Mutant forms of the Escherichia coli Lon protease with a modified N-terminal domain

被引:0
|
作者
Rasulova, FS [1 ]
Dergousova, NI [1 ]
Mel'nikov, EE [1 ]
Ginodman, LM [1 ]
Rotanova, TV [1 ]
机构
[1] MM Shemyakin Inst Bioorgan Chem, Moscow 117871, Russia
来源
BIOORGANICHESKAYA KHIMIYA | 1998年 / 24卷 / 05期
关键词
protease Lon; serine protease; domain-domain interactions; ion gene; recombinant genes; hybrid proteins; Escherichia coli;
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学科分类号
摘要
The functional domain boundaries of the ATP-dependent Lon proteases were identified by comparative analysis of the amino acid sequences of the enzymes from evolutionarily distant organisms. Modified forms of the Escherichia coli Lon protease with the elongated or substituted N-terminal domain and a truncated enzyme lacking the N-terminal domain were obtained through genetic engineering methods. Analysis of the enzymatic properties of the resulting modified forms of Lon protease revealed the importance of the N-terminal domain in its function.
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页码:370 / 375
页数:6
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