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Synthetic Substrates for an Endoplasmic Reticulum Protein‐Folding Sensor, UDP‐Glucose: Glycoprotein Glucosyltransferase
Author(s) -
Totani Kiichiro,
Ihara Yoshito,
Matsuo Ichiro,
Koshino Hiroyuki,
Ito Yukishige
Publication year - 2005
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200502723
Subject(s) - glucosyltransferase , calnexin , calreticulin , endoplasmic reticulum , glycoprotein , chemistry , mannose , biochemistry , glucosamine , substrate (aquarium) , golgi apparatus , glycan , microbiology and biotechnology , enzyme , biology , ecology
Quality control : UDP‐glucose:glycoprotein glucosyltransferase (UGGT) works as the folding sensor in glycoprotein quality control. It glucosylates the Man9GlcNAc2 of misfolded glycoproteins to produce Glc1Man9GlcNAc2, which is a ligand of calnexin and calreticulin. The synthetic substrate Man9GlcNAc2‐MTX can be used for the quantitative analysis of UGGT. UDP=uridine 5′‐diphosphate, Glc= D ‐glucose, Man= D ‐mannose, GlcNAc= N ‐acetyl‐ D ‐glucosamine, MTX=methotrexate.