3.6.1.17: bis(5'-nucleosyl)-tetraphosphatase (asymmetrical)

This is an abbreviated version!
For detailed information about bis(5'-nucleosyl)-tetraphosphatase (asymmetrical), go to the full flat file.

Reaction

Synonyms

(asymmetrical) diadenosine 5',5''�-P1,P4-tetraphosphate hydrolase, (asymmetrical) dinucleoside tetraphosphatase, Ap4A hydrolase, Ap4A-hydrolase, AP4AASE, Apf, asym-di-GDPase, asymmetric Ap4A hydrolase, asymmetric diadenosine tetraphosphate hydrolase, asymmetrical Ap4A hydrolase, asymmetrical bis-(5'-nucleosidyl)-tetraphosphatase, asymmetrical diadenosine tetraphosphate hydrolase, AtNUDX25 protein, ATP-producing Ap4A hydrolase, bis(5'-adenosyl)-tetraphosphatase, bis(5'-guanosyl)-tetraphosphatase, bis(5'-nucleosyl)-tetraphosphatase (asymmetrical), bis(5-guanosyl)tetraphosphatase, CT771, Diadenosine 5',5'''-P1,P4-tetraphosphate asymmetrical hydrolase, diadenosine 5',5'''-P1,P4-tetraphosphate pyrophosphohydrolase, diadenosine 5',5'-P1P4 tetraphosphate hydrolase, diadenosine 5,5-P1,P4-tetraphosphate hydrolase, diadenosine P1,P4-tetraphosphatase, Diadenosine tetraphosphatase, diadenosine tetraphosphate pyrophosphohydrolase, diguanosine tetraphosphatase, diguanosinetetraphosphatase (asymmetrical), diguanosinetetraphosphate guanosylhydrolase, dinucleoside tetraphosphatase, dinucleosidetetraphosphatase (asymmetrical), DIPP1, ENPP4, More, MXAN_1509, NDX-4, nudH, Nudix hydrolase, NUDT2, PFE1035c, PrpA

ECTree

     3 Hydrolases

         3.6 Acting on acid anhydrides

             3.6.1 In phosphorus-containing anhydrides

                3.6.1.17 bis(5'-nucleosyl)-tetraphosphatase (asymmetrical)

Advanced search results

Do not include text mining results

Include results (more...)

Include results (more...)

Results	in table
5	Activating Compound
2233	AA Sequence
1	CAS Registry Number
11	Cloned(Commentary)
5	Crystallization (Commentary)
51	Disease/ Diagnostics
6	General Information
1	IC50 Value
108	Inhibitors
16	kcat/KM [mM/s]
37	Ki Value [mM]
74	KM Value [mM]
9	Localization
52	Metals/Ions
23	Molecular Weight [Da]
42	Natural Substrates/ Products (Substrates)
52	Organism
3	Pathway
21	PDB ID
15	pH Optimum
6	pH Range
3	pH Stability
1	pI Value
28	Protein Variants
25	Purification (Commentary)
1	Reaction
3	Reaction Type
52	Reference
22	Source Tissue
21	Specific Activity [micromol/min/mg]
2	Storage Stability
124	Substrates and Products (Substrate)
3	Subunits
55	Synonyms
1	Systematic Name
5	Temperature Optimum [°C]
1	Temperature Range [°C]
6	Temperature Stability [°C]
50	Turnover Number [1/s]

Crystallization

print visible entries

print all entries

Go back to the abbreviated version
of the Enzyme Summary Page.

Crystallization on EC 3.6.1.17 - bis(5'-nucleosyl)-tetraphosphatase (asymmetrical)

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.

top print hide Go to Crystallization (commentary) Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

free and ATP-bound enzyme, hanging drop vapor diffusion method, using 0.1 M Tris-HCl pH 7.6, 29% (w/v) PEG 3350, and 0.75 M NaCl (free enzyme) or 1 ml 0.1 M Tris-HCl pH 8.8, 25% (w/v) PEG 3350, and 0.2 M NaCl (ATP-bound enzyme)

Aquifex aeolicus

O66548

710715

sitting-drop vapour diffusion, crystals diffract to a minimum d-spacing of 2 A and belong to either space group C222 or C222(1)

Caenorhabditis elegans

-

654817

structures of both apo- and ligand-bound CT771, to 2.6 A and 1.9 A resolution, respectively. The structure shows a alphabetaalpha-sandwich motif with many conserved elements lining the putative Nudix active site

Chlamydia trachomatis

-

733346

structure determined by NMR spectroscopy

Homo sapiens

P50583

669427

structure of wild-type and E58A mutant human Ap4A hydrolase, to 2.7 and 2.1 A resolution, respectively. Similar to the canonical Nudix fold, human Ap4A hydrolase shows the common alphabetaalpha-sandwich architecture. Two sulfate ions and one diphosphate coordinated with some conserved residues are observed in the active cleft

Homo sapiens

P50583

733257