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(2012). https://pubmed.ncbi.nlm.nih.gov/22123817/ DOI: 10.1074/jbc.m111.275982","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Purified HLCS and acceptor fragments","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"4155599e-1c3f-5126-9ddb-2fdb50883548","evidence_kind":"source_excerpt","locator":"Lines 416-427","start_line":416,"end_line":427,"excerpt":"### b7-hlcs-mcc-acceptor\nHLCS rapidly biotinylated the biotin-acceptor fragment of human MCCC1, with transfer limited by enzyme-substrate association.\nCondition category: normal\nnutrient_topic: Biotin research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: This mitochondrial enzyme has a biotin attachment domain recognized by HLCS.\norganism: Homo sapiens\ntissue_or_cell_type: Purified HLCS and acceptor fragments\nexperimental_model: Single-turnover biotin transfer to minimal BCCP fragments from all five human carboxylases\nlimitations: Fragment kinetics support differential recognition, not a universal nutrient-deficiency survival order in humans.\nexposure: Stopped-flow and quench-flow transfer kinetics\nevidence_span: {\"source_cache\": \"artifacts/biotin-research/22123817.abstract.txt\", \"locator\": \"Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"559afe20b6f8601a2d055d42fb121c89eaf1ece76afaa5cc0817c20787893233\", \"start_char\": 0, \"end_char\": 1502, \"text_sha256\": \"559afe20b6f8601a2d055d42fb121c89eaf1ece76afaa5cc0817c20787893233\"}\n[b7-p22123817] Selectivity in post-translational biotin addition to five human carboxylases. 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