{"id":"c0635c40-597a-5099-b1a2-7e3462131d0b","stable_key":"649e861b-265a-5912-bc36-3a73e53ef892:l-serine-phgdh-reaction","predicate":"oxidizes_3_phosphoglycerate_to","statement":"Human PHGDH catalyzes the NAD+-dependent oxidation of 3-phosphoglycerate to phosphohydroxypyruvate, the first step of phosphorylated serine biosynthesis.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"6aa8f3e5-3f05-50bb-a2b9-1802f76b88a6","mechanism_event_label":"A glycolysis intermediate can be diverted into serine production.","subject":{"id":"bde7376b-95ef-5b84-8789-353ec30d5b9b","slug":"phgdh","display_name":"Human phosphoglycerate dehydrogenase / PHGDH","entity_type_key":"protein"},"object":{"id":"09de4621-09f2-50d3-b344-8ccdc6b3c467","slug":"3-phosphohydroxypyruvate","display_name":"3-Phosphohydroxypyruvate","entity_type_key":"small_molecule"},"evidence_count":1,"mechanism_event":{"id":"6aa8f3e5-3f05-50bb-a2b9-1802f76b88a6","stable_key":"649e861b-265a-5912-bc36-3a73e53ef892:l-serine-phgdh-reaction-event","event_type":"observed_relationship","label":"A glycolysis intermediate can be diverted into serine production.","description":"Human PHGDH catalyzes the NAD+-dependent oxidation of 3-phosphoglycerate to phosphohydroxypyruvate, the first step of phosphorylated serine biosynthesis.","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":"09de4621-09f2-50d3-b344-8ccdc6b3c467","slug":"3-phosphohydroxypyruvate","display_name":"3-Phosphohydroxypyruvate","entity_type_key":"small_molecule"},"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":""},{"entity":{"id":"7120d12b-1691-55fc-bec5-d42f857b44ca","slug":"3-phosphoglycerate","display_name":"3-Phosphoglycerate","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""},{"entity":{"id":"283ed24b-06a1-50aa-9281-df3bac6ce37e","slug":"nad-plus","display_name":"NAD+","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":4,"notes":""},{"entity":{"id":"9fbf2e03-16a9-5ca7-965c-0bfc07ca24da","slug":"nadh","display_name":"NADH","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":5,"notes":""}]},"contexts":[{"dimension":"evidence_access","value_text":"Primary abstract","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Recombinant human PHGDH catalytic-domain structure and enzyme assays.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"The truncated dimeric structure does not define the complete native oligomer.","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":"A glycolysis intermediate can be diverted into serine production.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"Structural insights into the enzymatic activity and potential substrate promiscuity of human 3-phosphoglycerate dehydrogenase (PHGDH). · 2017 · https://pubmed.ncbi.nlm.nih.gov/29262655/ · DOI 10.18632/oncotarget.22327","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"1815ddd5-85ab-5959-824c-fd1de9e73c5c","evidence_kind":"source_excerpt","locator":"Lines 14-20","start_line":14,"end_line":20,"excerpt":"## l-serine-phgdh-reaction\nA glycolysis intermediate can be diverted into serine production.\nHuman PHGDH catalyzes the NAD+-dependent oxidation of 3-phosphoglycerate to phosphohydroxypyruvate, the first step of phosphorylated serine biosynthesis.\nModel: Recombinant human PHGDH catalytic-domain structure and enzyme assays.\nLimitations: The truncated dimeric structure does not define the complete native oligomer.\nEvidence access: Primary abstract\nStructural insights into the enzymatic activity and potential substrate promiscuity of human 3-phosphoglycerate dehydrogenase (PHGDH). · 2017 · https://pubmed.ncbi.nlm.nih.gov/29262655/ · DOI 10.18632/oncotarget.22327","model_system":"Recombinant human PHGDH catalytic-domain structure and enzyme assays.","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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