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Literature summary extracted from

  • Steiner, R.A.; Janssen, H.J.; Roversi, P.; Oakley, A.J.; Fetzner, S.
    Structural basis for cofactor-independent dioxygenation of N-heteroaromatic compounds at the alpha/beta-hydrolase fold (2010), Proc. Natl. Acad. Sci. USA, 107, 657-662.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

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

Protein Variants

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

KM Value [mM]

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

Natural Substrates/ Products (Substrates)

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
-
?

Organism

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
-
-

Substrates and Products (Substrate)

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 ?
-
?

Subunits

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

Synonyms

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

Turnover Number [1/s]

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

General Information

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