Endo-β-N-acetylglucosaminidase (Endo A)

Endo-β-N-acetylglucosaminidase (Endo A) Structure
Endo-β-N-acetylglucosaminidase (Endo A) structure
Common Name Endo-β-N-acetylglucosaminidase (Endo A)
CAS Number 37278-88-9 Molecular Weight N/A
Density N/A Boiling Point 100.0 °C
Molecular Formula N/A Melting Point N/A
MSDS USA Flash Point N/A

Improved plasma membrane expression of the trafficking defective P344R mutant of muscle, skeletal, receptor tyrosine kinase (MuSK) causing congenital myasthenic syndrome.

Int. J. Biochem. Cell Biol. 60 , 119-29, (2015)

Muscle, skeletal, receptor tyrosine kinase (MuSK) is a key organizer at the postsynaptic membrane and critical for proper development and maintenance of the neuromuscular junction. Mutations in MUSK result in congenital myasthenic syndrome (CMS). We hypothesi...

A cholesterol consensus motif is required for efficient intracellular transport and raft association of a group 2 HA from influenza virus.

Biochem. J. 465(2) , 305-14, (2015)

The HA (haemagglutinin) of influenza viruses must be recruited to membrane rafts to perform its function in membrane fusion and virus budding. We previously showed using FRET that deletion of the two raft-targeting features of HA, S-acylation at the cytoplasm...

Proteome analysis of the farnesol-induced stress response in Aspergillus nidulans--The role of a putative dehydrin.

J. Proteomics 75(13) , 4038-49, (2012)

The isoprenoid alcohol farnesol represents a quorum-sensing molecule in pathogenic yeasts, but was also shown to inhibit the growth of many filamentous fungi. In order to gain a deeper insight into the antifungal activity of farnesol, we performed 2D-differen...

The hepatitis C virus E1 glycoprotein undergoes productive folding but accelerated degradation when expressed as an individual subunit in CHO cells.

PLoS ONE 6(8) , e23838, (2011)

Hepatitis C Virus E1E2 heterodimers are components of the viral spike. Although there is a general agreement on the necessity of the co-expression of both E1 and E2 on a single coding unit for their productive folding and assembly, in a previous study using a...

An endo-β-N-acetylglucosaminidase from Enterococcus faecalis V583 responsible for the hydrolysis of high-mannose and hybrid-type N-linked glycans.

FEMS Microbiol. Lett. 325(2) , 123-9, (2011)

It has been demonstrated previously that Enterococcus faecalis produces secreted endoglycosidases that enable the bacteria to remove N-linked glycans from glycoproteins. One enzyme potentially responsible for this activity is EF0114, comprising a typical GH18...

Double-knockout of putative endo-β-N-acetylglucosaminidase (ENGase) genes in Arabidopsis thaliana: loss of ENGase activity induced accumulation of high-mannose type free N-glycans bearing N,N'-acetylchitobiosyl unit.

Biosci. Biotechnol. Biochem. 75(5) , 1019-21, (2011)

Endo-β-N-acetylglucosaminidase (ENGase) is involved in the production of high-mannose type free N-glycans during plant development and fruit maturation. In a previous study (K. Nakamura et al. Biosci. Biotechnol. Biochem., 73, 461-464 (2009)), we identified t...

Deglycosylation systematically improves N-glycoprotein identification in liquid chromatography-tandem mass spectrometry proteomics for analysis of cell wall stress responses in Saccharomyces cerevisiae lacking Alg3p.

J. Chromatogr. B. Analyt. Technol. Biomed. Life Sci. 923-924 , 16-21, (2013)

Post-translational modification of proteins with glycosylation is of key importance in many biological systems in eukaryotes, influencing fundamental biological processes and regulating protein function. Changes in glycosylation are therefore of interest in u...

Large-scale assignment of N-glycosylation sites using complementary enzymatic deglycosylation

Talanta 85(1) , 499-505, (2011)

Endoglycosidase is a class of glycosidases that specifically cleaves the glycosidic bond between two proximal residues of GlcNAc in the pentasaccharide core of N-glycan, leaving the innermost GlcNAc still attached to its parent protein, which provides a diffe...

Identification and origin of N-linked β-D-N-acetylglucosamine monosaccharide modifications on Arabidopsis proteins.

Plant Physiol. 161(1) , 455-64, (2013)

Many plant proteins are modified with N-linked oligosaccharides at asparagine-X-serine/threonine sites during transit through the endoplasmic reticulum and the Golgi. We have identified a number of Arabidopsis (Arabidopsis thaliana) proteins with modification...

Cytosolic location of an endo-N-acetyl-beta-D-glucosaminidase activity in rat liver and kidney.

Biochem. J. 180(3) , 673-76, (1979)

Endo-N-acetyl-beta-D-glucosaminidase activity towards an oligomannosidic type glycoamino acid substrate was found in the soluble fraction of rat liver and kidney. No evidence for a lysosomal form of the activity was found.