1.13.11.47	1H-3-Hydroxy-4-oxoquinaldine + O2	-	Arthrobacter sp.	N-Acetylanthranilate + CO	-	?	139494	
1.13.11.47	1H-3-Hydroxy-4-oxoquinaldine + O2	-	Arthrobacter sp. Ru61a	N-Acetylanthranilate + CO	-	?	139494	
1.13.11.47	1H-3-hydroxy-4-oxoquinaldine + O2	-	Paenarthrobacter nitroguajacolicus	N-acetylanthranilic acid + CO	-	?	186663	
1.13.11.47	1H-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	-	?	186663	
1.13.11.47	1H-3-hydroxy-4-oxoquinaldine + O2	-	Paenarthrobacter nitroguajacolicus Rü61a	N-acetylanthranilic acid + CO	-	?	186663	
1.13.11.47	1H-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	-	?	186663	
1.13.11.47	1H-3-Hydroxy-4-oxoquinoline + O2	-	Pseudomonas putida	N-Formylanthranilate + CO	-	?	139493	
1.13.11.47	1H-3-Hydroxy-4-oxoquinoline + O2	at 20% of the activity with 1H-3-Hydroxy-4-oxoquinaldine	Arthrobacter sp.	N-Formylanthranilate + CO	-	?	139493	
1.13.11.47	1H-3-Hydroxy-4-oxoquinoline + O2	-	Pseudomonas putida 33/1	N-Formylanthranilate + CO	-	?	139493	
1.13.11.47	1H-3-Hydroxy-4-oxoquinoline + O2	at 20% of the activity with 1H-3-Hydroxy-4-oxoquinaldine	Arthrobacter sp. Ru61a	N-Formylanthranilate + CO	-	?	139493	
1.13.11.47	1H-3-hydroxy-4-oxoquinoline + O2	-	Pseudomonas putida	N-formylanthranilic acid + CO	-	?	186664	
1.13.11.47	1H-3-hydroxy-4-oxoquinoline + O2	QDO 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	Pseudomonas putida	N-formylanthranilic acid + CO	-	?	186664	
1.13.11.47	1H-3-hydroxy-4-oxoquinoline + O2	-	Pseudomonas putida 33/1	N-formylanthranilic acid + CO	-	?	186664	
1.13.11.47	1H-3-hydroxy-4-oxoquinoline + O2	QDO 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	Pseudomonas putida 33/1	N-formylanthranilic acid + CO	-	?	186664	
1.13.11.47	additional information	active site cavity and its access, and N-heteroaromatic substrate binding and kinetics, HOD follows a compulsory-order ternary-complex mechanism in which the N-heteroaromatic organic substrate binds to the enzyme prior to dioxygen attack, overview	Paenarthrobacter nitroguajacolicus	?	-	?	89	
1.13.11.47	additional information	N-heteroaromatic substrate binding and kinetics	Pseudomonas putida	?	-	?	89	
1.13.11.47	additional information	substrate deprotonation under transient-state conditions is not rate-limiting and shows a pKa value of 7.2 for wild-type. A large solvent isotope effect is found, and the pKa value is shifted to 8.3 in D2O	Paenarthrobacter nitroguajacolicus	?	-	?	89	
1.13.11.47	additional information	N-heteroaromatic substrate binding and kinetics	Pseudomonas putida 33/1	?	-	?	89	
1.13.11.47	additional information	active site cavity and its access, and N-heteroaromatic substrate binding and kinetics, HOD follows a compulsory-order ternary-complex mechanism in which the N-heteroaromatic organic substrate binds to the enzyme prior to dioxygen attack, overview	Paenarthrobacter nitroguajacolicus Rü61a	?	-	?	89