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(2000). https://pubmed.ncbi.nlm.nih.gov/10651636/ DOI: 10.1021/bi9918700","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Recombinant human muscle/heart CPT1B","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"d69f851e-13f7-54d1-b509-88f84986c4e2","evidence_kind":"source_excerpt","locator":"Lines 741-752","start_line":741,"end_line":752,"excerpt":"### b7-malonyl-cpt1b\nWild-type human CPT1B showed high-affinity malonyl-CoA binding and inhibition in recombinant mitochondrial assays.\nCondition category: normal\nnutrient_topic: Biotin research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: Malonyl-CoA links the carboxylase pathway to the carnitine-dependent fat-entry step.\norganism: Homo sapiens\ntissue_or_cell_type: Recombinant human muscle/heart CPT1B\nexperimental_model: Human CPT1B wild type and N-terminal deletions expressed in yeast mitochondria\nlimitations: Expression host is yeast; these data concern human CPT1B, not every CPT1 isoform or a biotin supplementation outcome.\nexposure: Malonyl-CoA binding and activity assays\nevidence_span: {\"source_cache\": \"artifacts/biotin-research/10651636.abstract.txt\", \"locator\": \"Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"e99728ef83700f17a810421385b71ea243576419df807dc4749b588beb01d400\", \"start_char\": 0, \"end_char\": 1542, \"text_sha256\": \"e99728ef83700f17a810421385b71ea243576419df807dc4749b588beb01d400\"}\n[b7-p10651636] The first 28 N-terminal amino acid residues of human heart muscle carnitine palmitoyltransferase I are essential for malonyl CoA sensitivity and high-affinity binding. 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