{"id":"0fea0ed8-79ad-5596-af0f-b4592a3d8fbf","stable_key":"6cdb37aa-8998-5ea8-829d-4f995caf98fc:l-carnitine-cntb-redox","predicate":"transfers_electrons_to","statement":"CntB passed NADH-derived electrons through FMN and iron-sulfur centers to support CntA oxygen activation.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"969ed72c-7e83-5ac7-a8d0-cd1f369eefa2","mechanism_event_label":"Riboflavin-derived FMN, iron centers and NADH connect to microbial carnitine chemistry.","subject":{"id":"96e90bd3-7403-5b82-8743-896d14024eb1","slug":"a-baumannii-cntb","display_name":"Acinetobacter baumannii CntB reductase component","entity_type_key":"protein"},"object":{"id":"eba25fb7-ae7f-5b0f-8a5d-b6b658c55657","slug":"a-baumannii-cnta","display_name":"Acinetobacter baumannii CntA carnitine monooxygenase component","entity_type_key":"protein"},"evidence_count":1,"mechanism_event":{"id":"969ed72c-7e83-5ac7-a8d0-cd1f369eefa2","stable_key":"6cdb37aa-8998-5ea8-829d-4f995caf98fc:l-carnitine-cntb-redox-event","event_type":"observed_relationship","label":"Riboflavin-derived FMN, iron centers and NADH connect to microbial carnitine chemistry.","description":"CntB passed NADH-derived electrons through FMN and iron-sulfur centers to support CntA oxygen activation.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"96e90bd3-7403-5b82-8743-896d14024eb1","slug":"a-baumannii-cntb","display_name":"Acinetobacter baumannii CntB reductase component","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"eba25fb7-ae7f-5b0f-8a5d-b6b658c55657","slug":"a-baumannii-cnta","display_name":"Acinetobacter baumannii CntA carnitine monooxygenase component","entity_type_key":"protein"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"9fbf2e03-16a9-5ca7-965c-0bfc07ca24da","slug":"nadh","display_name":"NADH","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""},{"entity":{"id":"d3eacf85-1a35-546d-bd30-161474dd9691","slug":"fmn","display_name":"Flavin mononucleotide","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""},{"entity":{"id":"59d6d1cd-df32-5b58-b950-3188bc7b95d6","slug":"iron-ii","display_name":"Ferrous iron","entity_type_key":"ion"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":4,"notes":""},{"entity":{"id":"6e34c035-9371-578f-b799-fd2a14e9e40f","slug":"l-carnitine","display_name":"L-Carnitine","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":5,"notes":""}]},"contexts":[{"dimension":"evidence_access","value_text":"Primary abstract","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Acinetobacter enzyme redox spectroscopy and site-directed mutants.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Bacterial cofactor dependence does not show that human B2 or iron supplementation increases TMAO.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"L-Carnitine collection; isomer, preparation, species, exposure and manipulation remain explicit.","comparator":null,"unit":null,"notes":"","entity":{"slug":"l-carnitine","display_name":"L-Carnitine","entity_type_key":"small_molecule"}},{"dimension":"plain_language","value_text":"Riboflavin-derived FMN, iron centers and NADH connect to microbial carnitine chemistry.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"Carnitine metabolism in the human gut: characterization of the two-component carnitine monooxygenase CntAB from Acinetobacter baumannii. · 2020 · https://pubmed.ncbi.nlm.nih.gov/32694223/ · DOI 10.1074/jbc.RA120.014266","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"6c54c722-f181-5310-a9d6-9a19f335685a","evidence_kind":"source_excerpt","locator":"Lines 394-400","start_line":394,"end_line":400,"excerpt":"## l-carnitine-cntb-redox\nRiboflavin-derived FMN, iron centers and NADH connect to microbial carnitine chemistry.\nCntB passed NADH-derived electrons through FMN and iron-sulfur centers to support CntA oxygen activation.\nModel: Acinetobacter enzyme redox spectroscopy and site-directed mutants.\nLimitations: Bacterial cofactor dependence does not show that human B2 or iron supplementation increases TMAO.\nEvidence access: Primary abstract\nCarnitine metabolism in the human gut: characterization of the two-component carnitine monooxygenase CntAB from Acinetobacter baumannii. · 2020 · https://pubmed.ncbi.nlm.nih.gov/32694223/ · DOI 10.1074/jbc.RA120.014266","model_system":"Acinetobacter enzyme redox spectroscopy and site-directed mutants.","directness":"reported_statement","verification_status":"source_derived_draft","notes":"Original curation paraphrase; 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