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Literature summary for 3.6.1.23 extracted from

  • Kovari, J.; Barabas, O.; Takacs, E.; Bekesi, A.; Dubrovay, Z.; Pongracz, V.; Zagyva, I.; Imre, T.; Szabo, P.; Vertessy, B.G.
    Altered active site flexibility and a structural metal-binding site in eukaryotic dUTPase: kinetic characterization, folding, and crystallographic studies of the homotrimeric Drosophila enzyme (2004), J. Biol. Chem., 279, 17932-17944.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in different Escherichia coli strains Drosophila melanogaster

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging and sitting drop vapor diffusion method, stable monomers observed in crystal phase Drosophila melanogaster

Protein Variants

Protein Variants Comment Organism
DELTA160-187 truncated form Drosophila melanogaster

General Stability

General Stability Organism
dUMP protects against tryptic digestion, slight fragmentation caused by frequent freezing and thawing that does not affect the activity Drosophila melanogaster

Inhibitors

Inhibitors Comment Organism Structure
dUDP
-
Drosophila melanogaster
dUMP
-
Drosophila melanogaster

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0004
-
dUTP pH 7.5, 25°C Drosophila melanogaster
0.64
-
dTTP pH 7.5, 25°C Drosophila melanogaster
2.3
-
dCTP pH 7.5, 25°C Drosophila melanogaster

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required, modulates conformation of the enzyme Drosophila melanogaster

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
17200
-
3 * 19800, full length enzyme, 3 * 17200, truncated enzyme, mass spectrometry, gel filtration Drosophila melanogaster
19800
-
3 * 19800, full length enzyme, 3 * 17200, truncated enzyme, mass spectrometry, gel filtration Drosophila melanogaster
54000
-
truncated enzyme, gel filtration Drosophila melanogaster
65000
-
full length enzyme, gel filtration Drosophila melanogaster

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
dUTP + H2O Drosophila melanogaster removes dUTP from the nucleotide triphosphate pool and therefore prevents the incorporation of uracil into the DNA, provides substrate for dTTP synthesis dUMP + diphosphate
-
?

Organism

Organism UniProt Comment Textmining
Drosophila melanogaster
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant protein Drosophila melanogaster

Storage Stability

Storage Stability Organism
-70°C, stable for at least 3 months Drosophila melanogaster

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dCTP + H2O
-
Drosophila melanogaster dCMP + diphosphate
-
?
dTTP + H2O
-
Drosophila melanogaster dTMP + diphosphate
-
?
dUTP + H2O
-
Drosophila melanogaster dUMP + diphosphate
-
?
dUTP + H2O removes dUTP from the nucleotide triphosphate pool and therefore prevents the incorporation of uracil into the DNA, provides substrate for dTTP synthesis Drosophila melanogaster dUMP + diphosphate
-
?
additional information no hydrolysis of dUDP Drosophila melanogaster ?
-
?

Subunits

Subunits Comment Organism
trimer 3 * 19800, full length enzyme, 3 * 17200, truncated enzyme, mass spectrometry, gel filtration Drosophila melanogaster

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
54
-
melting point Drosophila melanogaster

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.1
-
dTTP pH 7.5, 25°C Drosophila melanogaster
0.7
-
dCTP pH 7.5, 25°C Drosophila melanogaster
12
-
dUTP pH 7.5, 25°C Drosophila melanogaster