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- W2015418685 abstract "The formation of glucose 6-arsenate and glucose 6-phosphate shows similar thermodynamic constants: both reactions are endothermic, endergonic, and occur with a decrease of entropy. However, the kinetic coefficients of the spontaneous formation of the arsenate esters are ca. 105 times greater than those of their homologous phosphate esters. The activation energy of the spontaneous formation of glucose 6-arsenate (E = + 12 kcal mol−1) is even smaller than that of the formation of glucose 6-phosphate by alkaline phosphate (E = + 13 kcal mol−1). Similar to the case of the monoalkylphosphates, the monoanion species of glucose 6-arsenate is much more reactive than the dianion species. This is an important difference with respect to glucose 6-phosphate. The calculated half-lives at 25 °C and pH 7.0 of glucose 6-arsenate and 6-arsenogluconate are only ca. 6 and 30 min, respectively; they increase at lower temperatures and alkaline pH. At 0 °C and pH 9.0 the half-life of glucose 6-arsenate is ca. 20 h. Therefore, arsenate esters could probably be isolated for use as a tool in biochemical studies. Arsenate esters are good analogs of the phosphate esters for a variety of enzymes. Glucose-6-phosphate dehydrogenase shows nearly similar values of Km and V for either glucose 6-phosphate or glucose 6-arsenate, and hexokinase is similarly inhibited by both compounds. 6-Phosphogluconate dehydrogenase has the same V with respect to 6-phosphogluconate and 6-arsenogluconate although the enzyme shows a much lower affinity for the latter substrate." @default.
- W2015418685 created "2016-06-24" @default.
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- W2015418685 date "1980-11-01" @default.
- W2015418685 modified "2023-10-16" @default.
- W2015418685 title "Sugar-arsenate esters: Thermodynamics and biochemical behavior" @default.
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- W2015418685 doi "https://doi.org/10.1016/0003-9861(80)90084-3" @default.
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