{"id":"3680ccf3-79e7-51a4-9dd7-c0394d034f68","stable_key":"4910e17b-aaec-52cd-b9e5-caca85d817ee:red-yeast-rice-human-mevalonate-machinery","predicate":"catalyzes_formation_of","statement":"Human HMG-CoA reductase catalyzes mevalonate formation; substrate/cofactor-bound structures locate HMG-CoA and the nicotinamide cofactor in the catalytic domain.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"b91272e1-2320-5f1e-8739-c087bb1ba062","mechanism_event_label":"This enzyme supplies a shared precursor pathway.","subject":{"id":"a8b5e5e1-b5b5-551d-8fd4-72f7b45de78a","slug":"hmgcr","display_name":"HMG-CoA reductase (HMGCR)","entity_type_key":"protein"},"object":{"id":"3df322fd-ac21-5bd1-aa46-4af1ec708b57","slug":"mevalonate","display_name":"Mevalonate","entity_type_key":"small_molecule"},"evidence_count":1,"mechanism_event":{"id":"b91272e1-2320-5f1e-8739-c087bb1ba062","stable_key":"4910e17b-aaec-52cd-b9e5-caca85d817ee:red-yeast-rice-human-mevalonate-machinery-event","event_type":"observed_relationship","label":"This enzyme supplies a shared precursor pathway.","description":"Human HMG-CoA reductase catalyzes mevalonate formation; substrate/cofactor-bound structures locate HMG-CoA and the nicotinamide cofactor in the catalytic domain.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"a8b5e5e1-b5b5-551d-8fd4-72f7b45de78a","slug":"hmgcr","display_name":"HMG-CoA reductase (HMGCR)","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"3df322fd-ac21-5bd1-aa46-4af1ec708b57","slug":"mevalonate","display_name":"Mevalonate","entity_type_key":"small_molecule"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"81e5bb47-0c11-54c9-a0ec-5c213930c173","slug":"hmg-coa","display_name":"(S)-3-Hydroxy-3-methylglutaryl-CoA","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""},{"entity":{"id":"4aba2a5e-8d06-5304-bb01-c0402b225a94","slug":"nadph","display_name":"NADPH","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""},{"entity":{"id":"d3a1b93d-0a2c-5d1b-b672-5e4ef4b09a10","slug":"cholesterol","display_name":"Cholesterol","entity_type_key":"lipid"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":4,"notes":""}]},"contexts":[{"dimension":"evidence_access","value_text":"Primary abstract","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Human recombinant catalytic-domain crystallography and biochemical background.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Shared human machinery; the source is not an experiment administering red yeast rice.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"Red yeast rice collection; species, compartment, exposure, co-substrates and manipulation remain explicit.","comparator":null,"unit":null,"notes":"","entity":{"slug":"red-yeast-rice","display_name":"Red yeast rice","entity_type_key":"chemical_species"}},{"dimension":"plain_language","value_text":"This enzyme supplies a shared precursor pathway.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[10698924] Crystal structure of the catalytic portion of human HMG-CoA reductase: insights into regulation of activity and catalysis. · 2000 · https://pubmed.ncbi.nlm.nih.gov/10698924/ · DOI 10.1093/emboj/19.5.819","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"2eb5d7e8-d8c7-563f-ba2f-2b113f9aaa41","evidence_kind":"source_excerpt","locator":"Lines 76-82","start_line":76,"end_line":82,"excerpt":"## red-yeast-rice-human-mevalonate-machinery\nThis enzyme supplies a shared precursor pathway.\nHuman HMG-CoA reductase catalyzes mevalonate formation; substrate/cofactor-bound structures locate HMG-CoA and the nicotinamide cofactor in the catalytic domain.\nModel: Human recombinant catalytic-domain crystallography and biochemical background.\nLimitations: Shared human machinery; the source is not an experiment administering red yeast rice.\nEvidence access: Primary abstract\n[10698924] Crystal structure of the catalytic portion of human HMG-CoA reductase: insights into regulation of activity and catalysis. · 2000 · https://pubmed.ncbi.nlm.nih.gov/10698924/ · DOI 10.1093/emboj/19.5.819","model_system":"Human recombinant catalytic-domain crystallography and biochemical background.","directness":"reported_statement","verification_status":"source_derived_draft","notes":"Original curation paraphrase; evidence access and experimental limitations specified.","relationship":"supports","weight":1.0,"link_notes":"","source":{"id":"261a12bc-3d00-52a4-a5ec-70e174390596","stable_key":"import-4910e17b-aaec-52cd-b9e5-caca85d817ee","title":"Red yeast rice: constituents, mevalonate, CoQ and product-specific interactions (2026-09-20)","document_type":"imported_text","citation_label":"AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text.","file_path":"","sha256":"271bbcecaaacc76ad4d06718ae592dc6a1b33e3e459adfdd36cbd0ac5f09c0f6","revision_id":"9c30956c-206c-5c49-ae42-81b070088e26","review_status":"unverified_draft","notes":""}}],"relations":[],"conflicts":[],"corrections":[],"research":null}