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Results 1 - 10 of 19 > >>
EC Number Substrates Commentary Substrates Organism Products Commentary (Products) Reversibility
Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.471H-3-Hydroxy-4-oxoquinaldine + O2 - Arthrobacter sp. N-Acetylanthranilate + CO - ?
Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.471H-3-Hydroxy-4-oxoquinaldine + O2 - Arthrobacter sp. Ru61a N-Acetylanthranilate + CO - ?
Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.471H-3-hydroxy-4-oxoquinaldine + O2 - Paenarthrobacter nitroguajacolicus N-acetylanthranilic acid + CO - ?
Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.471H-3-hydroxy-4-oxoquinaldine + O2 HOD possesses a classical alpha/beta-hydrolase fold core domain additionally equipped with a cap domain. Organic substrates bind in a preorganized active site with an orientation ideally suited for selective deprotonation of their hydroxyl group by a His/Asp charge-relay system affording the generation of electron-donating species. The oxyanion hole of the alpha/beta-hydrolase fold, typically employed to stabilize the tetrahedral intermediate in ester hydrolysis reactions, is utilized here to host and control oxygen chemistry, which is proposed to involve a peroxide anion intermediate. Product release by proton back transfer from the catalytic histidine is driven by minimization of intramolecular charge repulsion. Structural and kinetic data suggest a nonnucleophilic general-base mechanism Paenarthrobacter nitroguajacolicus N-acetylanthranilic acid + CO - ?
Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.471H-3-hydroxy-4-oxoquinaldine + O2 - Paenarthrobacter nitroguajacolicus Rü61a N-acetylanthranilic acid + CO - ?
Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.471H-3-hydroxy-4-oxoquinaldine + O2 HOD possesses a classical alpha/beta-hydrolase fold core domain additionally equipped with a cap domain. Organic substrates bind in a preorganized active site with an orientation ideally suited for selective deprotonation of their hydroxyl group by a His/Asp charge-relay system affording the generation of electron-donating species. The oxyanion hole of the alpha/beta-hydrolase fold, typically employed to stabilize the tetrahedral intermediate in ester hydrolysis reactions, is utilized here to host and control oxygen chemistry, which is proposed to involve a peroxide anion intermediate. Product release by proton back transfer from the catalytic histidine is driven by minimization of intramolecular charge repulsion. Structural and kinetic data suggest a nonnucleophilic general-base mechanism Paenarthrobacter nitroguajacolicus Rü61a N-acetylanthranilic acid + CO - ?
Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.471H-3-Hydroxy-4-oxoquinoline + O2 - Pseudomonas putida N-Formylanthranilate + CO - ?
Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.471H-3-Hydroxy-4-oxoquinoline + O2 at 20% of the activity with 1H-3-Hydroxy-4-oxoquinaldine Arthrobacter sp. N-Formylanthranilate + CO - ?
Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.471H-3-Hydroxy-4-oxoquinoline + O2 - Pseudomonas putida 33/1 N-Formylanthranilate + CO - ?
Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.471H-3-Hydroxy-4-oxoquinoline + O2 at 20% of the activity with 1H-3-Hydroxy-4-oxoquinaldine Arthrobacter sp. Ru61a N-Formylanthranilate + CO - ?
Results 1 - 10 of 19 > >>