EC Number | Crystallization (Comment) | Organism |
---|---|---|
1.13.11.47 | HOD mutant C69S/H251A in complex with its natural 1-H-3-hydroxy-4-oxoquinaldine substrate, its N-acetylanthranilate reaction product, and chloride as dioxygen mimic, X-ray diffraction structure determination and analysis at 2.1 A resolution | Paenarthrobacter nitroguajacolicus |
1.13.11.47 | QDO in complex with its natural 1-H-3-hydroxy-4-oxoquinoline substrate, its N-formylanthranilate reaction product, and chloride as dioxygen mimic, X-ray diffraction structure determination and analysis at 2.6 A resolution | Pseudomonas putida |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.13.11.47 | C69S/H251A | inactive mutant | Paenarthrobacter nitroguajacolicus |
1.13.11.47 | D120A | site-directed mutagenesism the mutant shows altered kinetics and reduced catalytic efficiency compared to the wild-type enzyme | Pseudomonas putida |
1.13.11.47 | D126A | site-directed mutagenesis, the mutant shows altered kinetics and reduced catalytic efficiency compared to the wild-type enzyme | Paenarthrobacter nitroguajacolicus |
1.13.11.47 | H102L | site-directed mutagenesis, the mutant shows altered kinetics and reduced catalytic efficiency compared to the wild-type enzyme | Paenarthrobacter nitroguajacolicus |
1.13.11.47 | H251A | site-directed mutagenesis, the mutant shows altered kinetics and reduced catalytic efficiency compared to the wild-type enzyme | Paenarthrobacter nitroguajacolicus |
1.13.11.47 | H38A | site-directed mutagenesis, the mutant shows altered kinetics and reduced catalytic efficiency compared to the wild-type enzyme | Paenarthrobacter nitroguajacolicus |
1.13.11.47 | S101A | site-directed mutagenesis, the mutant shows altered kinetics and reduced catalytic efficiency compared to the wild-type enzyme | Paenarthrobacter nitroguajacolicus |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.13.11.47 | 0.0027 | - |
1H-3-Hydroxy-4-oxoquinaldine | wild-type HOD, pH not specified in the publication, temperature not specified in the publication | Paenarthrobacter nitroguajacolicus | |
1.13.11.47 | 0.0104 | - |
1H-3-Hydroxy-4-oxoquinoline | wild-type QDO, pH not specified in the publication, temperature not specified in the publication | Pseudomonas putida | |
1.13.11.47 | 0.0233 | - |
1H-3-Hydroxy-4-oxoquinaldine | HOD mutant H102L, pH not specified in the publication, temperature not specified in the publication | Paenarthrobacter nitroguajacolicus | |
1.13.11.47 | 0.0272 | - |
1H-3-Hydroxy-4-oxoquinaldine | HOD mutant D126A, pH not specified in the publication, temperature not specified in the publication | Paenarthrobacter nitroguajacolicus | |
1.13.11.47 | 0.059 | - |
1H-3-Hydroxy-4-oxoquinaldine | HOD mutant H251A, pH not specified in the publication, temperature not specified in the publication | Paenarthrobacter nitroguajacolicus | |
1.13.11.47 | 0.1595 | - |
1H-3-Hydroxy-4-oxoquinaldine | HOD mutant H38A, pH not specified in the publication, temperature not specified in the publication | Paenarthrobacter nitroguajacolicus | |
1.13.11.47 | 0.162 | - |
1H-3-Hydroxy-4-oxoquinaldine | HOD mutant S101A, pH not specified in the publication, temperature not specified in the publication | Paenarthrobacter nitroguajacolicus | |
1.13.11.47 | 0.1809 | - |
1H-3-Hydroxy-4-oxoquinoline | QDO mutant D120A, pH not specified in the publication, temperature not specified in the publication | Pseudomonas putida |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.13.11.47 | 1H-3-hydroxy-4-oxoquinaldine + O2 | Paenarthrobacter nitroguajacolicus | - |
N-acetylanthranilic acid + CO | - |
? | |
1.13.11.47 | 1H-3-hydroxy-4-oxoquinaldine + O2 | Paenarthrobacter nitroguajacolicus Rü61a | - |
N-acetylanthranilic acid + CO | - |
? | |
1.13.11.47 | 1H-3-hydroxy-4-oxoquinoline + O2 | Pseudomonas putida | - |
N-formylanthranilic acid + CO | - |
? | |
1.13.11.47 | 1H-3-hydroxy-4-oxoquinoline + O2 | Pseudomonas putida 33/1 | - |
N-formylanthranilic acid + CO | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.13.11.47 | Paenarthrobacter nitroguajacolicus | O31266 | - |
- |
1.13.11.47 | Paenarthrobacter nitroguajacolicus Rü61a | O31266 | - |
- |
1.13.11.47 | Pseudomonas putida | O33472 | - |
- |
1.13.11.47 | Pseudomonas putida 33/1 | O33472 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.13.11.47 | 1H-3-hydroxy-4-oxoquinaldine + O2 | - |
Paenarthrobacter nitroguajacolicus | N-acetylanthranilic acid + CO | - |
? | |
