Fischer G, Jatzkewitz H
Biochim Biophys Acta. 1978 Jan 27;528(1):69-76. doi: 10.1016/0005-2760(78)90053-x.
The activator of cereboroside-sulphatase (cerebroside-3-sulphate-3-sulphohydrolase, EC 3.1.6.8) is necessary for the enzymic hydrolysis of sulphatides (cerebroside sulphates) at ionic concentrations in the physiological range. The pH optimum of the reaction is 4.5--4.8. Under similar incubation conditions, a complex is formed between activator and sulphatides which is partially inhibited, due to competitive binding in the presence of cerebrosides of phosphatidylserine. Inhibition depends upon the concentration of the lipids and is of the same order of magnitude as the inhibition (by these lipids) of enzymic sulphatide hydrolysis in the presence of activator. Complex formation between activator and sulphatides is reversible since the complex dissociates partially when certain concentrations of phosphatidylserine are added. Moreover, the rate of sulphatide hydrolysis increases with the concentration of the activator.sulphatide complex in the reaction mixture. This indicates that the activator.sulphatide complex is the substrate for the enzyme and a model for this activation is presented.
脑苷脂硫酸酯酶(脑苷脂-3-硫酸酯-3-硫酸水解酶,EC 3.1.6.8)的激活剂对于在生理范围内离子浓度下硫脂(脑苷脂硫酸盐)的酶促水解是必需的。该反应的最适pH为4.5 - 4.8。在相似的孵育条件下,激活剂与硫脂之间形成复合物,在磷脂酰丝氨酸脑苷脂存在时,由于竞争性结合,该复合物会受到部分抑制。抑制作用取决于脂质的浓度,并且与(这些脂质)在激活剂存在下对硫脂酶促水解的抑制作用处于相同的数量级。激活剂与硫脂之间的复合物形成是可逆的,因为当加入一定浓度的磷脂酰丝氨酸时,复合物会部分解离。此外,硫脂水解速率随反应混合物中激活剂-硫脂复合物的浓度增加而增加。这表明激活剂-硫脂复合物是该酶的底物,并提出了这种激活作用的模型。