甘氨酸384是早老素-1功能所必需的，并且在细菌多跨膜天冬氨酸蛋白酶中保守存在。

Glycine 384 is required for presenilin-1 function and is conserved in bacterial polytopic aspartyl proteases.

作者信息

Steiner H, Kostka M, Romig H, Basset G, Pesold B, Hardy J, Capell A, Meyn L, Grim M L, Baumeister R, Fechteler K, Haass C

机构信息

Adolf Butenandt-Institute, Department of Biochemistry, Laboratory for Alzheimer's Disease Research, Ludwig-Maximilians-University, 80336 Munich, Germany.

出版信息

Nat Cell Biol. 2000 Nov;2(11):848-51. doi: 10.1038/35041097.

DOI:10.1038/35041097

PMID:11056541

Abstract

Endoproteolysis of beta-amyloid precursor protein (betaAPP) and Notch requires conserved aspartate residues in presenilins 1 and 2 (PS1 and PS2). Although PS1 and PS2 have therefore been proposed to be aspartyl proteases, no homology to other aspartyl proteases has been found. Here we identify homology between the presenilin active site and polytopic aspartyl proteases of bacterial origin, thus supporting the hypothesis that presenilins are novel aspartyl proteases.

摘要

β-淀粉样前体蛋白（βAPP）和Notch的内蛋白水解需要早老素1和2（PS1和PS2）中保守的天冬氨酸残基。因此，尽管有人提出PS1和PS2是天冬氨酸蛋白酶，但尚未发现它们与其他天冬氨酸蛋白酶有同源性。在这里，我们确定了早老素活性位点与细菌来源的多结构域天冬氨酸蛋白酶之间的同源性，从而支持了早老素是新型天冬氨酸蛋白酶的假说。