{"id":"f38c0677-ce23-5697-9c2f-4895ed71ee26","stable_key":"63ce713e-6aea-59f6-9896-ca30e010b2ce:l-tyrosine-tyrosine-cleavage","predicate":"inhibits","statement":"At 0.5 millimolar in the substrate preincubation assay, tyrosine inhibited MMP8 cleavage of YARS1 but did not inhibit MMP7 cleavage.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"negative","is_public":true,"mechanism_event_id":"89f54e0a-23d4-5d41-b65a-2f82936490b4","mechanism_event_label":"The amino acid can alter how one protease handles its loading enzyme.","subject":{"id":"bcfef85f-831d-5439-ba51-1aef4b090441","slug":"l-tyrosine","display_name":"L-Tyrosine","entity_type_key":"small_molecule"},"object":{"id":"df91ef29-7249-5d65-8dd0-02d86f1bc12e","slug":"human-mmp8-yars1-cleavage","display_name":"Human MMP8 cleavage of YARS1","entity_type_key":"cellular_process"},"evidence_count":1,"mechanism_event":{"id":"89f54e0a-23d4-5d41-b65a-2f82936490b4","stable_key":"63ce713e-6aea-59f6-9896-ca30e010b2ce:l-tyrosine-tyrosine-cleavage-event","event_type":"observed_relationship","label":"The amino acid can alter how one protease handles its loading enzyme.","description":"At 0.5 millimolar in the substrate preincubation assay, tyrosine inhibited MMP8 cleavage of YARS1 but did not inhibit MMP7 cleavage.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"bcfef85f-831d-5439-ba51-1aef4b090441","slug":"l-tyrosine","display_name":"L-Tyrosine","entity_type_key":"small_molecule"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"df91ef29-7249-5d65-8dd0-02d86f1bc12e","slug":"human-mmp8-yars1-cleavage","display_name":"Human MMP8 cleavage of YARS1","entity_type_key":"cellular_process"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"1e70f8cb-144f-5c63-b862-0c8670840077","slug":"yars1","display_name":"Human cytosolic tyrosyl-tRNA synthetase / YARS1","entity_type_key":"protein"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""},{"entity":{"id":"ecfa9184-22c1-5465-8df6-ddf33cee0bbf","slug":"mmp8","display_name":"Human matrix metalloproteinase 8 / MMP8","entity_type_key":"protein"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""},{"entity":{"id":"754f79df-5314-5c4a-ae4f-77193d72489d","slug":"mmp7","display_name":"Human matrix metalloproteinase 7 / MMP7","entity_type_key":"protein"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":4,"notes":""}]},"contexts":[{"dimension":"evidence_access","value_text":"Primary full text; substrate/product cleavage methods and results","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"30-minute substrate preincubation at 22 degrees C; subsequent recombinant-enzyme cleavage assay.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"This is not demonstrated inhibition of MMP8 generally or a clinical anti-inflammatory effect.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"L-Tyrosine collection; species, compartment, exposure, co-substrates and manipulation remain explicit.","comparator":null,"unit":null,"notes":"","entity":{"slug":"l-tyrosine","display_name":"L-Tyrosine","entity_type_key":"small_molecule"}},{"dimension":"plain_language","value_text":"The amino acid can alter how one protease handles its loading enzyme.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"Moonlighting matrix metalloproteinase substrates: Enhancement of proinflammatory functions of extracellular tyrosyl-tRNA synthetase upon cleavage. · 2020 · https://pubmed.ncbi.nlm.nih.gov/31771979/ · DOI 10.1074/jbc.RA119.010486","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"fc4e05b2-2e57-5cc9-9bdd-7c6a3db1770c","evidence_kind":"source_excerpt","locator":"Lines 124-130","start_line":124,"end_line":130,"excerpt":"## l-tyrosine-tyrosine-cleavage\nThe amino acid can alter how one protease handles its loading enzyme.\nAt 0.5 millimolar in the substrate preincubation assay, tyrosine inhibited MMP8 cleavage of YARS1 but did not inhibit MMP7 cleavage.\nModel: 30-minute substrate preincubation at 22 degrees C; subsequent recombinant-enzyme cleavage assay.\nLimitations: This is not demonstrated inhibition of MMP8 generally or a clinical anti-inflammatory effect.\nEvidence access: Primary full text; substrate/product cleavage methods and results\nMoonlighting matrix metalloproteinase substrates: Enhancement of proinflammatory functions of extracellular tyrosyl-tRNA synthetase upon cleavage. · 2020 · https://pubmed.ncbi.nlm.nih.gov/31771979/ · DOI 10.1074/jbc.RA119.010486","model_system":"30-minute substrate preincubation at 22 degrees C; subsequent recombinant-enzyme cleavage assay.","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":"12917df2-c6e0-5b61-850f-dbff6d4b4d30","stable_key":"import-63ce713e-6aea-59f6-9896-ca30e010b2ce","title":"L-Tyrosine: catecholamines, thyroid chemistry, pigment, metabolism 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. 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