{"id":"0370ddbf-16f0-5edd-a1b1-5a56d877e417","stable_key":"31b1baa4-4113-5541-b9e7-fe44a5253a07:gallic-aroe","predicate":"converted_to_in_recorded_reaction","statement":"The studied E. coli AroE system supported NADP+-dependent DHS oxidation toward gallic acid.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"neutral","is_public":true,"mechanism_event_id":"29d1216b-a390-5516-922f-ce4f29fdce7f","mechanism_event_label":"The studied E. coli AroE system supported NADP+-dependent DHS oxidation toward gallic acid.","subject":{"id":"320d1df4-8da0-5e1a-bb17-5140e264bf06","slug":"3-dehydroshikimate","display_name":"3-Dehydroshikimate / DHS","entity_type_key":"small_molecule"},"object":{"id":"3f57fdfc-6135-5103-acae-ce55206fca16","slug":"gallic-acid","display_name":"Gallic acid","entity_type_key":"small_molecule"},"evidence_count":1,"mechanism_event":{"id":"29d1216b-a390-5516-922f-ce4f29fdce7f","stable_key":"31b1baa4-4113-5541-b9e7-fe44a5253a07:gallic-aroe-event","event_type":"biochemical_reaction","label":"The studied E. coli AroE system supported NADP+-dependent DHS oxidation toward gallic acid.","description":"**A plant oxidative branch is not a human metabolic pathway.** Walnut shikimate-dehydrogenase work and E. coli AroE assays support oxidation of DHS toward gallic acid with NADP+ in the studied enzyme systems; expression of walnut JrSDH in tobacco increased gallic-acid accumulation. This branch shows why substrate and redox context matter for enzyme function. It is not evidence that oral shikimic acid is converted into gallic acid by a human shikimate pathway. [Mechanism of gallic acid biosynthesis in bacteria (Escherichia coli) and walnut (Juglans regia).](https://pubmed.ncbi.nlm.nih.gov/21279669/)","status":"provisional","compartment":null,"participants":[{"entity":{"id":"320d1df4-8da0-5e1a-bb17-5140e264bf06","slug":"3-dehydroshikimate","display_name":"3-Dehydroshikimate / DHS","entity_type_key":"small_molecule"},"role":"input","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"3f57fdfc-6135-5103-acae-ce55206fca16","slug":"gallic-acid","display_name":"Gallic acid","entity_type_key":"small_molecule"},"role":"output","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"6abc4184-d20e-5708-af26-b04fbbc4393f","slug":"ecoli-aroe","display_name":"Escherichia coli shikimate dehydrogenase / AroE","entity_type_key":"protein"},"role":"catalyst","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""},{"entity":{"id":"be6e4670-953f-5a4e-97da-1e536a54e0e4","slug":"nadp-plus","display_name":"NADP+","entity_type_key":"small_molecule"},"role":"input","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""},{"entity":{"id":"4aba2a5e-8d06-5304-bb01-c0402b225a94","slug":"nadph","display_name":"NADPH","entity_type_key":"small_molecule"},"role":"output","stoichiometry":null,"state_label":"","sequence_order":4,"notes":""}]},"contexts":[{"dimension":"evidence_access","value_text":"Primary full text retrieved; relevant methods/results/figures reviewed. 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No clinical efficacy, nutrient deficiency or unique molecular mediation is inferred.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"The studied E. coli AroE system supported NADP+-dependent DHS oxidation toward gallic acid.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"Mechanism of gallic acid biosynthesis in bacteria (Escherichia coli) and walnut (Juglans regia). | 2011 | DOI 10.1007/s11103-011-9739-3 | PMID 21279669 | https://pubmed.ncbi.nlm.nih.gov/21279669/ | https://doi.org/10.1007/s11103-011-9739-3 | https://pmc.ncbi.nlm.nih.gov/articles/PMC3057006/","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"source_locator","value_text":"Reviewed reference lines 87-87; exact primary location described in quoted passage where extracted.","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"ca68950d-d584-5f1b-9b8c-4499fd09c6ef","evidence_kind":"source_excerpt","locator":"Lines 87-87","start_line":87,"end_line":87,"excerpt":"**A plant oxidative branch is not a human metabolic pathway.** Walnut shikimate-dehydrogenase work and E. coli AroE assays support oxidation of DHS toward gallic acid with NADP+ in the studied enzyme systems; expression of walnut JrSDH in tobacco increased gallic-acid accumulation. This branch shows why substrate and redox context matter for enzyme function. It is not evidence that oral shikimic acid is converted into gallic acid by a human shikimate pathway. [Mechanism of gallic acid biosynthesis in bacteria (Escherichia coli) and walnut (Juglans regia).](https://pubmed.ncbi.nlm.nih.gov/21279669/)","model_system":"Purified enzyme oxidative branch with subsequent spontaneous aromatization proposed in the paper, distinct from NADPH-driven DHS reduction.","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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