In Enzymology, a dUTP diphosphatase () is an enzyme that catalysis, catalyzes the chemical reaction
:dUTP + H
2O
dUMP + diphosphate
Thus, the two substrate (biochemistry), substrates of this enzyme are Deoxyuridine triphosphate, dUTP and water, H
2O, whereas its two product (chemistry), products are dUMP and diphosphate.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides in phosphorus-containing anhydrides. The List of enzymes, systematic name of this enzyme class is dUTP nucleotidohydrolase. Other names in common use include deoxyuridine-triphosphatase, dUTPase, dUTP pyrophosphatase, desoxyuridine 5'-triphosphate nucleotidohydrolase, and desoxyuridine 5'-triphosphatase. This enzyme participates in pyrimidine metabolism.
This enzyme has a dual function: on one hand, it removes dUTP from the nucleotide, deoxynucleotide pool, which reduces the probability of this base being incorporated into DNA by DNA polymerases, while on the other hand, it produces the dTTP precursor dUMP. Lack or inhibition of dUTPase action leads to harmful perturbations in the nucleotide pool resulting in increased uracil content of DNA that activates a hyperactive futile cycle of DNA repair.
Structural studies
As of late 2007, 48 tertiary structure, structures have been solved for this class of enzymes, with Protein Data Bank, PDB accession codes , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , and .
There are at least two structurally distinct families of dUTPases. The crystal structure of Homo sapiens, human dUTPase reveals that each subunit of the dUTPase Trimer (biochemistry), trimer protein folding, folds into an eight-stranded jelly-roll beta barrel, with the C-terminal beta sheet, beta strands interchanged among the protein subunit, subunits. The secondary structure, structure is similar to that of the ''Escherichia coli'' enzyme, despite low sequence homology between the two enzymes.
The second family has a novel all-alpha protein folding, fold, members of this family are unrelated to the all-beta tertiary structure, fold found in dUTPases of the majority of organisms.
See also
*DUT (gene), DUT, the gene that codes for this enzyme in humans
*DnaS or ''dut'', the gene that codes for this enzyme in ''E. coli''
References
Further reading
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EC 3.6.1
Enzymes of known structure
{{3.6-enzyme-stub