生物化学
糖蛋白
秀丽隐杆线虫
N-糖酰胺酶F
酶
糖基化
化学
胞浆
聚糖
肽
磷酸果糖激酶2
基因
作者
T. Kato,Atsuo Kawahara,Hisashi Ashida,Kenji Yamamoto
摘要
Peptide:N-glycanase (PNGase) is the enzyme responsible for de-N-glycosylation of misfolded glycoproteins in the cytosol. Here, we report the molecular identification and characterization of PNGase (png-1, F56G4.5) from Caenorhabditis elegans. This enzyme released both high mannose- and complex-type N-glycans from glycopeptides and denatured glycoproteins. Deglycosylation activity was inhibited by Zn(2+) and z-VAD-fmk, but not by EDTA. PNG-1 has a thioredoxin-like domain in addition to a transglutaminase domain, the core domain of PNGases, and exhibited protein disulphide reductase activity in vitro. Our biochemical studies revealed that PNG-1 is a unique bifunctional protein possessing two enzyme activities.
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