Rider M H, Kuntz D A, Hue L
Institute of Cellular and Molecular Pathology, Louvain University Medical School, Brussels, Belgium.
Biochem J. 1988 Jul 15;253(2):597-601. doi: 10.1042/bj2530597.
Purified chicken liver 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase was phosphorylated either from fructose 2,6-bis[2-32P]phosphate or fructose 2-phosphoro[35S]thioate 6-phosphate. The turnover of the thiophosphorylated enzyme intermediate as well as the overall phosphatase reaction was four times faster than with authentic fructose 2,6-bisphosphate. Fructose 2-phosphorothioate 6-phosphate was 10-100-fold less potent than authentic fructose 2,6-bisphosphate in stimulating 6-phosphofructo-1-kinase and pyrophosphate:fructose 6-phosphate phosphotransferase, but about 10 times more potent in inhibiting fructose 1,6-bisphosphatase. The analogue was twice as effective as authentic fructose 2,6-bisphosphate in stimulating pyruvate kinase from trypanosomes.
纯化的鸡肝6-磷酸果糖-2-激酶/果糖2,6-二磷酸酶可由果糖2,6-双[2-³²P]磷酸或果糖2-磷酰[³⁵S]硫代酸6-磷酸进行磷酸化。硫代磷酸化酶中间体的周转以及整个磷酸酶反应比使用真实的果糖2,6-二磷酸快四倍。果糖2-磷酰硫代酸6-磷酸在刺激6-磷酸果糖-1-激酶和焦磷酸：果糖6-磷酸磷酸转移酶方面的效力比真实的果糖2,6-二磷酸低10-100倍，但在抑制果糖1,6-二磷酸酶方面的效力约高10倍。该类似物在刺激锥虫丙酮酸激酶方面的效果是真实果糖2,6-二磷酸的两倍。
