{"id":"388ed3f4-819a-5a6f-b154-c9251088f7bb","stable_key":"31b1baa4-4113-5541-b9e7-fe44a5253a07:kinase-ecoli-arok","predicate":"converted_to_in_recorded_reaction","statement":"The ecoli-arok kinase phosphorylates shikimate using ATP.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"neutral","is_public":true,"mechanism_event_id":"23d444b6-5ca1-56ef-9d14-aa2d13e21256","mechanism_event_label":"The ecoli-arok kinase phosphorylates shikimate using ATP.","subject":{"id":"fe7a4dc3-4f06-586b-9457-2dd949e2fa36","slug":"shikimate","display_name":"Shikimate anion","entity_type_key":"small_molecule"},"object":{"id":"ba13ffaa-56b5-5976-945c-71c0921defd8","slug":"shikimate-3-phosphate","display_name":"Shikimate 3-phosphate","entity_type_key":"small_molecule"},"evidence_count":1,"mechanism_event":{"id":"23d444b6-5ca1-56ef-9d14-aa2d13e21256","stable_key":"31b1baa4-4113-5541-b9e7-fe44a5253a07:kinase-ecoli-arok-event","event_type":"biochemical_reaction","label":"The ecoli-arok kinase phosphorylates shikimate using ATP.","description":"**ATP and magnesium at shikimate kinase.** Shikimate kinase transfers a phosphoryl group from ATP to shikimate, yielding shikimate-3-phosphate and ADP. The Erwinia chrysanthemi enzyme study identifies magnesium dependence and a Mg–ADP structural complex; this is a microbial enzyme requirement, not a demonstrated human magnesium-deficiency phenotype. E. coli has AroK and AroL kinase isoenzymes with different substrate affinities. The AroK structural paper discusses approximate shikimate Km values of 20 mM versus 0.2 mM for the two systems; these are organism/assay properties, not plasma targets. Loss of both kinases produces aromatic-amino-acid auxotrophy; environmental nutrient rescue and isoenzyme compensation matter. [Biochemical and X-ray crystallographic studies on shikimate kinase: the important structural role of the P-loop lysine.](https://pubmed.ncbi.nlm.nih.gov/11369852/) [Crystal structure of the Escherichia coli shikimate kinase I (AroK) that confers sensitivity to mecillinam.](https://pubmed.ncbi.nlm.nih.gov/12001235/)","status":"provisional","compartment":null,"participants":[{"entity":{"id":"fe7a4dc3-4f06-586b-9457-2dd949e2fa36","slug":"shikimate","display_name":"Shikimate anion","entity_type_key":"small_molecule"},"role":"input","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"ba13ffaa-56b5-5976-945c-71c0921defd8","slug":"shikimate-3-phosphate","display_name":"Shikimate 3-phosphate","entity_type_key":"small_molecule"},"role":"output","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"71659bcc-4aaf-57af-a4df-e8affd61b300","slug":"ecoli-arok","display_name":"Escherichia coli shikimate kinase I / AroK","entity_type_key":"protein"},"role":"catalyst","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""},{"entity":{"id":"58b974f1-d389-5bf6-81cd-889c44442c42","slug":"atp","display_name":"ATP","entity_type_key":"small_molecule"},"role":"input","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""},{"entity":{"id":"136c3764-1b93-5f79-8673-9001cab9bc3d","slug":"adp","display_name":"Adenosine diphosphate","entity_type_key":"small_molecule"},"role":"output","stoichiometry":null,"state_label":"","sequence_order":4,"notes":""}]},"contexts":[{"dimension":"evidence_access","value_text":"Primary full-text HTML and indexed abstract reviewed for the stated results; archived locally.\nPrimary publisher article introductory text reviewed; precise affinity estimates are contextual, not newly remeasured.","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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The Erwinia chrysanthemi enzyme study identifies magnesium dependence and a Mg–ADP structural complex; this is a microbial enzyme requirement, not a demonstrated human magnesium-deficiency phenotype. E. coli has AroK and AroL kinase isoenzymes with different substrate affinities. The AroK structural paper discusses approximate shikimate Km values of 20 mM versus 0.2 mM for the two systems; these are organism/assay properties, not plasma targets. Loss of both kinases produces aromatic-amino-acid auxotrophy; environmental nutrient rescue and isoenzyme compensation matter. [Biochemical and X-ray crystallographic studies on shikimate kinase: the important structural role of the P-loop lysine.](https://pubmed.ncbi.nlm.nih.gov/11369852/) [Crystal structure of the Escherichia coli shikimate kinase I (AroK) that confers sensitivity to mecillinam.](https://pubmed.ncbi.nlm.nih.gov/12001235/)","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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