1.13.11.37: hydroxyquinol 1,2-dioxygenase

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

Reaction

Synonyms

1,2-HQD, Ar 1,2-HQD, cphA-1, cphA-2, cphA-I, HQD, hydroxyquinol 1,2-dioxygenase, hydroxyquinon dioxygenase, More, NpcC, oxygenase, hydroxyquinol 1,2-di-, oxygenase, hydroxyquinol di-, PdcC, PnpC, PnpG

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

                1.13.11.37 hydroxyquinol 1,2-dioxygenase

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Results	in table
2	Activating Compound
395	AA Sequence
4	Application
1	CAS Registry Number
10	Cloned(Commentary)
3	Crystallization (Commentary)
7	General Information
30	Inhibitors
25	Ki Value [mM]
6	KM Value [mM]
1	Localization
7	Metals/Ions
16	Molecular Weight [Da]
25	Natural Substrates/ Products (Substrates)
52	Organism
12	Pathway
3	PDB ID
7	pH Optimum
2	pH Range
1	Protein Variants
9	Purification (Commentary)
1	Reaction
3	Reaction Type
40	Reference
10	Source Tissue
21	Specific Activity [micromol/min/mg]
4	Storage Stability
75	Substrates and Products (Substrate)
18	Subunits
30	Synonyms
1	Systematic Name
4	Temperature Optimum [°C]
1	Temperature Range [°C]
2	Temperature Stability [°C]
4	Turnover Number [1/s]

Crystallization

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Crystallization on EC 1.13.11.37 - hydroxyquinol 1,2-dioxygenase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

sitting drop vapor difffusion from a solution containing 2 M ammonium sulfate, 4% polyethylene glycol 400, 100 mM Hepes, pH 7.5, drops consist of 0.004 ml of 20 mg/ml protein solution and 0.006 ml reservoir solution equilibrated against 0.05 ml of reservoir solution, crystals diffract to 1.75 A

Pimelobacter simplex

Q5PXQ6

659477

unit-cell dimensions: a = 81.15, b = 86.79, c = 114.93

Pimelobacter simplex

-

439431

structure at 2.1 A resolution. The catalytic Fe(III) is pentacoordinated by the conserved Tyr160, Tyr194, His218 and His220 residues, the citrate anion and one water molecule. Asp80, Thr81 and Val248 are responsible for the substrate specificity. The N-terminal domain is required for its soluble expression and enzyme catalysis

Pseudomonas putida

C6FI44

764071