{"id":"d6ae849e-ed2b-57e7-93e0-85933a4ede99","stable_key":"649e861b-265a-5912-bc36-3a73e53ef892:l-serine-phgdh-assembly","predicate":"requires_assembly_for","statement":"Alanine substitutions at the predicted human PHGDH tetramer interface disrupted assembly, stability and activity for several tested ACT-domain residues.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"3266f2cd-7e75-5bef-a4d4-4e279fbd457f","mechanism_event_label":"The enzyme must fold and assemble correctly as well as receive its cofactor.","subject":{"id":"bde7376b-95ef-5b84-8789-353ec30d5b9b","slug":"phgdh","display_name":"Human phosphoglycerate dehydrogenase / PHGDH","entity_type_key":"protein"},"object":{"id":"8d6c4cd4-48b1-5384-a39d-ea75815c1ef5","slug":"human-phgdh-folding-activity","display_name":"Human PHGDH folding and catalytic activity","entity_type_key":"cellular_process"},"evidence_count":1,"mechanism_event":{"id":"3266f2cd-7e75-5bef-a4d4-4e279fbd457f","stable_key":"649e861b-265a-5912-bc36-3a73e53ef892:l-serine-phgdh-assembly-event","event_type":"observed_relationship","label":"The enzyme must fold and assemble correctly as well as receive its cofactor.","description":"Alanine substitutions at the predicted human PHGDH tetramer interface disrupted assembly, stability and activity for several tested ACT-domain residues.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"bde7376b-95ef-5b84-8789-353ec30d5b9b","slug":"phgdh","display_name":"Human phosphoglycerate dehydrogenase / PHGDH","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"8d6c4cd4-48b1-5384-a39d-ea75815c1ef5","slug":"human-phgdh-folding-activity","display_name":"Human PHGDH folding and catalytic activity","entity_type_key":"cellular_process"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"c882cd0b-9d83-5b07-bd1c-fe4d45657dcb","slug":"l-serine","display_name":"L-Serine","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""}]},"contexts":[{"dimension":"availability_state","value_text":"machinery_impairment","comparator":null,"unit":null,"notes":"Imported condition classification; unverified.","entity":null},{"dimension":"evidence_access","value_text":"Primary abstract","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Human recombinant variants; solution biochemistry with AlphaFold and molecular-dynamics model refinement.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"The complete tetramer model is computationally derived; it is not an experimentally solved full-length crystal structure.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"L-Serine collection; species, compartment, exposure, co-substrates and manipulation remain explicit.","comparator":null,"unit":null,"notes":"","entity":{"slug":"l-serine","display_name":"L-Serine","entity_type_key":"small_molecule"}},{"dimension":"plain_language","value_text":"The enzyme must fold and assemble correctly as well as receive its cofactor.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"On the quaternary structure of human D-3-phosphoglycerate dehydrogenase. · 2024 · https://pubmed.ncbi.nlm.nih.gov/39012001/ · DOI 10.1002/pro.5089","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"trigger_kind","value_text":"machinery_impairment","comparator":null,"unit":null,"notes":"Imported condition classification; unverified.","entity":null}],"evidence":[{"id":"36be2406-3712-54f3-b1c1-7185c5791db9","evidence_kind":"source_excerpt","locator":"Lines 22-28","start_line":22,"end_line":28,"excerpt":"## l-serine-phgdh-assembly\nThe enzyme must fold and assemble correctly as well as receive its cofactor.\nAlanine substitutions at the predicted human PHGDH tetramer interface disrupted assembly, stability and activity for several tested ACT-domain residues.\nModel: Human recombinant variants; solution biochemistry with AlphaFold and molecular-dynamics model refinement.\nLimitations: The complete tetramer model is computationally derived; it is not an experimentally solved full-length crystal structure.\nEvidence access: Primary abstract\nOn the quaternary structure of human D-3-phosphoglycerate dehydrogenase. · 2024 · https://pubmed.ncbi.nlm.nih.gov/39012001/ · DOI 10.1002/pro.5089","model_system":"Human recombinant variants; solution biochemistry with AlphaFold and molecular-dynamics model refinement.","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":"70bcf57a-36bb-563f-9073-2d616e5f155a","stable_key":"import-649e861b-265a-5912-bc36-3a73e53ef892","title":"L-Serine: synthesis, one-carbon metabolism, lipids and cross-nutrient mechanisms (2026-09-19)","document_type":"imported_text","citation_label":"AI-assisted research curation; primary references, access levels and experimental limitations individually identified. 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