{"id":"8a37d483-9a0f-595c-9b9f-5ea5e4f8a94f","stable_key":"97957230-601f-5dec-8524-0812be8fadbf:l-threonine-human-sdsl-catabolism","predicate":"dehydrates_threonine_toward","statement":"The recombinant human SDH-like protein also had threonine dehydratase activity, with kinetic constants differing substantially from hepatic SDS.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"7366afd1-b0ac-5b82-8e21-1b7c95e2b5f2","mechanism_event_label":"Closely related enzymes can process the same substrate at different rates.","subject":{"id":"694036f6-b7f5-5bc0-8967-a4de835ba23c","slug":"sdsl","display_name":"Human serine dehydratase-like protein / SDSL","entity_type_key":"protein"},"object":{"id":"dee03e61-050d-5bde-ad0a-7f9652799ec8","slug":"alpha-ketobutyrate","display_name":"Alpha-ketobutyrate","entity_type_key":"small_molecule"},"evidence_count":1,"mechanism_event":{"id":"7366afd1-b0ac-5b82-8e21-1b7c95e2b5f2","stable_key":"97957230-601f-5dec-8524-0812be8fadbf:l-threonine-human-sdsl-catabolism-event","event_type":"observed_relationship","label":"Closely related enzymes can process the same substrate at different rates.","description":"The recombinant human SDH-like protein also had threonine dehydratase activity, with kinetic constants differing substantially from hepatic SDS.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"694036f6-b7f5-5bc0-8967-a4de835ba23c","slug":"sdsl","display_name":"Human serine dehydratase-like protein / SDSL","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"dee03e61-050d-5bde-ad0a-7f9652799ec8","slug":"alpha-ketobutyrate","display_name":"Alpha-ketobutyrate","entity_type_key":"small_molecule"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"fcef4dc2-a7b6-5812-bc33-c8af3d83f4d0","slug":"l-threonine","display_name":"L-Threonine","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":""},{"entity":{"id":"fc4df87c-aec1-5de5-8122-effc2c5ee721","slug":"sds","display_name":"Human hepatic serine dehydratase / SDS","entity_type_key":"protein"},"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":"Comparative human enzyme kinetics and PLP-binding measurements.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Isoform abundance in cultured cells was low; catalytic capacity does not establish its dominant tissue role.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"L-Threonine collection; species, compartment, exposure, co-substrates and manipulation remain explicit.","comparator":null,"unit":null,"notes":"","entity":{"slug":"l-threonine","display_name":"L-Threonine","entity_type_key":"small_molecule"}},{"dimension":"plain_language","value_text":"Closely related enzymes can process the same substrate at different rates.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"Enzymatic and biochemical properties of a novel human serine dehydratase isoform. · 2006 · https://pubmed.ncbi.nlm.nih.gov/16580895/ · DOI 10.1016/j.bbapap.2006.02.010","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"ee8c9fc4-70de-5f90-948f-849ff3e3aae2","evidence_kind":"source_excerpt","locator":"Lines 258-264","start_line":258,"end_line":264,"excerpt":"## l-threonine-human-sdsl-catabolism\nClosely related enzymes can process the same substrate at different rates.\nThe recombinant human SDH-like protein also had threonine dehydratase activity, with kinetic constants differing substantially from hepatic SDS.\nModel: Comparative human enzyme kinetics and PLP-binding measurements.\nLimitations: Isoform abundance in cultured cells was low; catalytic capacity does not establish its dominant tissue role.\nEvidence access: Primary abstract\nEnzymatic and biochemical properties of a novel human serine dehydratase isoform. · 2006 · https://pubmed.ncbi.nlm.nih.gov/16580895/ · DOI 10.1016/j.bbapap.2006.02.010","model_system":"Comparative human enzyme kinetics and PLP-binding measurements.","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":"35396730-235a-537e-8a05-c6ef2960c509","stable_key":"import-97957230-601f-5dec-8524-0812be8fadbf","title":"L-Threonine: translation, intestinal barrier, metabolism 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":"3365aed939d9f567bd098449c7d67c7c00fb6c9ba163dcf34dc7cf6081f324fb","revision_id":"10a7b648-8dd7-5d4e-b618-c560a6e2d3c7","review_status":"unverified_draft","notes":""}}],"relations":[],"conflicts":[],"corrections":[],"research":null}