[大肠杆菌中ATP依赖型Lon蛋白酶的结构与功能特性]
[Structural and functional characteristics of ATP-dependent Lon-proteinase from Escherichia coli].
作者信息
Rotanova T V
机构信息
Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia.
出版信息
Bioorg Khim. 1999 Dec;25(12):883-91.
PMID:10734549
Abstract
Enzymic and structural peculiarities of the ATP-dependent Lon protease from Escherichia coli and its mutant and modified forms were studied. Amino acid residues important for the function of proteolytic and ATPase sites and for the transmission of the interdomain signals of the activity coupling were found. It was shown that the protein substrates are hydrolyzed only by the full-size enzyme, whereas the isolated proteolytic domain displays a peptide-hydrolyzing activity.
摘要
对来自大肠杆菌的ATP依赖型Lon蛋白酶及其突变体和修饰形式的酶学和结构特性进行了研究。发现了对蛋白水解位点和ATP酶位点功能以及活性偶联的结构域间信号传递很重要的氨基酸残基。结果表明，蛋白质底物仅被全长酶水解，而分离的蛋白水解结构域具有肽水解活性。
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