组蛋白去乙酰化酶突变体水解酰基底物的研究

Study on hydrolysis of acyl substrate by histone deacetylase mutant

蛋白质的去乙酰化修饰是由组蛋白去乙酰化酶家族协同调控的,将野生型的组蛋白去乙酰化酶水解酶活中心位置的141位的色氨酸分别突变为丙氨酸、甘氨酸、组氨酸和苯丙氨酸,发现其对酰基底物的水解能力较野生型变弱,因此,得出野生型组蛋白去乙酰化酶的141氨基酸所占空间位置的大小,影响其酶活性的结论。

The deacetylation of proteins was synergistically regulated by the histone deacetylase family, and the tryptophan at position 141 of the wild-type HDAC8 hydrolytic enzyme was mutated to alanine, Glycine, histidine and phenylalanine, it was found that the hydrolysis ability of the acyl substrate was weaker than that of the wild type. Therefore, the spatial position of the 141 amino acid of HDAC8 was obtained size, affecting its enzymatic activity.