کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1931085 | 1536786 | 2010 | 7 صفحه PDF | دانلود رایگان |
In glycoprotein quality control system in the endoplasmic reticulum (ER), UGGT (UDP-glucose:glycoprotein glucosyltransferase) and glucosidase II (G-II) play key roles. UGGT serves as a glycoprotein folding sensor by virtue of its unique specificity to glucosylate glycoproteins at incompletely folded stage. By using various UDP-Glc analogues, we first analyzed donor specificity of UGGT, which was proven to be rather narrow. However, marginal activity was observed with UDP-galactose and UDP-glucuronic acid as well as with 3-, 4- and 6-deoxy glucose analogues to give corresponding transfer products. Intriguingly, G-II smoothly converted all of them back to Man9GlcNAc2, providing an indication that G-II has a promiscuous activity as a broad specificity hexosidase.
Research highlights
► UGGT has a narrow donor specificity.
► UGGT gave several non-natural high-mannose-type glycans.
► G-II has a promiscuous activity as broad specificity hexosidase.
Journal: Biochemical and Biophysical Research Communications - Volume 403, Issues 3–4, 17 December 2010, Pages 322–328