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Literature summary for 3.6.1.23 extracted from

  • Rotoli, S.M.; Jones, J.L.; Caradonna, S.J.
    Cysteine residues contribute to the dimerization and enzymatic activity of human nuclear dUTP nucleotidohydrolase (nDut) (2018), Protein Sci., 27, 1797-1809 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
nucleus
-
Homo sapiens 5634
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
dUTP + H2O Homo sapiens
-
dUMP + diphosphate
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens P33316
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA column chromatography and Superdex S200 gel filtration Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
A-549 cell
-
Homo sapiens
-
CCD-18Co cell
-
Homo sapiens
-
SAOS-2 cell
-
Homo sapiens
-
U2-OS cell
-
Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dUTP + H2O
-
Homo sapiens dUMP + diphosphate
-
?

Subunits

Subunits Comment Organism
monomer or dimer
-
Homo sapiens

Synonyms

Synonyms Comment Organism
DUT
-
Homo sapiens
dUTP nucleotidohydrolase
-
Homo sapiens
dUTPase
-
Homo sapiens