Structural and functional peculiarities of the ATP-dependent Lon protease from Escherichia coli

被引：0
|
作者：
Rotanova, TV [1 ]
机构：
[1] Russian Acad Sci, Shemyakin Ovchinnikov Inst Bioorgan Chem, Moscow 117871, Russia
来源：
BIOORGANICHESKAYA KHIMIYA | 1999年 / 25卷 / 12期
关键词：
active site; ATP-dependent proteolysis; Escherichia coli; Lon protease; interdomain interactions; site-directed mutagenesis;
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摘要：
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 transmition 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.
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页码：883 / 891
页数：9
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