cb8d-1d80-5cfe-9690-4068d21878e3","stable_key":"import-00c24cfe-6189-5244-b81f-5d693e4e177d","title":"Chlorogenic acid: metabolism, signaling 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":"dabd56b55fb10d82913b222343d9592d3baf61ef3cc81cf47f3e3e7537eb7992","revision_id":"340aee2f-52a6-56aa-99c1-0a24c534752a","review_status":"unverified_draft","notes":""}}],"relations":[],"conflicts":[],"corrections":[],"research":null}