1.13.11.66: hydroquinone 1,2-dioxygenase

This is an abbreviated version!
For detailed information about hydroquinone 1,2-dioxygenase, go to the full flat file.

Reaction

Synonyms

HQDO, hydroquinone 1,2-dioxygenase, hydroquinone dioxygenase, LinE, mnpC, PcpA, PdcDE, PnpC1, PnpC2, PnpCD, ring-cleavage hydroquinone 1,2-dioxygenase, two-subunit hydroquinone 1,2-dioxygenase, type II HQDO, YaiA

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

                1.13.11.66 hydroquinone 1,2-dioxygenase

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Results	in table
1	Activating Compound
35	AA Sequence
7	Cloned(Commentary)
3	Crystallization (Commentary)
2	Expression
7	General Information
1	General Stability
27	Inhibitors
10	kcat/KM [mM/s]
1	Ki Value [mM]
17	KM Value [mM]
15	Metals/Ions
12	Molecular Weight [Da]
10	Natural Substrates/ Products (Substrates)
66	Organism
5	Pathway
7	pH Optimum
4	pH Range
2	pH Stability
19	Protein Variants
6	Purification (Commentary)
3	Reaction
25	Reference
5	Specific Activity [micromol/min/mg]
3	Storage Stability
75	Substrates and Products (Substrate)
20	Subunits
27	Synonyms
1	Systematic Name
4	Temperature Optimum [°C]
1	Temperature Range [°C]
1	Temperature Stability [°C]
12	Turnover Number [1/s]

Crystallization

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Crystallization on EC 1.13.11.66 - hydroquinone 1,2-dioxygenase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

purified full-length or proteolytically truncated PnpCD in apo form and in complex with Fe3+ or substrate analogue hydroxybenzonitrile and Cd2+, i.e. apo-PnpCD, PnpCD-Fe3+, and PnpCD-Cd2+-HBN, sitting-drop vapor diffusion method, 15-20 mg/ml protein in 10mM Tris-HCl, pH 8.0, and 100 mM NaCl, is mixed with reservoir solution containing 0.2 M sodium thiocyanate, 20% w/v PEG 3350, 20°C, method optimization, X-ray diffraction structure determination and analysis

Pseudomonas sp.

C1I210; C1I209

745331

generation of a homology model, based on zinc protein PDB entry 1ZSW, which predicts that the tertiary structure of the enzyme differs significantly from that of the extradiol dioxygenases, and that the residues ligating the Fe(II) are H11, H227, and E276

Sphingobium chlorophenolicum

Q9ZBB0

720066

purified enzyme free or in complex with substrate methylhydroquinone under anaerobic conditions, or with inhibitors 4-hydroxybenzoate and 4-nitrophenol, sitting drop vapor diffusion method, mixing of 0.001 ml of 8 mg/ml protein in 25 mM Tris, pH 7.0, 5 mM NaCl, and 0.5 mM ligand, with 0.001 ml of reservoir solution containing 14% PEG 3350, 0.35 M MgCl2, and 0.1 M MES, pH 6.5, 4°C, 1 day, the structure of the free enzyme is obtained by soaking the crystals in a stabilizing solution containing 16% PEG 3350, 0.35 M MgCl2, and 0.1 M MES, pH 6.5, for two days, changing the solution three times, in order to remove the ligands, X-ray diffraction structure determination and analysis at 1.90-2.40 resolution, molecular replacement using the coordinates of PnpCD structure from Pseudomonas sp. strain WBC-3, PDB ID 4ZXA as template, modeling

Sphingomonas sp.

F8TW82; F8TW83

744430