1.13.11.47: 3-hydroxy-4-oxoquinoline 2,4-dioxygenase

This is an abbreviated version!
For detailed information about 3-hydroxy-4-oxoquinoline 2,4-dioxygenase, go to the full flat file.

Reaction

Synonyms

(1H)-3-Hydroxy-4-oxoquinoline 2,4-dioxygenase, 1-H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase, 1H-3-Hydroxy-4-oxo-quinoline oxygenase, 1H-3-Hydroxy-4-oxoquinaldine 2,4-dioxygenase, 1H-3-Hydroxy-4-oxoquinoline 2,4-dioxygenase, 1H-3-Hydroxy-4-oxoquinoline oxygenase, 3,4-dihydroxyquinoline 2,4-dioxygenase, 3-Hydroxy-4(1H)-one, 2,4-dioxygenase, 3-Hydroxy-4-oxo-1,4-dihydroquinoline 2,4-dioxygenase, EC 1.12.99.5, EC 1.13.99.5, HOD, MeQDO, More, Oxygenase, 1H-3-hydroxy-4-oxoquinoline 2,4-di, QDO, Quinoline-3,4-diol 2,4-dioxygenase, quinoline-3,4-diol 2,4-dioxygenase (carbon monoxide-forming)

ECTree

     1 Oxidoreductases

         1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)

             1.13.11 With incorporation of two atoms of oxygen

                1.13.11.47 3-hydroxy-4-oxoquinoline 2,4-dioxygenase

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Results	in table
7	AA Sequence
1	CAS Registry Number
1	Cloned(Commentary)
2	Cofactor
5	Crystallization (Commentary)
4	General Information
28	Inhibitors
6	kcat/KM [mM/s]
17	KM Value [mM]
6	Metals/Ions
3	Molecular Weight [Da]
4	Natural Substrates/ Products (Substrates)
21	Organism
1	PDB ID
3	pH Optimum
15	Protein Variants
4	Purification (Commentary)
1	Reaction
2	Reaction Type
14	Reference
2	Source Tissue
3	Specific Activity [micromol/min/mg]
2	Storage Stability
22	Substrates and Products (Substrate)
9	Subunits
30	Synonyms
1	Systematic Name
2	Temperature Optimum [°C]
1	Temperature Stability [°C]
14	Turnover Number [1/s]

Crystallization

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Crystallization on EC 1.13.11.47 - 3-hydroxy-4-oxoquinoline 2,4-dioxygenase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

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

O31266

713426

mutations H251A and D126A have a minor effect on substrate positioning. Both His-251 and Asp-126 are essential for the proton transfer driving force of the initial reaction

Paenarthrobacter nitroguajacolicus

O31266

742869

random-acceleration molecular dynamics study. Gates for expulsion of O2 from the protein, which can also be taken as gates for O2 uptake, are found throughout almost the whole external surface of the protein, alongside a variety of binding pockets for O2 . The most exploited gates and binding pockets do not correspond to the single gate and binding pocket proposed from the examination of the static model from X-ray diffraction analysis

Paenarthrobacter nitroguajacolicus

O31266

742251

crystallized by the vapour-diffusion method, giving hexagonal bipyramid crystals belonging to space group P6122. Selenomethionine-containing native QDO is prepared and crystallized under identical conditions

Pseudomonas putida

-

684174

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

O33472

713426