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evolution
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phylogenetic analysis of acidic PNGases, yeast PNGases are diverse and distantly related from filamentous fungi PNGases in the phylogenetic tree
evolution
the enzyme from Dictyostelium discoideum is a member of transglutaminase (TG) -like superfamily and shows presence of a common transglutaminase core domain and sequence homology with the known PNGases, the tertiary structure matches with the mouse PNGase. DdPNGase possess the catalytic triad residues Cys210, His237 and Asp252, corresponding to the conserved core residues of other PNGases. DdPNGase also possess the corresponding Trp239 and Trp248, Arg229 and Glu241 conserved residues which possibly are essential for catalysis
evolution
PNGases are classified into two types based on their optimum pH: neutral or cytosolic PNGase (cPNGase) and acidic PNGase (aPNGase). cPNGase is found ubiquitously in eukaryotic cells, while aPNGase is found mainly in plants
evolution
PNGases are classified into two types based on their optimum pH: neutral or cytosolic PNGase (cPNGase) and acidic PNGase (aPNGase). cPNGase is found ubiquitously in eukaryotic cells, while aPNGase is found mainly in plants
evolution
PNGases are classified into two types based on their optimum pH: neutral or cytosolic PNGase (cPNGase) and acidic PNGase (aPNGase). cPNGase is found ubiquitously in eukaryotic cells, while aPNGase is found mainly in plants
evolution
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PNGases are classified into two types based on their optimum pH: neutral or cytosolic PNGase (cPNGase) and acidic PNGase (aPNGase). cPNGase is found ubiquitously in eukaryotic cells, while aPNGase is found mainly in plants
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evolution
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the enzyme from Dictyostelium discoideum is a member of transglutaminase (TG) -like superfamily and shows presence of a common transglutaminase core domain and sequence homology with the known PNGases, the tertiary structure matches with the mouse PNGase. DdPNGase possess the catalytic triad residues Cys210, His237 and Asp252, corresponding to the conserved core residues of other PNGases. DdPNGase also possess the corresponding Trp239 and Trp248, Arg229 and Glu241 conserved residues which possibly are essential for catalysis
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evolution
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PNGases are classified into two types based on their optimum pH: neutral or cytosolic PNGase (cPNGase) and acidic PNGase (aPNGase). cPNGase is found ubiquitously in eukaryotic cells, while aPNGase is found mainly in plants
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evolution
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phylogenetic analysis of acidic PNGases, yeast PNGases are diverse and distantly related from filamentous fungi PNGases in the phylogenetic tree
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malfunction
mutations in png-1 result in an increase in axon branching during morphogenesis of the vulval egg-laying organ and egg-laying behavior changes, neuronal defects include an increase in the branched morphology of the VC4 and VC5 egg-laying neurons as well as inappropriate branches from axons that run adjacent to the vulva
malfunction
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PNG1 deletion results in strong polarity defects
malfunction
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homozygous deletion mutants show developmental defect
malfunction
an enzyme knockout results in small sized aggregates, all of which do not form fruiting bodies. Knockout mutants show defect in aggregation, penotypes, overview
malfunction
in yeast cells, the absence of cytoplasmic PNGase (Png1) results in significant reduction of the levels of free oligosaccharidesfound in the cytosol, suggesting that the majority, if not all, of the free oligosaccharidesin yeast are generated from misfolded glycoproteins in a PNGase-dependent manner. Phenotypes/pathological conditions caused by mutations in gene orthologues of cytoplasmic PNGase are defect in ERAD, but no growth/viability defects
malfunction
phenotypes/pathological conditions caused by mutations in gene orthologues of cytoplasmic PNGase are abnormal axon branching of VC4/VC5 egg-laying neurons, and egg-laying behaviour defect
malfunction
phenotypes/pathological conditions caused by mutations in gene orthologues of cytoplasmic PNGase are global developmental delay, movement disorder, and hypotonia
malfunction
phenotypes/pathological conditions caused by mutations in gene orthologues of cytoplasmic PNGase are not detected
malfunction
phenotypes/pathological conditions caused by mutations in gene orthologues of cytoplasmic PNGase are severe developmental delay. An exome analysis identified a human patient with mutations in the NGLY1 gene and an increasing number of the patients harbouring mutations in NGLY1 alleles have been reported since then. The patients exhibited multiple symptoms that include global developmental delay, multifocal epilepsy, involuntary movement, abnormal liver function and the absence of tears
malfunction
phenotypes/pathological conditions caused by mutations in gene orthologues of cytoplasmic PNGase are slow growth and development, as well as defect in cell aggregation during multicellular development
malfunction
phenotypes/pathological conditions caused by mutations in gene orthologues of cytoplasmic PNGase are temperature-sensitive growth with strong polarity defects
malfunction
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an enzyme knockout results in small sized aggregates, all of which do not form fruiting bodies. Knockout mutants show defect in aggregation, penotypes, overview
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malfunction
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in yeast cells, the absence of cytoplasmic PNGase (Png1) results in significant reduction of the levels of free oligosaccharidesfound in the cytosol, suggesting that the majority, if not all, of the free oligosaccharidesin yeast are generated from misfolded glycoproteins in a PNGase-dependent manner. Phenotypes/pathological conditions caused by mutations in gene orthologues of cytoplasmic PNGase are defect in ERAD, but no growth/viability defects
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metabolism
the enzyme is proposed to participate in the proteasome dependent glycoprotein degradation pathway
metabolism
acidic peptide:N-glycanase (aPNGase) plays a pivotal role in plant glycoprotein turnover
metabolism
acidic peptide:N-glycanase (aPNGase) plays a pivotal role in plant glycoprotein turnover
metabolism
acidic peptide:N-glycanase (aPNGase) plays a pivotal role in plant glycoprotein turnover
metabolism
