磷酸化酶激酶α亚基和β亚基中的类葡糖淀粉酶结构域。
Glucoamylase-like domains in the alpha- and beta-subunits of phosphorylase kinase.
作者信息
Pallen Mark J
机构信息
Division of Immunity and Infection, University of Birmingham Medical School, Vincent Drive, Edgbaston, Birmingham B15 2TT, UK.
出版信息
Protein Sci. 2003 Aug;12(8):1804-7. doi: 10.1110/ps.0371103.
Abstract
Phosphorylase kinase is a four-subunit enzyme involved in the regulation of glycogen breakdown. The traditional textbook view is that only the gamma subunit has enzymatic activity, whereas the other three subunits have a regulatory role. Evidence from homology searches and sequence alignments, however, shows that the alpha- and beta-subunits possess amino-terminal glucoamylase-like domains and suggests that they might possess a previously overlooked amylase activity. If true, this would have important implications for the understanding, diagnosis, and management of glycogen storage diseases. There is thus a clear need to test this hypothesis through enzymatic assays and structural studies.
摘要
磷酸化酶激酶是一种参与糖原分解调节的四亚基酶。传统教科书观点认为只有γ亚基具有酶活性，而其他三个亚基具有调节作用。然而，同源性搜索和序列比对的证据表明，α亚基和β亚基具有氨基末端葡糖淀粉酶样结构域，并表明它们可能具有先前被忽视的淀粉酶活性。如果这是真的，这将对糖原贮积病的理解、诊断和管理产生重要影响。因此，显然需要通过酶分析和结构研究来验证这一假设。
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