{"id":"1632217e-8ac5-57d8-9ae9-a4f4766addee","stable_key":"649e861b-265a-5912-bc36-3a73e53ef892:l-serine-serrs-bmaa-boundary","predicate":"does_not_activate","statement":"Purified BMAA was not a substrate for human seryl-tRNA synthetase in the study; human alanyl-tRNA synthetase instead activated it and formed BMAA-tRNA Ala.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"neutral","is_public":true,"mechanism_event_id":"9a19383a-10b0-575d-8b3e-f78c1cad290b","mechanism_event_label":"Chemical similarity to serine does not establish entry through the serine-loading enzyme.","subject":{"id":"990f63d9-f73d-56e3-af41-1e2569702480","slug":"sars1","display_name":"Human cytosolic seryl-tRNA synthetase / SARS1","entity_type_key":"protein"},"object":{"id":"bb3bbd7f-8ea6-5e87-9a4c-2d4e36251410","slug":"bmaa","display_name":"Beta-N-methylamino-L-alanine / BMAA","entity_type_key":"small_molecule"},"evidence_count":1,"mechanism_event":{"id":"9a19383a-10b0-575d-8b3e-f78c1cad290b","stable_key":"649e861b-265a-5912-bc36-3a73e53ef892:l-serine-serrs-bmaa-boundary-event","event_type":"observed_relationship","label":"Chemical similarity to serine does not establish entry through the serine-loading enzyme.","description":"Purified BMAA was not a substrate for human seryl-tRNA synthetase in the study; human alanyl-tRNA synthetase instead activated it and formed BMAA-tRNA Ala.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"990f63d9-f73d-56e3-af41-1e2569702480","slug":"sars1","display_name":"Human cytosolic seryl-tRNA synthetase / SARS1","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"bb3bbd7f-8ea6-5e87-9a4c-2d4e36251410","slug":"bmaa","display_name":"Beta-N-methylamino-L-alanine / BMAA","entity_type_key":"small_molecule"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"c882cd0b-9d83-5b07-bd1c-fe4d45657dcb","slug":"l-serine","display_name":"L-Serine","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""}]},"contexts":[{"dimension":"evidence_access","value_text":"Primary abstract","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Purified-substrate amino-acid activation and tRNA-charging assays.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Aminoacylation is not direct proof of the frequency of proteome misincorporation in humans.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"L-Serine collection; species, compartment, exposure, co-substrates and manipulation remain explicit.","comparator":null,"unit":null,"notes":"","entity":{"slug":"l-serine","display_name":"L-Serine","entity_type_key":"small_molecule"}},{"dimension":"plain_language","value_text":"Chemical similarity to serine does not establish entry through the serine-loading enzyme.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"The mechanism of β-N-methylamino-l-alanine inhibition of tRNA aminoacylation and its impact on misincorporation. · 2020 · https://pubmed.ncbi.nlm.nih.gov/31862734/ · DOI 10.1074/jbc.RA119.011714","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"63b5ee28-15ff-5988-8944-82617a57bb17","evidence_kind":"source_excerpt","locator":"Lines 398-404","start_line":398,"end_line":404,"excerpt":"## l-serine-serrs-bmaa-boundary\nChemical similarity to serine does not establish entry through the serine-loading enzyme.\nPurified BMAA was not a substrate for human seryl-tRNA synthetase in the study; human alanyl-tRNA synthetase instead activated it and formed BMAA-tRNA Ala.\nModel: Purified-substrate amino-acid activation and tRNA-charging assays.\nLimitations: Aminoacylation is not direct proof of the frequency of proteome misincorporation in humans.\nEvidence access: Primary abstract\nThe mechanism of β-N-methylamino-l-alanine inhibition of tRNA aminoacylation and its impact on misincorporation. · 2020 · https://pubmed.ncbi.nlm.nih.gov/31862734/ · DOI 10.1074/jbc.RA119.011714","model_system":"Purified-substrate amino-acid activation and tRNA-charging assays.","directness":"reported_statement","verification_status":"source_derived_draft","notes":"Original curation paraphrase; evidence access and experimental limitations specified.","relationship":"supports","weight":1.0,"link_notes":"","source":{"id":"70bcf57a-36bb-563f-9073-2d616e5f155a","stable_key":"import-649e861b-265a-5912-bc36-3a73e53ef892","title":"L-Serine: synthesis, one-carbon metabolism, lipids and cross-nutrient mechanisms (2026-09-19)","document_type":"imported_text","citation_label":"AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text.","file_path":"","sha256":"22a750ce2b94f8607268c58322c48c4f0468f403b72a4008307538a6e5ff86d5","revision_id":"c1d6a7e1-9558-5bc6-9e3b-7080c26d3dbc","review_status":"unverified_draft","notes":""}}],"relations":[],"conflicts":[],"corrections":[],"research":null}