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- W2023696192 abstract "Abstract UDP-glucose: d -fruetose 2-glucosyltransferase (EC 2.4.1.13) was purified 97-fold from cell-free extracts of tapioca tuber. The purified enzyme was stable at 0–5 °. The optimum activity in the direction of sucrose synthesis occurred at 37 °, whereas sucrose cleavage was maximum at 45 °. The reaction in the direction of sucrose cleavage was powerfully inhibited by Tris-HCl buffer. UDP-glucose and ADP-glucose were almost equally effective in the synthesis of sucrose. The K m values of the enzyme for UDP-glucose and for ADP-glucose were 8.3 and 6.7 m m , respectively. UDP and ADP inhibited the reaction. In the direction of sucrose cleavage, both UDP and ADP served as glucosyl acceptors. The K m of the enzyme for UDP and for ADP were 6.6 and 33.3 m m , respectively." @default.
- W2023696192 created "2016-06-24" @default.
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- W2023696192 date "1971-01-01" @default.
- W2023696192 modified "2023-09-27" @default.
- W2023696192 title "Studies on UDP-glucose: d-Fructose 2-glucosyltransferase from tapioca tuber" @default.
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- W2023696192 doi "https://doi.org/10.1016/0003-9861(71)90288-8" @default.
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