On the mechanism of SPP-catalysed intramembrane proteolysis; conformational control of peptide bond hydrolysis in the plane of the membrane

被引:41
作者
Lemberg, MK [1 ]
Martoglio, B [1 ]
机构
[1] ETH Honggerberg, Swiss Fed Inst Technol, Inst Biochem, CH-8093 Zurich, Switzerland
来源
FEBS LETTERS | 2004年 / 564卷 / 03期
关键词
integral membrane protein; lipid bilayer; presenilin; protease; signal peptide peptidase;
D O I
10.1016/S0014-5793(04)00192-9
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Intramembrane-cleaving proteases are members of a novel type of enzyme that hydrolyse substrate proteins within transmembrane regions. The presently known proteases that catalyse such cleavage reactions are membrane proteins of high hydrophobicity and multiple predicted transmembrane regions. A key feature is the positioning of active site residues in hydrophobic segments implying that the catalytic centre is assembled within the plane of the membrane. Nevertheless, all these proteases appear to utilise catalytic mechanisms similar to classic proteases that expose their active site domains in aqueous compartments. In the present review, we will address the mechanism of intramembrane proteolysis on the example of the signal peptide peptidase, and discuss how enzyme-catalysed hydrolysis of peptide bonds within the plane of a cellular membrane might occur. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码:213 / 218
页数:6
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