Disease relevance of dUTPase

• The homotrimer enzyme unfolds reversibly as a trimeric entity with a melting temperature of 54 degrees C, 23 degrees C lower than Escherichia coli dUTPase [1].

High impact information on dUTPase

• dUTPase prevents uracil incorporation into DNA by strict regulation of the cellular dUTP:dTTP ratio [2].
• dUTPase is responsible for preventive DNA repair via exclusion of uracil [1].
• Altered active site flexibility and a structural metal-binding site in eukaryotic dUTPase: kinetic characterization, folding, and crystallographic studies of the homotrimeric Drosophila enzyme [1].
• In contrast to the bacterial enzyme, Mg(2+) binding modulates conformation of fly dUTPase, as identified by spectroscopy and by increment in melting temperature [1].
• Deoxyuridine triphosphatase (dUTPase), an enzyme that catalyzes hydrolysis of dUTP to deoxyuridylate and inorganic pyrophosphate, has been purified approximately 6,000-fold from Drosophila embryos [3].

Biological context of dUTPase

• The expression of dUTPase appears stage-specific, with embryos representing the only step in the life cycle of Drosophila with clearly detectable levels of the enzyme [3].

Analytical, diagnostic and therapeutic context of dUTPase

• In the present work, employing differential circular dichroism spectroscopy, we show that D. mel. dUTPase, a recently described eukaryotic model, has a similar affinity of binding towards alpha,beta-imino-dUTP as compared to the prokaryotic E. coli enzyme [4].

References