从线粒体天冬氨酸氨基转移酶上去除N端肽会在体外消除其与线粒体的相互作用。
Removal of an N-terminal peptide from mitochondrial aspartate aminotransferase abolishes its interactions with mitochondria in vitro.
作者信息
O'Donovan K M, Doonan S, Marra E, Passarella S, Quagliariello E
出版信息
Biochem J. 1985 Jun 15;228(3):609-14. doi: 10.1042/bj2280609.
Abstract
Treatment of mitochondrial aspartate aminotransferase from rat liver with trypsin leads to specific cleavage of the bonds between residues 26 and 27, and residues 31 and 32. The proteolysed enzyme has only a small residual catalytic activity, but retains a conformation similar to that of the native form as judged by accessibility and reactivity of cysteine residues. Proteolysis abolishes the ability of the enzyme either to bind to mitochondria or to be imported into the organelles. This suggests that the N-terminal segment of the native enzyme is essential for both of these functions, at least in the model system used to study the import process.
摘要
用胰蛋白酶处理大鼠肝脏中的线粒体天冬氨酸氨基转移酶会导致26位与27位残基之间以及31位与32位残基之间的肽键发生特异性裂解。经蛋白酶解的酶仅具有很小的残余催化活性，但根据半胱氨酸残基的可及性和反应性判断，其保留了与天然形式相似的构象。蛋白酶解消除了该酶与线粒体结合或被导入细胞器的能力。这表明，至少在用于研究导入过程的模型系统中，天然酶的N端片段对这两种功能均至关重要。
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