寡聚酶蛋白水解模型及其在柠檬酸合酶胰蛋白酶水解中的应用。
Models of proteolysis of oligomeric enzymes and their applications to the trypsinolysis of citrate synthases.
作者信息
Else A J, Danson M J, Weitzman P D
机构信息
Department of Biochemistry, University of Bath, Claverton Down, U.K.
出版信息
Biochem J. 1988 Sep 1;254(2):437-42. doi: 10.1042/bj2540437.
A simple statistical approach was used to generate predictive models of the proteolysis of multisubunit enzymes in order to correlate the loss of enzyme activity with the loss of native subunit. The models were applied to the trypsinolysis of the citrate synthases of pig heart, Bacillus megaterium and Escherichia coli. With the dimeric citrate synthases (pig heart and B. megaterium) trypsinolysis of one of the subunits appears to destroy the activity of the whole enzymic molecule. The hexameric E. coli citrate synthase behaves like a trimer of dimeric units, each of the dimers behaving similarly to the B. megaterium and pig heart enzymes. Palmitoyl-CoA is required for the trypsinolysis of pig heart citrate synthase, and at relatively high concentrations of this compound trypsinolysis of one subunit leaves the other subunit fully active. Palmitoyl-CoA is not required for the trypsinolysis of the other citrate synthases, and high concentrations of this metabolite do not affect the correlation of proteolysis with inactivation of these enzymes.
采用一种简单的统计方法来生成多亚基酶蛋白水解的预测模型，以便将酶活性的丧失与天然亚基的丧失联系起来。这些模型应用于猪心、巨大芽孢杆菌和大肠杆菌柠檬酸合酶的胰蛋白酶水解。对于二聚体柠檬酸合酶（猪心和巨大芽孢杆菌），其中一个亚基的胰蛋白酶水解似乎会破坏整个酶分子的活性。六聚体大肠杆菌柠檬酸合酶的行为类似于二聚体单元的三聚体，每个二聚体的行为与巨大芽孢杆菌和猪心的酶相似。猪心柠檬酸合酶的胰蛋白酶水解需要棕榈酰辅酶A，在这种化合物浓度相对较高时，一个亚基的胰蛋白酶水解会使另一个亚基保持完全活性。其他柠檬酸合酶的胰蛋白酶水解不需要棕榈酰辅酶A，并且这种代谢物的高浓度不会影响这些酶的蛋白水解与失活之间的相关性。
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