3.6.1.67: dihydroneopterin triphosphate diphosphatase

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For detailed information about dihydroneopterin triphosphate diphosphatase, go to the full flat file.

Reaction

Synonyms

At1g68760, At1g68760 protein, AtNUDT1, DHNTP pyrophosphohydrolase, DHNTPase, dihydroneopterin triphosphate pyrophosphatase, dihydroneopterin triphosphate pyrophosphohydrolase, folQ, H2-neopterin-PPP pyrophosphohydrolase, nudB, NUDT1, Orf17 protein, YlgG

ECTree

     3 Hydrolases

         3.6 Acting on acid anhydrides

             3.6.1 In phosphorus-containing anhydrides

                3.6.1.67 dihydroneopterin triphosphate diphosphatase

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Results	in table
1362	AA Sequence
5	Cloned(Commentary)
3	Crystallization (Commentary)
6	General Information
5	Inhibitors
5	kcat/KM [mM/s]
6	KM Value [mM]
9	Metals/Ions
6	Molecular Weight [Da]
6	Natural Substrates/ Products (Substrates)
9	Organism
5	Pathway
17	PDB ID
4	pH Optimum
2	pH Range
5	Purification (Commentary)
1	Reaction
8	Reference
3	Specific Activity [micromol/min/mg]
17	Substrates and Products (Substrate)
3	Subunits
29	Synonyms
1	Systematic Name
4	Temperature Optimum [°C]
3	Temperature Stability [°C]
5	Turnover Number [1/s]

Crystallization

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Crystallization on EC 3.6.1.67 - dihydroneopterin triphosphate diphosphatase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

apoenzyme and enzyme bound to Co2+ and Ni2+, sitting drop vapor diffusion method, using 35% (w/v) PEG 8000, 0.05 M ammonium sulfate in 50 mM Tris pH 7.5, 1 mM EDTA pH 7.4

Escherichia coli

-

758154

crystal structure resolved to 1.8 A resolution

Escherichia coli

P0AFC0

728808

the structure of the enzyme is determined by X-ray diffraction, 1.8 A resolution. The best crystals grow by microseeding in sitting-drop experiments with a 1 ml reservoir solution of 1.3–1.5 M ammonium sulfate, 1% propanol, 3–5 mM DTT, 4 mM sodium diphosphate, 100 mM Na HEPES (pH 6.8). Crystals belong to monoclinic space group C2 with cell dimensions a = 124.1 A, b = 43.2 A, c = 108.0 A, and b = 115.0°

Escherichia coli

P0AFC0

728808