Peptide N-glycanase
FunctionPeptide N-glycanase (PNG) cleaves oligosaccharides from misfolded proteins and prepares them for degradation. PNG cleaves at β-aspartyl glucosamine bond to remove a glycan moiety from glycoprotein substrate[1]. PNG is present in prokaryotes and eukaryotes. PNG N terminal PUB domain interacts with the AAA ATPase protein p97 which is a central component in the ubiquitin-proteasome system. Peptide N-glycanase F cleaves Asn-GlcNac bond in N-linked glycoproteins and glycopeptides[2]. DiseaseMutations in human PNG genes were found in patients showing developmental delay, multifocal epilepsy and other multiple symptoms[3]. RelevancePNG F is used in studying of glycoproteins. Structural highlights
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3D Structures of PNGase3D Structures of PNGase
Updated on 22-August-2023
ReferencesReferences
- ↑ Tanabe K, Lennarz WJ, Suzuki T. A cytoplasmic peptide: N-glycanase. Methods Enzymol. 2006;415:46-55. PMID:17116467 doi:http://dx.doi.org/10.1016/S0076-6879(06)15004-1
- ↑ Norris GE, Stillman TJ, Anderson BF, Baker EN. The three-dimensional structure of PNGase F, a glycosylasparaginase from Flavobacterium meningosepticum. Structure. 1994 Nov 15;2(11):1049-59. PMID:7881905
- ↑ Suzuki T. The cytoplasmic peptide:N-glycanase (Ngly1)-basic science encounters a human genetic disorder. J Biochem. 2015 Jan;157(1):23-34. doi: 10.1093/jb/mvu068. Epub 2014 Nov 13. PMID:25398991 doi:http://dx.doi.org/10.1093/jb/mvu068