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(2001). https://pubmed.ncbi.nlm.nih.gov/11747433/ DOI: 10.1021/bi011526e","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Argininosuccinate cleavage","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"e4bcee69-c4ec-555c-8315-c28aeebe1284","evidence_kind":"source_excerpt","locator":"Lines 190-201","start_line":190,"end_line":201,"excerpt":"### citrulline-asl-fumarate\nFumarate is the other product of the ASL-catalyzed argininosuccinate cleavage reaction.\nCondition category: normal\nnutrient_topic: Citrulline research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: This reaction connects amino-acid nitrogen handling with a carbon-metabolism intermediate.\norganism: Human ASL expressed experimentally\ntissue_or_cell_type: Argininosuccinate cleavage\nexperimental_model: Recombinant human enzyme complementation and stability experiments\nlimitations: Reaction identity and complementation are established in enzyme systems; these variants do not describe all ASL deficiencies.\nexposure: Wild type and Q286R, D87G, M360T or A398D variants\nevidence_span: {\"source_cache\": \"artifacts/citrulline-research/11747433.abstract.txt\", \"locator\": \"Primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"1d57b633c558211169c38f4dc40cceeeb373c63d291c80d2523c8e48b54427b1\", \"start_char\": 0, \"end_char\": 1617, \"text_sha256\": \"1d57b633c558211169c38f4dc40cceeeb373c63d291c80d2523c8e48b54427b1\"}\n[citrulline-p11747433] Mechanisms for intragenic complementation at the human argininosuccinate lyase locus. 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