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Yeast N ‐glycanase distinguishes between native and non‐native glycoproteins
Author(s) -
Hirsch Christian,
Misaghi Shahram,
Blom Daniël,
Pacold Michael E,
Ploegh Hidde L
Publication year - 2004
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/sj.embor.7400066
Subject(s) - glycoprotein , endoplasmic reticulum , glycan , biochemistry , cytoplasm , saccharomyces cerevisiae , endoplasmic reticulum associated protein degradation , yeast , biology , substrate (aquarium) , microbiology and biotechnology , transferase , enzyme , chemistry , unfolded protein response , ecology
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.