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(2015). https://pubmed.ncbi.nlm.nih.gov/26592762/ DOI: 10.1038/srep16950","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Mitochondrial carbamoyl-phosphate synthesis","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"05494c33-ddbf-52b6-a747-c82e9bbce14b","evidence_kind":"source_excerpt","locator":"Lines 242-253","start_line":242,"end_line":253,"excerpt":"### citrulline-cps1-product\nCPS1 uses two ATP-dependent phosphorylation steps to convert bicarbonate and ammonia into carbamoyl phosphate.\nCondition category: normal\nnutrient_topic: Citrulline research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: The upstream part of citrulline synthesis consumes energy to handle ammonia.\norganism: Human CPS1\ntissue_or_cell_type: Mitochondrial carbamoyl-phosphate synthesis\nexperimental_model: Human recombinant enzyme crystallography and mutation analysis\nlimitations: Mechanism of enzyme activation; clinical effects of adding nutritional cofactors were not tested.\nexposure: Structures without NAG and with NAG plus nucleotides\nevidence_span: {\"source_cache\": \"artifacts/citrulline-research/26592762.fulltext.txt\", \"locator\": \"Primary full-text span; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"9807338d87ba1b5602512aa3765c7cc48d391595cc1f35e6a43bcbe1250d3c7d\", \"start_char\": 1169, \"end_char\": 1477, \"text_sha256\": \"c5e2a8e1d3e3a09064b7b233635f7d573f8761b3f6ae18a68bc9b102a2d5874c\"}\n[citrulline-p26592762] Structure of human carbamoyl phosphate synthetase: deciphering the on/off switch of human ureagenesis. 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