面包酵母中的腺苷5'-焦磷酸硫酸化酶。
Adenosine 5'-pyrophosphate sulphurylase in baker's yeast.
作者信息
Adams C A, Nicholas D J
出版信息
Biochem J. 1972 Jul;128(3):647-54. doi: 10.1042/bj1280647.
Abstract
ADP sulphurylase from baker's yeast was purified and its properties were studied. The enzyme is very heat-labile and its activity shows linear kinetics over narrow ranges of time and protein concentration. It is not activated by metals and is inhibited by thiol-reactive compounds. The enzyme, which replaces inorganic sulphate in adenosine 5'-sulphatophosphate with P(i) to yield ADP, also catalyses an exchange of P(i) into ADP. Kinetic studies show that the enzyme has a high affinity for adenosine 5'-sulphatophosphate, although concentrations in excess of 1.0mm are inhibitory. However, the kinetics for P(i) are more complex and the enzyme is not inhibited by P(i) up to 20.0mm.
摘要
对来自面包酵母的ADP硫酸化酶进行了纯化并研究了其性质。该酶对热非常不稳定，其活性在狭窄的时间和蛋白质浓度范围内呈线性动力学。它不受金属激活，而受硫醇反应性化合物抑制。该酶能将腺苷5'-磷酸硫酸酯中的无机硫酸盐替换为P(i)以生成ADP，还能催化P(i)与ADP的交换。动力学研究表明，该酶对腺苷5'-磷酸硫酸酯具有高亲和力，尽管浓度超过1.0mM时具有抑制作用。然而，P(i)的动力学更为复杂，该酶在高达20.0mM的P(i)浓度下不受抑制。
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