1.13.11.9: 2,5-dihydroxypyridine 5,6-dioxygenase

This is an abbreviated version!
For detailed information about 2,5-dihydroxypyridine 5,6-dioxygenase, go to the full flat file.

Reaction

Synonyms

2,5-DHP dioxygenase, 2,5-dihydroxypyridine dioxygenase, 2,5-dihydroxypyridine oxygenase, 2,5DHP dioxygenase, EC 1.13.1.9, NicX, NicX protein, oxygenase, 2,5-dihydroxypyridine 5,6-di-, pyridine-2,5-diol dioxygenase

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

                1.13.11.9 2,5-dihydroxypyridine 5,6-dioxygenase

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Results	in table
3	Activating Compound
278	AA Sequence
2	Application
1	CAS Registry Number
4	Cloned(Commentary)
1	Cofactor
4	Crystallization (Commentary)
3	General Information
7	General Stability
24	Inhibitors
2	KM Value [mM]
2	Localization
10	Metals/Ions
7	Molecular Weight [Da]
16	Natural Substrates/ Products (Substrates)
136	Organism
1	Oxidation Stability
7	Pathway
18	PDB ID
5	pH Optimum
2	Protein Variants
5	Purification (Commentary)
1	Reaction
3	Reaction Type
14	Reference
2	Source Tissue
5	Specific Activity [micromol/min/mg]
5	Storage Stability
28	Substrates and Products (Substrate)
8	Subunits
23	Synonyms
1	Systematic Name
4	Temperature Optimum [°C]
2	Temperature Stability [°C]

Crystallization

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Crystallization on EC 1.13.11.9 - 2,5-dihydroxypyridine 5,6-dioxygenase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

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Pseudomonas putida

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396333, 396334

hanging-drop vapor-diffusion method at 20°C, crystal structure for the resting form of the enzyme (NicX), as well as a complex structure wherein 2,5-hydroxy-pyridine and N-formylmaleamic acid are trapped in different subunits. The resting state structure displays an octahedral coordination for Fe(II) with two histidine residues (His265 and His318), a serine residue (Ser302), a carboxylate ligand (Asp320), and two water molecules. 2,5-Hydroxy-pyridine does not bind as a ligand to Fe(II), yet its interactions with Leu104 and His105 function to guide and stabilize the substrate to the appropriate position to initiate the reaction

Pseudomonas putida

Q88FY1

765451

purified recombinant NicX, hanging drop vapour diffusion method, 0.001 ml of 14 mg/ml protein in 20 mM HEPES pH 7.5, 0.1 M NaCl, and 2 mM DTT, is mixed with 0.001 ml of reservoir solution, containing 22% w/v PEG 4000, 0.1 M sodium acetate and 0.1 M HEPES pH 7.5, 2 mM DTT, and with 1 ml 50 mM EDTA, 18°C, method optimization, X-ray diffraction structure determination and analysis at 2.0 A resolution

Pseudomonas putida

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710759