{"id":"161e4c97-361e-5b97-984a-a344edc55e4c","stable_key":"08ce9896-9d1c-5bbf-b705-5bfe771091d5:b7-pcc-pccb","predicate":"provides_carboxyltransferase_activity","statement":"PCCB provides the carboxyltransferase activity of human PCC.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"a82f7960-f241-57b7-992c-efa05061d4e8","mechanism_event_label":"The beta subunit performs the transfer onto the carbon substrate.","subject":{"id":"7b89757c-8128-5a33-949b-278db62f047a","slug":"pccb","display_name":"Human propionyl-CoA carboxylase beta subunit / PCCB","entity_type_key":"protein"},"object":{"id":"54eb0f2f-091c-54cd-b4a1-a528b994560a","slug":"human-propionyl-coa-carboxylase","display_name":"Human propionyl-CoA carboxylase / PCC","entity_type_key":"protein_complex"},"evidence_count":1,"mechanism_event":{"id":"a82f7960-f241-57b7-992c-efa05061d4e8","stable_key":"08ce9896-9d1c-5bbf-b705-5bfe771091d5:b7-pcc-pccb-event","event_type":"biochemical_relationship","label":"The beta subunit performs the transfer onto the carbon substrate.","description":"PCCB provides the carboxyltransferase activity of human PCC.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"69ac0570-94d8-59d8-85ef-7f67cf302d16","slug":"propionyl-coa","display_name":"Propionyl-CoA","entity_type_key":"small_molecule"},"role":"acceptor","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"a70f19d8-f2d2-5951-9f48-7961317a14ea","slug":"s-methylmalonyl-coa","display_name":"(S)-Methylmalonyl-CoA","entity_type_key":"small_molecule"},"role":"product","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"9cd8356f-9496-51f7-9d0b-270019e39810","slug":"pcca","display_name":"Human propionyl-CoA carboxylase alpha subunit / PCCA","entity_type_key":"protein"},"role":"partner subunit","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""},{"entity":{"id":"7b89757c-8128-5a33-949b-278db62f047a","slug":"pccb","display_name":"Human propionyl-CoA carboxylase beta subunit / PCCB","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""},{"entity":{"id":"54eb0f2f-091c-54cd-b4a1-a528b994560a","slug":"human-propionyl-coa-carboxylase","display_name":"Human propionyl-CoA carboxylase / PCC","entity_type_key":"protein_complex"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":4,"notes":""}]},"contexts":[{"dimension":"evidence_span","value_text":"{\"source_cache\": \"artifacts/biotin-research/20725044.abstract.txt\", \"locator\": \"Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"825bf28b9f35a8d45f8d08d883fa200bd430336b0558db035ce4fd1c5ef19053\", \"start_char\": 0, \"end_char\": 1921, \"text_sha256\": \"825bf28b9f35a8d45f8d08d883fa200bd430336b0558db035ce4fd1c5ef19053\"}","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Bacterial PCC crystallography and separate 15-angstrom human PCC cryo-EM reconstruction","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"Structural analysis","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Atomic bacterial positions are not high-resolution human measurements. Human cryo-EM establishes the overall assembly at lower resolution.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"Biotin research collection; topical membership is not evidence of a direct dietary effect.","comparator":null,"unit":null,"notes":"","entity":{"slug":"biotin","display_name":"Biotin","entity_type_key":"small_molecule"}},{"dimension":"organism","value_text":"Homo sapiens; bacterial PCC comparison","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"The beta subunit performs the transfer onto the carbon substrate.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[b7-p20725044] Crystal structure of the alpha(6)beta(6) holoenzyme of propionyl-coenzyme A carboxylase. (2010). https://pubmed.ncbi.nlm.nih.gov/20725044/ DOI: 10.1038/nature09302","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Purified PCC complexes","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"947d82c9-af8d-52df-bbbe-01425b468cdd","evidence_kind":"source_excerpt","locator":"Lines 611-622","start_line":611,"end_line":622,"excerpt":"### b7-pcc-pccb\nPCCB provides the carboxyltransferase activity of human PCC.\nCondition category: normal\nnutrient_topic: Biotin research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: The beta subunit performs the transfer onto the carbon substrate.\norganism: Homo sapiens; bacterial PCC comparison\ntissue_or_cell_type: Purified PCC complexes\nexperimental_model: Bacterial PCC crystallography and separate 15-angstrom human PCC cryo-EM reconstruction\nlimitations: Atomic bacterial positions are not high-resolution human measurements. Human cryo-EM establishes the overall assembly at lower resolution.\nexposure: Structural analysis\nevidence_span: {\"source_cache\": \"artifacts/biotin-research/20725044.abstract.txt\", \"locator\": \"Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"825bf28b9f35a8d45f8d08d883fa200bd430336b0558db035ce4fd1c5ef19053\", \"start_char\": 0, \"end_char\": 1921, \"text_sha256\": \"825bf28b9f35a8d45f8d08d883fa200bd430336b0558db035ce4fd1c5ef19053\"}\n[b7-p20725044] Crystal structure of the alpha(6)beta(6) holoenzyme of propionyl-coenzyme A carboxylase. (2010). https://pubmed.ncbi.nlm.nih.gov/20725044/ DOI: 10.1038/nature09302","model_system":"Bacterial PCC crystallography and separate 15-angstrom human PCC cryo-EM reconstruction","directness":"author_interpretation","verification_status":"source_derived_draft","notes":"Exact curation-document quotation, not publisher quotation. Study references: [b7-p20725044] Crystal structure of the alpha(6)beta(6) holoenzyme of propionyl-coenzyme A carboxylase. (2010). https://pubmed.ncbi.nlm.nih.gov/20725044/ DOI: 10.1038/nature09302","relationship":"supports","weight":1.0,"link_notes":"","source":{"id":"9608806b-adb6-5a35-b042-057147135642","stable_key":"import-08ce9896-9d1c-5bbf-b705-5bfe771091d5","title":"Biotin: carboxylases, recycling, 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":"a05b23a45e0813ba2fcda0027e3f5d9d58b82858f8dd8598ffb7aca17e942a38","revision_id":"e0d0c2a2-e9e2-55dd-b467-41c22ba960d4","review_status":"unverified_draft","notes":""}}],"relations":[],"conflicts":[],"corrections":[],"research":null}