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 | - |
? | |
1.13.11.47 | 1H-3-hydroxy-4-oxoquinaldine + O2 | - |
Paenarthrobacter nitroguajacolicus Rü61a | N-acetylanthranilic acid + CO | - |
? | |
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 | - |
? | |
1.13.11.47 | 1H-3-hydroxy-4-oxoquinoline + O2 | - |
Pseudomonas putida | N-formylanthranilic acid + CO | - |
? | |
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 | - |
? | |
1.13.11.47 | 1H-3-hydroxy-4-oxoquinoline + O2 | - |
Pseudomonas putida 33/1 | N-formylanthranilic acid + CO | - |
? | |
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 | - |
? | |
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 | ? | - |
? | |
1.13.11.47 | additional information | N-heteroaromatic substrate binding and kinetics | Pseudomonas putida | ? | - |
? | |
1.13.11.47 | additional information | N-heteroaromatic substrate binding and kinetics | Pseudomonas putida 33/1 | ? | - |
? | |
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 | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.13.11.47 | More | the enzyme shows an alpha/beta forld, residues Ser101/His251/Asp126 in HOD located at the interface between the core domain and the cap domain, correspond to the nucleophile/histidine/acidic residue triad required for activity by members of the alpha/beta-hydrolase fold superfamily | Paenarthrobacter nitroguajacolicus |
1.13.11.47 | More | the enzyme shows an alpha/beta forld, residues Ser95/His244/Asp120 in QDO located at the interface between the core domain and the cap domain, correspond to the nucleophile/histidine/acidic residue triad required for activity by members of the alpha/beta-hydrolase fold superfamily | Pseudomonas putida |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.13.11.47 | 1-H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase | - |
Pseudomonas putida |
1.13.11.47 | HOD | - |
Paenarthrobacter nitroguajacolicus |
1.13.11.47 | More | the dioxygenase belongs to the alpha/beta-hydrolase fold superfamily. Members of this family typically catalyze hydrolytic processes rather than oxygenation reactions, but the enzyme's crystal structure shows a typical alpha/beta fold | Pseudomonas putida |
1.13.11.47 | More | the dioxygenase belongs to the alpha/beta-hydrolase fold superfamily. Members of this family typically catalyze hydrolytic processes rather than oxygenation reactions, but the enzyme's crystal structure shows a typical alpha/beta fold | Paenarthrobacter nitroguajacolicus |
1.13.11.47 | QDO | - |
Pseudomonas putida |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.13.11.47 | 0.0034 | - |
1H-3-Hydroxy-4-oxoquinaldine | HOD mutant H251A, pH not specified in the publication, temperature not specified in the publication | Paenarthrobacter nitroguajacolicus | |
1.13.11.47 | 0.027 | - |
1H-3-Hydroxy-4-oxoquinaldine | HOD mutant H102L, pH not specified in the publication, temperature not specified in the publication | Paenarthrobacter nitroguajacolicus | |
1.13.11.47 | 1.05 | - |
1H-3-Hydroxy-4-oxoquinaldine | HOD mutant D126A, pH not specified in the publication, temperature not specified in the publication | Paenarthrobacter nitroguajacolicus | |
1.13.11.47 | 2.55 | - |
1H-3-Hydroxy-4-oxoquinoline | QDO mutant D120A, pH not specified in the publication, temperature not specified in the publication | Pseudomonas putida | |
1.13.11.47 | 3 | - |
1H-3-Hydroxy-4-oxoquinaldine | HOD mutant H38A, pH not specified in the publication, temperature not specified in the publication | Paenarthrobacter nitroguajacolicus | |
1.13.11.47 | 20.6 | - |
1H-3-Hydroxy-4-oxoquinoline | wild-type QDO, pH not specified in the publication, temperature not specified in the publication | Pseudomonas putida | |
1.13.11.47 | 38.4 | - |
1H-3-Hydroxy-4-oxoquinaldine | wild-type HOD, pH not specified in the publication, temperature not specified in the publication | Paenarthrobacter nitroguajacolicus | |
1.13.11.47 | 46.4 | - |
1H-3-Hydroxy-4-oxoquinaldine | HOD mutant S101A, pH not specified in the publication, temperature not specified in the publication | Paenarthrobacter nitroguajacolicus |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.13.11.47 | physiological function | the cofactor-independent dioxygenase is involved in the breakdown of N-heteroaromatic compounds | Pseudomonas putida |
1.13.11.47 | physiological function | the cofactor-independent dioxygenase is involved in the breakdown of N-heteroaromatic compounds | Paenarthrobacter nitroguajacolicus |