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Literature summary for 1.13.11.47 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)

Crystallization (Comment) Organism
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
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

Protein Variants Comment Organism
C69S/H251A inactive mutant Paenarthrobacter nitroguajacolicus
D120A site-directed mutagenesism the mutant shows altered kinetics and reduced catalytic efficiency compared to the wild-type enzyme Pseudomonas putida
D126A site-directed mutagenesis, the mutant shows altered kinetics and reduced catalytic efficiency compared to the wild-type enzyme Paenarthrobacter nitroguajacolicus
H102L site-directed mutagenesis, the mutant shows altered kinetics and reduced catalytic efficiency compared to the wild-type enzyme Paenarthrobacter nitroguajacolicus
H251A site-directed mutagenesis, the mutant shows altered kinetics and reduced catalytic efficiency compared to the wild-type enzyme Paenarthrobacter nitroguajacolicus
H38A site-directed mutagenesis, the mutant shows altered kinetics and reduced catalytic efficiency compared to the wild-type enzyme Paenarthrobacter nitroguajacolicus
S101A site-directed mutagenesis, the mutant shows altered kinetics and reduced catalytic efficiency compared to the wild-type enzyme Paenarthrobacter nitroguajacolicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0027
-
1H-3-Hydroxy-4-oxoquinaldine wild-type HOD, pH not specified in the publication, temperature not specified in the publication Paenarthrobacter nitroguajacolicus
0.0104
-
1H-3-Hydroxy-4-oxoquinoline wild-type QDO, pH not specified in the publication, temperature not specified in the publication Pseudomonas putida
0.0233
-
1H-3-Hydroxy-4-oxoquinaldine HOD mutant H102L, pH not specified in the publication, temperature not specified in the publication Paenarthrobacter nitroguajacolicus
0.0272
-
1H-3-Hydroxy-4-oxoquinaldine HOD mutant D126A, pH not specified in the publication, temperature not specified in the publication Paenarthrobacter nitroguajacolicus
0.059
-
1H-3-Hydroxy-4-oxoquinaldine HOD mutant H251A, pH not specified in the publication, temperature not specified in the publication Paenarthrobacter nitroguajacolicus
0.1595
-
1H-3-Hydroxy-4-oxoquinaldine HOD mutant H38A, pH not specified in the publication, temperature not specified in the publication Paenarthrobacter nitroguajacolicus
0.162
-
1H-3-Hydroxy-4-oxoquinaldine HOD mutant S101A, pH not specified in the publication, temperature not specified in the publication Paenarthrobacter nitroguajacolicus
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)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1H-3-hydroxy-4-oxoquinaldine + O2 Paenarthrobacter nitroguajacolicus
-
N-acetylanthranilic acid + CO
-
?
1H-3-hydroxy-4-oxoquinaldine + O2 Paenarthrobacter nitroguajacolicus Rü61a
-
N-acetylanthranilic acid + CO
-
?
1H-3-hydroxy-4-oxoquinoline + O2 Pseudomonas putida
-
N-formylanthranilic acid + CO
-
?
1H-3-hydroxy-4-oxoquinoline + O2 Pseudomonas putida 33/1
-
N-formylanthranilic acid + CO
-
?

Organism

Organism UniProt Comment Textmining
Paenarthrobacter nitroguajacolicus O31266
-
-
Paenarthrobacter nitroguajacolicus Rü61a O31266
-
-
Pseudomonas putida O33472
-
-
Pseudomonas putida 33/1 O33472
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1H-3-hydroxy-4-oxoquinaldine + O2
-
Paenarthrobacter nitroguajacolicus N-acetylanthranilic acid + CO
-
?
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
-
?
1H-3-hydroxy-4-oxoquinaldine + O2
-
Paenarthrobacter nitroguajacolicus Rü61a N-acetylanthranilic acid + CO
-
?
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
-
?
1H-3-hydroxy-4-oxoquinoline + O2
-
Pseudomonas putida N-formylanthranilic acid + CO
-
?
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
-
?
1H-3-hydroxy-4-oxoquinoline + O2
-
Pseudomonas putida 33/1 N-formylanthranilic acid + CO
-
?
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
-
?
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 ?
-
?
additional information N-heteroaromatic substrate binding and kinetics Pseudomonas putida ?
-
?
additional information N-heteroaromatic substrate binding and kinetics Pseudomonas putida 33/1 ?
-
?
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

Subunits Comment Organism
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
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

Synonyms Comment Organism
1-H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase
-
Pseudomonas putida
HOD
-
Paenarthrobacter nitroguajacolicus
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
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
QDO
-
Pseudomonas putida

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0034
-
1H-3-Hydroxy-4-oxoquinaldine HOD mutant H251A, pH not specified in the publication, temperature not specified in the publication Paenarthrobacter nitroguajacolicus
0.027
-
1H-3-Hydroxy-4-oxoquinaldine HOD mutant H102L, pH not specified in the publication, temperature not specified in the publication Paenarthrobacter nitroguajacolicus
1.05
-
1H-3-Hydroxy-4-oxoquinaldine HOD mutant D126A, pH not specified in the publication, temperature not specified in the publication Paenarthrobacter nitroguajacolicus
2.55
-
1H-3-Hydroxy-4-oxoquinoline QDO mutant D120A, pH not specified in the publication, temperature not specified in the publication Pseudomonas putida
3
-
1H-3-Hydroxy-4-oxoquinaldine HOD mutant H38A, pH not specified in the publication, temperature not specified in the publication Paenarthrobacter nitroguajacolicus
20.6
-
1H-3-Hydroxy-4-oxoquinoline wild-type QDO, pH not specified in the publication, temperature not specified in the publication Pseudomonas putida
38.4
-
1H-3-Hydroxy-4-oxoquinaldine wild-type HOD, pH not specified in the publication, temperature not specified in the publication Paenarthrobacter nitroguajacolicus
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

General Information Comment Organism
physiological function the cofactor-independent dioxygenase is involved in the breakdown of N-heteroaromatic compounds Pseudomonas putida
physiological function the cofactor-independent dioxygenase is involved in the breakdown of N-heteroaromatic compounds Paenarthrobacter nitroguajacolicus