Glycine 384 is required for presenilin-1 function and is conserved in bacterial polytopic aspartyl proteases
Glycine 384 is required for presenilin-1 function and is conserved in bacterial polytopic aspartyl proteases
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DOI：
10.1038/35041097
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发表时间：
2000-11-01
影响因子：
21.3
通讯作者：
Haass, C
中科院分区：
文献类型：
--
作者：
Steiner, H;Kostka, M;Haass, C
β-淀粉样前体蛋白（β APP）和Notch的内蛋白水解需要早老蛋白1和2（PS1和PS2）中保守的天冬氨酸残基。虽然PS1和PS2因此被认为是乙酰蛋白酶，但与其他乙酰蛋白酶没有同源性，因此我们确定了早老素活性位点与细菌来源的多位乙酰蛋白酶之间的同源性，从而支持了早老素是新的乙酰蛋白酶的假设。
Endoproteolysis of beta -amyloid precursor protein (beta APP) 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.