Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.7.4.6 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)

Cloned (Comment) Organism
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)

Crystallization (Comment) Organism
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]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Drosophila melanogaster P08879 gene awd
-

Purification (Commentary)

Purification (Comment) Organism
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

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + ADP
-
Drosophila melanogaster ADP + ATP
-
r
ATP + GDP
-
Drosophila melanogaster ADP + GTP
-
r
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

Subunits Comment Organism
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
trimer gel filtration and analytical ultracentrifugation Drosophila melanogaster

Synonyms

Synonyms Comment Organism
NDPK
-
Drosophila melanogaster
nucleoside diphosphate kinase
-
Drosophila melanogaster

Cofactor

Cofactor Comment Organism Structure
ATP
-
Drosophila melanogaster