| Literature DB >> 14726951 |
Christian Hirsch1, Shahram Misaghi, Daniël Blom, Michael E Pacold, Hidde L Ploegh.
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.Entities:
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Year: 2004 PMID: 14726951 PMCID: PMC1298977 DOI: 10.1038/sj.embor.7400066
Source DB: PubMed Journal: EMBO Rep ISSN: 1469-221X Impact factor: 8.807