酵母N-聚糖酶能够区分天然糖蛋白和非天然糖蛋白。
Yeast N-glycanase distinguishes between native and non-native glycoproteins.
作者信息
Hirsch Christian, Misaghi Shahram, Blom Daniël, Pacold Michael E, Ploegh Hidde L
机构信息
Department of Pathology, Harvard Medical School, Boston, Massachusetts 02115, USA.
出版信息
EMBO Rep. 2004 Feb;5(2):201-6. doi: 10.1038/sj.embor.7400066. Epub 2004 Jan 9.
Abstract
N-glycanase from Saccharomyces cerevisiae (Png1) preferentially removes N-glycans from misfolded proteins. The ability of Png1 to distinguish between folded and misfolded glycoproteins is reminiscent of substrate recognition by UDP-glucose glycoprotein glucosyl transferase, an enzyme that possesses this trait. The only known in vivo substrates of Png1 are aberrant glycoproteins that originate in the endoplasmic reticulum, and arrive in the cytoplasm for proteasomal degradation. The substrate specificity of Png1 is admirably suited for this task.
摘要
来自酿酒酵母的N-聚糖酶（Png1）优先从错误折叠的蛋白质中去除N-聚糖。Png1区分折叠和错误折叠糖蛋白的能力让人联想到UDP-葡萄糖糖蛋白葡糖基转移酶对底物的识别，后者是一种具有这种特性的酶。Png1唯一已知的体内底物是起源于内质网、到达细胞质进行蛋白酶体降解的异常糖蛋白。Png1的底物特异性非常适合这项任务。
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