Cadet F, Meunier J C
Centre de Biotechnologie Agro-Industrielle, Institut National Agronomique Paris-Grignon, Thiverval-Grignon, France.
Biochem J. 1988 Jul 1;253(1):243-8. doi: 10.1042/bj2530243.
In this paper we study activation by dithiothreitol and reduced thioredoxins and deactivation by oxidized thioredoxins f of sedoheptulose-1,7-bisphosphatase. The behaviour of the enzyme when chromatographed on a thioredoxin-Sepharose column is also described. The enzyme is autoxidizable upon removal of reducing agents, and is activated when reduced by any of the thioredoxins. This mechanism may allow the regulation of the Calvin cycle upon light-dark and dark-light transitions. The formation of a stable complex between enzyme and thioredoxin could explain the inhibitory effect of high thioredoxin concentrations. The use of immunological techniques shows that sedoheptulose-1,7-bisphosphatase and fructose-1,6-bisphosphatase are poorly related immunologically.
在本文中，我们研究了二硫苏糖醇和还原型硫氧还蛋白对景天庚酮糖-1,7-二磷酸酶的激活作用，以及氧化型硫氧还蛋白f对该酶的失活作用。还描述了该酶在硫氧还蛋白-琼脂糖柱上进行层析时的行为。去除还原剂后，该酶可自动氧化，并且被任何一种硫氧还蛋白还原时都会被激活。这种机制可能允许在光暗转换和暗亮转换时对卡尔文循环进行调节。酶与硫氧还蛋白之间形成稳定复合物可以解释高浓度硫氧还蛋白的抑制作用。免疫技术的应用表明，景天庚酮糖-1,7-二磷酸酶和果糖-1,6-二磷酸酶在免疫学上相关性较差。
