{"id":"fc61bcfa-3d41-53da-89da-14c5a972739c","stable_key":"56f1d914-e7da-595a-af69-c217b2b47407:l-phenylalanine-cytosolic-charging","predicate":"charges","statement":"Human cytosolic phenylalanyl-tRNA synthetase activates phenylalanine and attaches it to tRNA(Phe), with editing that discriminates against mischarged aromatic amino acids.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"5868b32d-6483-5dce-9eb6-470e77ae8c54","mechanism_event_label":"Protein construction needs a molecular loading and proofreading system.","subject":{"id":"26dc1ace-5c76-55b6-b3c8-b48b3f4b4c8e","slug":"farsa-farsb","display_name":"Human cytosolic FARSA/FARSB phenylalanyl-tRNA synthetase","entity_type_key":"protein_complex"},"object":{"id":"7a449c74-58e4-5180-b092-8dd37da05a69","slug":"human-cytosolic-trna-phe","display_name":"Human cytosolic tRNA(Phe)","entity_type_key":"rna"},"evidence_count":1,"mechanism_event":{"id":"5868b32d-6483-5dce-9eb6-470e77ae8c54","stable_key":"56f1d914-e7da-595a-af69-c217b2b47407:l-phenylalanine-cytosolic-charging-event","event_type":"observed_relationship","label":"Protein construction needs a molecular loading and proofreading system.","description":"Human cytosolic phenylalanyl-tRNA synthetase activates phenylalanine and attaches it to tRNA(Phe), with editing that discriminates against mischarged aromatic amino acids.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"26dc1ace-5c76-55b6-b3c8-b48b3f4b4c8e","slug":"farsa-farsb","display_name":"Human cytosolic FARSA/FARSB phenylalanyl-tRNA synthetase","entity_type_key":"protein_complex"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"7a449c74-58e4-5180-b092-8dd37da05a69","slug":"human-cytosolic-trna-phe","display_name":"Human cytosolic tRNA(Phe)","entity_type_key":"rna"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"190407ad-0219-54b5-b05f-7c75f3895ca6","slug":"l-phenylalanine","display_name":"L-Phenylalanine","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""},{"entity":{"id":"58b974f1-d389-5bf6-81cd-889c44442c42","slug":"atp","display_name":"ATP","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""}]},"contexts":[{"dimension":"evidence_access","value_text":"Primary abstract","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Human phenylalanyl-tRNA synthetase biochemical comparison.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"This aminoacylation function is distinct from conversion of phenylalanine to tyrosine.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"L-Phenylalanine collection; species, compartment, exposure, co-substrates and manipulation remain explicit.","comparator":null,"unit":null,"notes":"","entity":{"slug":"l-phenylalanine","display_name":"L-Phenylalanine","entity_type_key":"small_molecule"}},{"dimension":"plain_language","value_text":"Protein construction needs a molecular loading and proofreading system.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"Bacterial and eukaryotic phenylalanyl-tRNA synthetases catalyze misaminoacylation of tRNA(Phe) with 3,4-dihydroxy-L-phenylalanine. · 2011 · https://pubmed.ncbi.nlm.nih.gov/22035791/ · DOI 10.1016/j.chembiol.2011.08.008","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"2b83f6fd-4d4b-5b69-8dc7-a36e2ab21fa8","evidence_kind":"source_excerpt","locator":"Lines 126-132","start_line":126,"end_line":132,"excerpt":"## l-phenylalanine-cytosolic-charging\nProtein construction needs a molecular loading and proofreading system.\nHuman cytosolic phenylalanyl-tRNA synthetase activates phenylalanine and attaches it to tRNA(Phe), with editing that discriminates against mischarged aromatic amino acids.\nModel: Human phenylalanyl-tRNA synthetase biochemical comparison.\nLimitations: This aminoacylation function is distinct from conversion of phenylalanine to tyrosine.\nEvidence access: Primary abstract\nBacterial and eukaryotic phenylalanyl-tRNA synthetases catalyze misaminoacylation of tRNA(Phe) with 3,4-dihydroxy-L-phenylalanine. · 2011 · https://pubmed.ncbi.nlm.nih.gov/22035791/ · DOI 10.1016/j.chembiol.2011.08.008","model_system":"Human phenylalanyl-tRNA synthetase biochemical comparison.","directness":"reported_statement","verification_status":"source_derived_draft","notes":"Original curation paraphrase; 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