Peptide N-glycanase
From Proteopedia
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== Function == | == Function == | ||
| - | + | '''Peptide 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<ref>PMID:17116467</ref>. PNG is present in prokaryotes and eukaryotes. PNG N terminal PUB domain interacts with the AAA ATPase protein p97 is a central component in the ubiquitin-proteasome system. '''Peptide N-glycanase F''' cleaves Asn-GlcNac bond in N-linked glycoproteins and glycopeptides<ref>PMID:7881905</ref>. | |
| - | '''Peptide 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<ref>PMID:17116467</ref>. PNG is present in prokaryotes and eukaryotes. PNG N terminal PUB domain interacts with the AAA ATPase protein p97 is a central component in the ubiquitin-proteasome system. | + | |
== Disease == | == Disease == | ||
| + | Mutations in human PNG genes were found in patients showing developmental delay, multifocal epilepsy and other multiple symptoms<ref>PMID:25398991</ref>. | ||
== Relevance == | == Relevance == | ||
| - | + | PNG F is used in studying of glycoproteins. | |
== Structural highlights == | == Structural highlights == | ||
Revision as of 08:57, 20 June 2016
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3D Structures of PNGase
Updated on 20-June-2016
References
- ↑ 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
