果糖-2,6-二磷酸酶和6-磷酸果糖-2-激酶在酵母中是可分离的。
Fructose-2,6-bisphosphatase and 6-phosphofructo-2-kinase are separable in yeast.
作者信息
Kretschmer M, Schellenberger W, Otto A, Kessler R, Hofmann E
机构信息
Institute of Biochemistry, Karl-Marx-University Leipzig, German Democratic Republic.
出版信息
Biochem J. 1987 Sep 15;246(3):755-9. doi: 10.1042/bj2460755.
Abstract
Fructose-2,6-bisphosphatase was purified from yeast and separated from 6-phosphofructo-2-kinase and alkaline phosphatase. The enzyme released Pi from the 2-position of fructose 2,6-bisphosphate and formed fructose 6-phosphate in stoichiometric amounts. The enzyme displays hyperbolic kinetics towards fructose 2,6-bisphosphate, with a Km value of 0.3 microM. It is strongly inhibited by fructose 6-phosphate. The inhibition is counteracted by L-glycerol 3-phosphate. Phosphorylation of the enzyme by cyclic-AMP-dependent protein kinase causes inactivation, which is reversible by the action of protein phosphatase 2A.
摘要
果糖-2,6-二磷酸酶从酵母中纯化出来，并与6-磷酸果糖-2-激酶和碱性磷酸酶分离。该酶从果糖2,6-二磷酸的2位释放无机磷酸，并按化学计量形成果糖6-磷酸。该酶对果糖2,6-二磷酸呈现双曲线动力学，Km值为0.3微摩尔。它受到果糖6-磷酸的强烈抑制。L-甘油3-磷酸可抵消这种抑制作用。环磷酸腺苷依赖性蛋白激酶对该酶的磷酸化导致其失活，而蛋白磷酸酶2A的作用可使其逆转。
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本文引用的文献
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