{"id":"cb9ba7a6-cf32-5a3a-8877-d2bd3da47db3","stable_key":"649e861b-265a-5912-bc36-3a73e53ef892:l-serine-sds-catabolism","predicate":"deaminates_serine_to","statement":"Human liver serine dehydratase uses PLP to convert L-serine to pyruvate and ammonia; its active holoenzyme was structurally characterized.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"bcef11dd-697c-5db5-aa98-97bc440f3f89","mechanism_event_label":"Serine carbon can enter central metabolism through a B6-dependent breakdown step.","subject":{"id":"fc4df87c-aec1-5de5-8122-effc2c5ee721","slug":"sds","display_name":"Human hepatic serine dehydratase / SDS","entity_type_key":"protein"},"object":{"id":"91e6d4f5-fba1-542d-b68a-57cc28e1e425","slug":"pyruvate","display_name":"Pyruvate","entity_type_key":"small_molecule"},"evidence_count":1,"mechanism_event":{"id":"bcef11dd-697c-5db5-aa98-97bc440f3f89","stable_key":"649e861b-265a-5912-bc36-3a73e53ef892:l-serine-sds-catabolism-event","event_type":"observed_relationship","label":"Serine carbon can enter central metabolism through a B6-dependent breakdown step.","description":"Human liver serine dehydratase uses PLP to convert L-serine to pyruvate and ammonia; its active holoenzyme was structurally characterized.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"fc4df87c-aec1-5de5-8122-effc2c5ee721","slug":"sds","display_name":"Human hepatic serine dehydratase / SDS","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"91e6d4f5-fba1-542d-b68a-57cc28e1e425","slug":"pyruvate","display_name":"Pyruvate","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":"6b656ff5-9532-5da4-8eea-8ca163a48649","slug":"pyridoxal-phosphate","display_name":"PLP","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""}]},"contexts":[{"dimension":"evidence_access","value_text":"Primary abstract","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Purified human hepatic enzyme, activity assay and 2.5-angstrom crystal structure.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Enzyme capacity does not quantify its share of whole-body serine disposal.","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":"Serine carbon can enter central metabolism through a B6-dependent breakdown step.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"Crystal structure of the pyridoxal-5'-phosphate-dependent serine dehydratase from human liver. · 2005 · https://pubmed.ncbi.nlm.nih.gov/15689518/ · DOI 10.1110/ps.041179105","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"60b54ffb-14d4-5f75-a6fa-562050558dd0","evidence_kind":"source_excerpt","locator":"Lines 366-372","start_line":366,"end_line":372,"excerpt":"## l-serine-sds-catabolism\nSerine carbon can enter central metabolism through a B6-dependent breakdown step.\nHuman liver serine dehydratase uses PLP to convert L-serine to pyruvate and ammonia; its active holoenzyme was structurally characterized.\nModel: Purified human hepatic enzyme, activity assay and 2.5-angstrom crystal structure.\nLimitations: Enzyme capacity does not quantify its share of whole-body serine disposal.\nEvidence access: Primary abstract\nCrystal structure of the pyridoxal-5'-phosphate-dependent serine dehydratase from human liver. · 2005 · https://pubmed.ncbi.nlm.nih.gov/15689518/ · DOI 10.1110/ps.041179105","model_system":"Purified human hepatic enzyme, activity assay and 2.5-angstrom crystal structure.","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. Not publisher full text.","file_path":"","sha256":"22a750ce2b94f8607268c58322c48c4f0468f403b72a4008307538a6e5ff86d5","revision_id":"c1d6a7e1-9558-5bc6-9e3b-7080c26d3dbc","review_status":"unverified_draft","notes":""}}],"relations":[],"conflicts":[],"corrections":[],"research":null}