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acidic peptide:N-glycanase (aPNGase) plays a pivotal role in plant glycoprotein turnover
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metabolism
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the enzyme is proposed to participate in the proteasome dependent glycoprotein degradation pathway
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metabolism
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acidic peptide:N-glycanase (aPNGase) plays a pivotal role in plant glycoprotein turnover
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physiological function
png-1 can act from both neurons and epithelial cells to restrict axon branching. PNGase and Rad-23 regulate neuronal branching during organ innervation
physiological function
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the complex formed between peptide:N-glycanase and Rad23p exhibits enhanced deglycosylation activity, which suggests an important role for this enzyme in the misfolded glycoprotein degradation pathway in vivo
physiological function
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the complex formed between peptide:N-glycanase and Rad23p exhibits enhanced deglycosylation activity, which suggests an important role for this enzyme in the misfolded glycoprotein degradation pathway in vivo
physiological function
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the complex formed between peptide:N-glycanase and Rad23p exhibits enhanced deglycosylation activity, which suggests an important role for this enzyme in the misfolded glycoprotein degradation pathway in vivo
physiological function
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the peptide:N-glycanase ortholog PNG1 is essential for cell polarity despite its lack of enzymatic activity, PNG1 is involved in cell wall integrity
physiological function
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the enzyme is a deglycosylating enzyme involved in the endoplasmic reticulum-associated degradation process
physiological function
the enzyme is involved in a different de-N-glycosylation mechanism associated with plant growth and development
physiological function
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the enzyme plays a critical role during larval development and metamorphosis
physiological function
the N-terminal domain of PNGase (PUB) serves as a possible activator of HR23 in endoplasmic reticulum-associated degradation mechanisms
physiological function
the enzyme is an essential protein, important in aggregation during multicellular development of the organism
physiological function
Fbs1, a glycoprotein-specific ubiquitin ligase, protects misfolded glycoproteins from the action of cytoplasmic PNGase
physiological function
Fbs1, a glycoprotein-specific ubiquitin ligase, protects misfolded glycoproteins from the action of cytoplasmic PNGase
physiological function
PNGase F-II might have a function distinct from that of PNGase F
physiological function
the enzyme hydrolyzes the beta-aspartyl-glycosylamine bond of N-linked glycopeptides, and is involved in the degradation of misfolded or function-lost glycoproteins. cPNGase is believed to be involved in the protein quality control system, while aPNGase is involved in the release of N-glycan units from various glycopeptides produced in the degradation process of function-lost or aged glycoproteins
physiological function
the enzyme hydrolyzes the beta-aspartyl-glycosylamine bond of N-linked glycopeptides, and is involved in the degradation of misfolded or function-lost glycoproteins. cPNGase is believed to be involved in the protein quality control system, while aPNGase is involved in the release of N-glycan units from various glycopeptides produced in the degradation process of function-lost or aged glycoproteins
physiological function
the enzyme hydrolyzes the beta-aspartyl-glycosylamine bond of N-linked glycopeptides, and is involved in the degradation of misfolded or function-lost glycoproteins. cPNGase is believed to be involved in the protein quality control system, while aPNGase is involved in the release of N-glycan units from various glycopeptides produced in the degradation process of function-lost or aged glycoproteins
physiological function
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the enzyme hydrolyzes the beta-aspartyl-glycosylamine bond of N-linked glycopeptides, and is involved in the degradation of misfolded or function-lost glycoproteins. cPNGase is believed to be involved in the protein quality control system, while aPNGase is involved in the release of N-glycan units from various glycopeptides produced in the degradation process of function-lost or aged glycoproteins
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physiological function
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the enzyme is an essential protein, important in aggregation during multicellular development of the organism
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physiological function
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the enzyme hydrolyzes the beta-aspartyl-glycosylamine bond of N-linked glycopeptides, and is involved in the degradation of misfolded or function-lost glycoproteins. cPNGase is believed to be involved in the protein quality control system, while aPNGase is involved in the release of N-glycan units from various glycopeptides produced in the degradation process of function-lost or aged glycoproteins
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additional information
DdPNGase possess the catalytic triad residues Cys210, His237 and Asp252. DdPNGase also possess the corresponding Trp239 and Trp248, Arg229 and Glu241 conserved residues which possibly are essential for catalysis, structure homology modeling, overview
additional information
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DdPNGase possess the catalytic triad residues Cys210, His237 and Asp252. DdPNGase also possess the corresponding Trp239 and Trp248, Arg229 and Glu241 conserved residues which possibly are essential for catalysis, structure homology modeling, overview
additional information
structural comparison with PNGase F reveals a relatively larger glycan-binding groove in the catalytic domain and an additional bowl-like domain at the N-terminus of the protein
additional information
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structural comparison with PNGase F reveals a relatively larger glycan-binding groove in the catalytic domain and an additional bowl-like domain at the N-terminus of the protein
additional information
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DdPNGase possess the catalytic triad residues Cys210, His237 and Asp252. DdPNGase also possess the corresponding Trp239 and Trp248, Arg229 and Glu241 conserved residues which possibly are essential for catalysis, structure homology modeling, overview
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