{"id":"17b9d870-1a24-5246-8758-2d20fafea65e","stable_key":"a9828b14-fbd7-57bf-9e01-0d52d1b42a1f:citrulline-asl-arginine","predicate":"cleaves_to","statement":"Human ASL catalyzes reversible cleavage of argininosuccinate to arginine and fumarate.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"215036b3-fe9d-5976-9d0f-7b9575533cdd","mechanism_event_label":"The second enzyme releases arginine from the intermediate.","subject":{"id":"bb8e0338-29f7-581b-b0ba-971acff917c5","slug":"asl","display_name":"Human argininosuccinate lyase / ASL","entity_type_key":"protein"},"object":{"id":"eeca3c9e-7749-5677-b7bd-37fe8f7c228d","slug":"arginine","display_name":"L-Arginine","entity_type_key":"small_molecule"},"evidence_count":1,"mechanism_event":{"id":"215036b3-fe9d-5976-9d0f-7b9575533cdd","stable_key":"a9828b14-fbd7-57bf-9e01-0d52d1b42a1f:citrulline-asl-arginine-event","event_type":"biochemical_relationship","label":"The second enzyme releases arginine from the intermediate.","description":"Human ASL catalyzes reversible cleavage of argininosuccinate to arginine and fumarate.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"d4847103-f17d-57bf-8ad9-04436b9eb16f","slug":"argininosuccinate","display_name":"L-Argininosuccinate","entity_type_key":"small_molecule"},"role":"substrate","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"eeca3c9e-7749-5677-b7bd-37fe8f7c228d","slug":"arginine","display_name":"L-Arginine","entity_type_key":"small_molecule"},"role":"product","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"0d6dab6c-2d8c-5b60-a115-63f238631e1d","slug":"fumarate","display_name":"Fumarate","entity_type_key":"small_molecule"},"role":"product","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""},{"entity":{"id":"bb8e0338-29f7-581b-b0ba-971acff917c5","slug":"asl","display_name":"Human argininosuccinate lyase / ASL","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""}]},"contexts":[{"dimension":"evidence_span","value_text":"{\"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\"}","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Recombinant human enzyme complementation and stability experiments","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"Wild type and Q286R, D87G, M360T or A398D variants","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Reaction identity and complementation are established in enzyme systems; these variants do not describe all ASL deficiencies.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"Citrulline research collection; topical membership is not evidence of a direct dietary effect.","comparator":null,"unit":null,"notes":"","entity":{"slug":"citrulline","display_name":"L-Citrulline","entity_type_key":"small_molecule"}},{"dimension":"organism","value_text":"Human ASL expressed experimentally","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"The second enzyme releases arginine from the intermediate.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[citrulline-p11747433] Mechanisms for intragenic complementation at the human argininosuccinate lyase locus. (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":"b44d486f-3262-56ea-b64c-8c87982d1d55","evidence_kind":"source_excerpt","locator":"Lines 177-188","start_line":177,"end_line":188,"excerpt":"### citrulline-asl-arginine\nHuman ASL catalyzes reversible cleavage of argininosuccinate to arginine and fumarate.\nCondition category: normal\nnutrient_topic: Citrulline research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: The second enzyme releases arginine from the 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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