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A point mutation within the ATP-binding site inactivates both catalytic functions of the ATP-dependent protease La (Lon) from Escherichia coli.

作者信息

Fischer H, Glockshuber R

机构信息

Institut für Molekularbiologie und Biophysik, Eidgenössische Technische Hochschule Hönggerberg, Zürich, Switzerland.

出版信息

FEBS Lett. 1994 Dec 12;356(1):101-3. doi: 10.1016/0014-5793(94)01244-x.

DOI:10.1016/0014-5793(94)01244-x
PMID:7988699
Abstract

A point mutant in the ATP-binding motif (GPPGVGK362T) of the ATP-dependent protease La from Escherichia coli was investigated in which the lysine at position 362 was replaced by an alanine. The catalytic efficiency of the K362A mutant is at least two orders of magnitude lower than that of wild-type protease La due to a decreased Vmax and an increased KM for ATP. Simultaneously, the peptidase activity of La K362A is almost completely eliminated. Since selective inactivation of the peptidase activity of La does not affect its intrinsic ATPase activity, coupling of proteolysis with ATP hydrolysis is only uni-directional in this energy-dependent protease.

摘要

相似文献

1
A point mutation within the ATP-binding site inactivates both catalytic functions of the ATP-dependent protease La (Lon) from Escherichia coli.
FEBS Lett. 1994 Dec 12;356(1):101-3. doi: 10.1016/0014-5793(94)01244-x.
2
ATP hydrolysis is not stoichiometrically linked with proteolysis in the ATP-dependent protease La from Escherichia coli.在来自大肠杆菌的ATP依赖性蛋白酶La中，ATP水解与蛋白水解在化学计量上没有关联。
J Biol Chem. 1993 Oct 25;268(30):22502-7.
3
[Proteolysis coupled with ATP. Regulation of activity of proteolytic centers of Escherichia coli lon protease].[蛋白水解与ATP耦合。大肠杆菌lon蛋白酶蛋白水解中心活性的调节]
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4
[ATP-dependent proteinase La from Escherichia coli].[来自大肠杆菌的ATP依赖性蛋白酶La]
Bioorg Khim. 1994 Feb;20(2):114-25.
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[Structural and functional characteristics of ATP-dependent Lon-proteinase from Escherichia coli].[大肠杆菌中ATP依赖型Lon蛋白酶的结构与功能特性]
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Functional role of the N-terminal region of the Lon protease from Mycobacterium smegmatis.耻垢分枝杆菌Lon蛋白酶N端区域的功能作用
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7
[Coupling of proteolysis and hydrolysis of ATP upon functioning of Lon proteinase of Escherichia coli. II. Hydrolysis of ATP and activity of peptide hydrolase sites of the enzyme].[大肠杆菌Lon蛋白酶发挥功能时蛋白水解作用与ATP水解作用的偶联。II. ATP的水解及该酶肽水解酶位点的活性]
Bioorg Khim. 2001 Mar-Apr;27(2):120-9. doi: 10.1023/a:1011333103493.
8
ATP-dependent protease La (lon) from Escherichia coli.来自大肠杆菌的ATP依赖性蛋白酶La（lon）。
Methods Enzymol. 1994;244:350-75. doi: 10.1016/0076-6879(94)44027-1.
9
The lon protease from Mycobacterium smegmatis: molecular cloning, sequence analysis, functional expression, and enzymatic characterization.耻垢分枝杆菌的Lon蛋白酶：分子克隆、序列分析、功能表达及酶学特性研究
Biochemistry. 1998 Jan 6;37(1):377-86. doi: 10.1021/bi971732f.
10
Substrate sequestration by a proteolytically inactive Lon mutant.蛋白酶解失活的Lon突变体对底物的隔离作用
Proc Natl Acad Sci U S A. 1999 May 25;96(11):6064-71. doi: 10.1073/pnas.96.11.6064.

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