Dgt preparations lacking DNA are able to bind single-stranded DNA with high affinity. DNA binding positively affects the activity of the enzyme. dGTPase activity displays sigmoidal (cooperative) behavior without DNA but hyperbolic (Michaelis-Menten) kinetics in its presence, consistent with a specific lowering of the apparent Km for dGTP
blockage of the alternative dUMP phosphatase pathway for deoxyribose-1-phosphate generation greatly exacerbates the severity of thymine starvation in enriched media, and under these conditions the dgt pathway becomes crucial in protecting the cells against thymineless death
the minimal amount of thymine required for growth of thymine-requiring (thyA) strains decreases with increased expression level of the dgt gene. As expected, this dgt-mediated effect is dependent on the DeoD purine nucleoside phosphorylase. ThyA strains experience growth difficulties upon nutritional shift-up, the dgt gene facilitates adaptation to the new growth conditions
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structure at 3.1 A resolution. The protein hexamer contains two molecules of single-stranded DNA, causing significant conformational changes in the enzyme, including in the catalytic site of the enzyme
development of a continuous spectrophotometric enzyme-coupled assay. The deoxyguanosine released by Dgt is subjected to phosphorolysis by purine nucleoside phosphorylase, yielding deoxyribose-1-phosphate and guanine, which, in turn, can be oxidized to 8-oxoguanine by xanthine oxidase