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
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
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
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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