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Similarity to OGDH does not make the proteins interchangeable.","subject":{"id":"b8552ee2-4a84-59a0-9694-69991c9903bf","slug":"dhtkd1","display_name":"DHTKD1","entity_type_key":"protein"},"object":{"id":"187db168-8028-5ce6-9f8b-4bc61ebad1a0","slug":"thiamine-diphosphate","display_name":"Thiamine diphosphate","entity_type_key":"small_molecule"},"evidence_count":1,"mechanism_event":{"id":"c0adf37e-c161-5d5c-a232-de58cc6fe2e6","stable_key":"46d15d9e-d3b5-544d-ba01-b785aa3e4f42:b1-dhtkd1-thdp-dimer-sites-event","event_type":"biochemical_relationship","label":"DHTKD1 is its own B1 enzyme. Similarity to OGDH does not make the proteins interchangeable.","description":"The human DHTKD1 dimer structure places ThDP-containing active sites at the subunit interface and reveals a pocket compatible with the longer 2-oxoadipate substrate.","status":"provisional","compartment":{"slug":"mitochondrial-matrix","display_name":"Mitochondrial matrix"},"participants":[{"entity":{"id":"bff427ab-35f9-59c2-bb24-fd5953bbaec2","slug":"magnesium-ion","display_name":"Mg2+","entity_type_key":"ion"},"role":"cofactor-associated metal","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"22cbb32f-fa6b-57a0-a02d-8f2083585223","slug":"2-oxoadipate","display_name":"2-Oxoadipate","entity_type_key":"small_molecule"},"role":"preferred substrate considered by structural modeling","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"b8552ee2-4a84-59a0-9694-69991c9903bf","slug":"dhtkd1","display_name":"DHTKD1","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""},{"entity":{"id":"187db168-8028-5ce6-9f8b-4bc61ebad1a0","slug":"thiamine-diphosphate","display_name":"Thiamine diphosphate","entity_type_key":"small_molecule"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""}]},"contexts":[{"dimension":"evidence","value_text":"[{\"paper_key\": \"bezerra-2020-dhtkd1\", \"source_bundle\": \"artifacts/thiamine_metabolism_sources.json\", \"passage_ids\": [\"p-44\"], \"locator\": \"not included in the deposited\", \"preservation\": \"Exact text retained in the source bundle; full source document retained when openly retrievable.\"}]","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"1.9-A human DHTKD1 crystal structure.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Substrate-pocket interpretation is structural; an uncertain putative 2-oxoadipate density was not deposited as ligand.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient","value_text":"Thiamine (vitamin B1)","comparator":null,"unit":null,"notes":"","entity":{"slug":"thiamine","display_name":"Thiamine (vitamin B1)","entity_type_key":"small_molecule"}},{"dimension":"nutrient_topic","value_text":"Thiamine research collection; topical membership is not evidence of a direct dietary effect.","comparator":null,"unit":null,"notes":"","entity":{"slug":"thiamine","display_name":"Thiamine (vitamin B1)","entity_type_key":"small_molecule"}},{"dimension":"organism","value_text":"Homo sapiens","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"DHTKD1 is its own B1 enzyme. Similarity to OGDH does not make the proteins interchangeable.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[bezerra-2020-dhtkd1] Crystal structure and interaction studies of human DHTKD1 provide insight into a mitochondrial megacomplex in lysine catabolism (2020). https://pubmed.ncbi.nlm.nih.gov/32695416/ DOI: 10.1107/s205225252000696x","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Recombinant protein crystal","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"9dde0aa1-33e5-53a9-853e-d95278e85519","evidence_kind":"source_excerpt","locator":"Lines 896-907","start_line":896,"end_line":907,"excerpt":"### b1-dhtkd1-thdp-dimer-sites\nThe human DHTKD1 dimer structure places ThDP-containing active sites at the subunit interface and reveals a pocket compatible with the longer 2-oxoadipate substrate.\nCondition category: normal\nnutrient_topic: Thiamine research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: DHTKD1 is its own B1 enzyme. Similarity to OGDH does not make the proteins interchangeable.\norganism: Homo sapiens\ntissue_or_cell_type: Recombinant protein crystal\nexperimental_model: 1.9-A human DHTKD1 crystal structure.\nlimitations: Substrate-pocket interpretation is structural; an uncertain putative 2-oxoadipate density was not deposited as ligand.\nevidence: [{\"paper_key\": \"bezerra-2020-dhtkd1\", \"source_bundle\": \"artifacts/thiamine_metabolism_sources.json\", \"passage_ids\": [\"p-44\"], \"locator\": \"not included in the deposited\", \"preservation\": \"Exact text retained in the source bundle; full source document retained when openly retrievable.\"}]\nnutrient: Thiamine (vitamin B1)\n[bezerra-2020-dhtkd1] Crystal structure and interaction studies of human DHTKD1 provide insight into a mitochondrial megacomplex in lysine catabolism (2020). https://pubmed.ncbi.nlm.nih.gov/32695416/ DOI: 10.1107/s205225252000696x","model_system":"1.9-A human DHTKD1 crystal structure.","directness":"author_interpretation","verification_status":"source_derived_draft","notes":"Exact curation-document quotation, not publisher quotation. Study references: [bezerra-2020-dhtkd1] Crystal structure and interaction studies of human DHTKD1 provide insight into a mitochondrial megacomplex in lysine catabolism (2020). https://pubmed.ncbi.nlm.nih.gov/32695416/ DOI: 10.1107/s205225252000696x","relationship":"supports","weight":1.0,"link_notes":"","source":{"id":"158d2c03-ac8c-589f-8270-c468165ae346","stable_key":"import-46d15d9e-d3b5-544d-ba01-b785aa3e4f42","title":"Thiamine: mechanisms, deficiency and nutrient interactions (2026-09-17)","document_type":"imported_text","citation_label":"AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text.","file_path":"","sha256":"f376512fb3310141315548015b387833e3af45146e73fb73cd02cee20e4ddb9c","revision_id":"53bc5eda-dec8-58cc-a56f-a9eb4ab036ef","review_status":"unverified_draft","notes":""}}],"relations":[],"conflicts":[],"corrections":[],"research":null}