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Literature summary for 1.13.11.48 extracted from

  • Steiner, R.A.; Frerichs-Deeken, U.; Fetzner, S.
    Crystallization and preliminary X-ray analysis of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase from Arthrobacter nitroguajacolicus Rue61a: a cofactor-devoid dioxygenase of the alpha/beta-hydrolase-fold superfamily (2007), Acta Crystallogr. Sect. F, 63, 382-385.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
overexpression of wild-type and mutant N-terminally His6-tagged HODs in Escherichia coli strain M15 Paenarthrobacter nitroguajacolicus

Crystallization (Commentary)

Crystallization (Comment) Organism
N-terminally His6-tagged HOD is crystallized by the hanging-drop vapour-diffusion method using sodium/potassium tartrate as a precipitant and CuCl2 as an additive. The structure is solved by the single anomalous dispersion technique using data collected to 3.5 A resolution at the Cu absorption peak wavelength. The crystals belong to the primitive tetragonal space group P43212, with unit-cell parameters a = b = 153.788, c = 120.872 A Paenarthrobacter nitroguajacolicus
purified recombinant wild-type and mutants C69S and C69S/H251A N-terminally His6-tagged HOD, hanging drop vapour diffusion method, 50 mg/ml protein in 20 mM Tris-HCl pH 7.5, 100 mM NaCl, 2 mM EDTA, 1 mM DTT, is mixed with 1.65 M sodium/potassium tartrate, 0.1 M HEPES, pH 7.0, and 30 mM CuCl2, method optimization, X-ray diffraction structure determination and analysis at 3.5 A resolution, single anomalous dispersion technique Paenarthrobacter nitroguajacolicus

Protein Variants

Protein Variants Comment Organism
C69S site-directed mutagenesis, the mutant has catalytic properties that are identical to those of wild-type HOD Paenarthrobacter nitroguajacolicus
C69S/H251A site-directed mutagenesis, the mutant is catalytically inactive owing to the Ala substitution of the essential residue His251 Paenarthrobacter nitroguajacolicus

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-Acetylanthranilate + CO
-
?
1H-3-Hydroxy-4-oxoquinaldine + O2 Paenarthrobacter nitroguajacolicus Rü61a
-
N-Acetylanthranilate + CO
-
?
1H-3-Hydroxy-4-oxoquinaldine + O2 Paenarthrobacter nitroguajacolicus Rue61a
-
N-Acetylanthranilate + CO
-
?

Organism

Organism UniProt Comment Textmining
Paenarthrobacter nitroguajacolicus
-
-
-
Paenarthrobacter nitroguajacolicus Rue61a
-
-
-
Paenarthrobacter nitroguajacolicus Rü61a
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant N-terminally His6-tagged HODs from Escherichia coli strain M15 by nickel affinity and anion exchange chromatography Paenarthrobacter nitroguajacolicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1H-3-Hydroxy-4-oxoquinaldine + O2
-
Paenarthrobacter nitroguajacolicus N-Acetylanthranilate + CO
-
?
1H-3-Hydroxy-4-oxoquinaldine + O2
-
Paenarthrobacter nitroguajacolicus Rü61a N-Acetylanthranilate + CO
-
?
1H-3-Hydroxy-4-oxoquinaldine + O2
-
Paenarthrobacter nitroguajacolicus Rue61a N-Acetylanthranilate + CO
-
?

Subunits

Subunits Comment Organism
More three-dimensional structure analysis, overview Paenarthrobacter nitroguajacolicus

Synonyms

Synonyms Comment Organism
1H-3-Hydroxy-4-oxoquinaldine 2,4-dioxygenase
-
Paenarthrobacter nitroguajacolicus
HOD
-
Paenarthrobacter nitroguajacolicus
More HOD belongs to the alpha/beta-hydrolase-fold superfamily of enzymes Paenarthrobacter nitroguajacolicus