{"id":"0864d760-b6db-5e89-bfbc-958e04bbbf6f","stable_key":"31b1baa4-4113-5541-b9e7-fe44a5253a07:chorismate-production","predicate":"converted_to_in_recorded_reaction","statement":"AroC forms chorismate from EPSP with reduced-FMN dependence and phosphate elimination.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"neutral","is_public":true,"mechanism_event_id":"4143bfe4-6ee9-5a65-8662-82978213d893","mechanism_event_label":"AroC forms chorismate from EPSP with reduced-FMN dependence and phosphate elimination.","subject":{"id":"e27b2697-e6fe-59a6-ace0-69924b289e20","slug":"epsp","display_name":"5-Enolpyruvylshikimate 3-phosphate / EPSP","entity_type_key":"small_molecule"},"object":{"id":"849c016e-9dc8-567c-81b5-c8434c558a5f","slug":"chorismate","display_name":"Chorismate","entity_type_key":"small_molecule"},"evidence_count":1,"mechanism_event":{"id":"4143bfe4-6ee9-5a65-8662-82978213d893","stable_key":"31b1baa4-4113-5541-b9e7-fe44a5253a07:chorismate-production-event","event_type":"biochemical_reaction","label":"AroC forms chorismate from EPSP with reduced-FMN dependence and phosphate elimination.","description":"**Chorismate synthase needs reduced FMN.** E. coli AroC converts EPSP to chorismate with phosphate elimination. Reduced FMN is required although the overall substrate conversion is not a net redox reaction; flavin is a catalytic cofactor rather than a stoichiometrically consumed vitamin. The 1998 study observed a stable oxidized-FMN/EPSP/enzyme complex without productive turnover. Binding, cofactor quantity and cofactor redox state therefore answer different questions. In Neurospora crassa, bifunctional chorismate synthase can use NADPH to reduce its flavin; that reductase capability must not be assigned to every bacterial AroC. [Evidence for a major structural change in Escherichia coli chorismate synthase induced by flavin and substrate binding.](https://pubmed.ncbi.nlm.nih.gov/9761730/) [Mechanism of chorismate synthase. Role of the two invariant histidine residues in the active site.](https://pubmed.ncbi.nlm.nih.gov/14668332/)","status":"provisional","compartment":null,"participants":[{"entity":{"id":"e27b2697-e6fe-59a6-ace0-69924b289e20","slug":"epsp","display_name":"5-Enolpyruvylshikimate 3-phosphate / EPSP","entity_type_key":"small_molecule"},"role":"input","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"849c016e-9dc8-567c-81b5-c8434c558a5f","slug":"chorismate","display_name":"Chorismate","entity_type_key":"small_molecule"},"role":"output","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"c8d1c271-dd44-5865-ae28-e4de9e5db241","slug":"ecoli-aroc","display_name":"Escherichia coli chorismate synthase / AroC","entity_type_key":"protein"},"role":"catalyst","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""},{"entity":{"id":"b28dfc54-a5ef-5f9e-ac1f-890b68e58dc3","slug":"inorganic-phosphate","display_name":"Inorganic phosphate","entity_type_key":"chemical_species"},"role":"output","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""},{"entity":{"id":"1b570f02-2ada-5d19-b6f7-64afeb0a073c","slug":"reduced-fmn","display_name":"Reduced flavin mononucleotide / FMNH2","entity_type_key":"small_molecule"},"role":"cofactor","stoichiometry":null,"state_label":"","sequence_order":4,"notes":""}]},"contexts":[{"dimension":"evidence_access","value_text":"Primary indexed abstract reviewed; full results, tables and supplements not independently extracted.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Escherichia coli biochemical pathway; source-specific enzyme evidence recorded in the passage.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"interpretation_status","value_text":"Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Interpret only within the recorded preparation, exposure and comparator. 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Role of the two invariant histidine residues in the active site. | 2004 | DOI 10.1074/jbc.m312471200 | PMID 14668332 | https://pubmed.ncbi.nlm.nih.gov/14668332/ | https://doi.org/10.1074/jbc.m312471200","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"source_locator","value_text":"Reviewed reference lines 21-21; exact primary location described in quoted passage where extracted.","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"21e52722-e746-5b82-92ad-cd57a9a41abc","evidence_kind":"source_excerpt","locator":"Lines 21-21","start_line":21,"end_line":21,"excerpt":"**Chorismate synthase needs reduced FMN.** E. coli AroC converts EPSP to chorismate with phosphate elimination. Reduced FMN is required although the overall substrate conversion is not a net redox reaction; flavin is a catalytic cofactor rather than a stoichiometrically consumed vitamin. The 1998 study observed a stable oxidized-FMN/EPSP/enzyme complex without productive turnover. Binding, cofactor quantity and cofactor redox state therefore answer different questions. In Neurospora crassa, bifunctional chorismate synthase can use NADPH to reduce its flavin; that reductase capability must not be assigned to every bacterial AroC. [Evidence for a major structural change in Escherichia coli chorismate synthase induced by flavin and substrate binding.](https://pubmed.ncbi.nlm.nih.gov/9761730/) [Mechanism of chorismate synthase. Role of the two invariant histidine residues in the active site.](https://pubmed.ncbi.nlm.nih.gov/14668332/)","model_system":"Escherichia coli biochemical pathway; source-specific enzyme evidence recorded in the passage.","directness":"reported_statement","verification_status":"source_derived_draft","notes":"Exact excerpt of the retained AI-assisted reviewed reference; primary sources are cited in primary_references and access scope is retained. 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