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Literature summary extracted from

  • Qian, L.; Liu, X.
    Purification, characterization and structure of nucleoside diphosphate kinase from Drosophila melanogaster (2014), Protein Expr. Purif., 103, 48-55.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.4.6 gene awd, DNA and amino acid sequence determinatioon and analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha Drosophila melanogaster

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.4.6 purified recombinant His-tagged wild-type and selenomethionine-labeled enzymes, sitting drop vapor diffusion method, mixing of 0.001 ml of 10 mg/ml protein in 50 mM Tris, 500 mM NaCl, pH 8.0, with 0.001 ml of precipitatant solution, followed by equilibration aganst 0.1 ml reservoir solution containing 60% v/v Tacsimate, pH 7.0, 20°C, X-ray diffraction structure determination and analysis at 1.39-1.94 A resolution Drosophila melanogaster

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.4.6 60000
-
 recombinant wild-type enzyme, gel filtration Drosophila melanogaster
2.7.4.6 63500
-
 recombinant wild-type enzyme, analytical ultracentrifugation Drosophila melanogaster

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.4.6 ATP + ADP Drosophila melanogaster
-
 ADP + ATP
-
 r
2.7.4.6 ATP + GDP Drosophila melanogaster
-
 ADP + GTP
-
 r

Organism

EC Number Organism UniProt Comment Textmining
2.7.4.6 Drosophila melanogaster P08879 gene awd
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.4.6 recombinant His-tagged wild-type and selenomethionine-labeled enzymes to homogeneity from Escherichia coli by nickel affinity chromatography, cation exchange chromatography, and gel filtration Drosophila melanogaster

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.4.6 Schneider 2 cell S2 cell Drosophila melanogaster
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.4.6 ATP + ADP
-
 Drosophila melanogaster ADP + ATP
-
 r
2.7.4.6 ATP + GDP
-
 Drosophila melanogaster ADP + GTP
-
 r
2.7.4.6 additional information binding affinity of NDPs with the recombinant enzyme measured by isothermal titration calorimetry, indicate that the purines nucleotides show higher binding affinity compared with pyrimidines. The recombinant enzyme rNDPK has a definite nuclease activity in vitro, which cleaves supercoiled plasmid DNA, but has no effect on dsDNA and ssDNA. No or poor activity with CDP and UDP Drosophila melanogaster ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.4.6 More the asymmetric enzyme unit is made of three molecules, each of which consists of a four-stranded anti-parallel beta-sheets and seven alpha-helices, the simulated nucleotide-binding active site is conserved, structure analysis and modelling, overview Drosophila melanogaster
2.7.4.6 trimer gel filtration and analytical ultracentrifugation Drosophila melanogaster

Synonyms

EC Number Synonyms Comment Organism
2.7.4.6 NDPK
-
 Drosophila melanogaster
2.7.4.6 nucleoside diphosphate kinase
-
 Drosophila melanogaster

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.4.6 ATP
-
 Drosophila melanogaster