2.4.99.19: undecaprenyl-diphosphooligosaccharide-protein glycotransferase
This is an abbreviated version!
For detailed information about undecaprenyl-diphosphooligosaccharide-protein glycotransferase, go to the full flat file.
Word Map on EC 2.4.99.19
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2.4.99.19
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campylobacter
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n-glycosylation
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jejuni
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n-linked
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glycans
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lipid-linked
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lari
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sequons
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asparagine-linked
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meningitidis
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single-subunit
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glycoengineering
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ribophorin
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dolichols
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pilins
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medicine
- 2.4.99.19
- campylobacter
-
n-glycosylation
- jejuni
-
n-linked
- glycans
-
lipid-linked
- lari
-
sequons
-
asparagine-linked
- meningitidis
-
single-subunit
-
glycoengineering
-
ribophorin
- dolichols
- pilins
- medicine
Reaction
Synonyms
bacterial oligosaccharyltransferase, bacterial OST, N-oligosaccharyltransferase, N-OTase, oligosaccharyl transferase, oligosaccharyltransferase, oligosacharyltransferase, OST, OT, OTase, PglB, PglB oligosaccharyltransferase, PglB protein, PglB1, PglB2
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General Information
General Information on EC 2.4.99.19 - undecaprenyl-diphosphooligosaccharide-protein glycotransferase
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evolution
malfunction
metabolism
physiological function
additional information
bacterial PglB and archaeal AglB constitute a protein family of the catalytic subunit of OST, along with STT3 from eukaryotes, that has three types of OST catalytic centers, structure analysis and comparison, overview
evolution
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eukaryotic and prokaryotic OTases catalyze the transfer of oligosaccharides by a conserved mechanism
evolution
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in the delta proteobacteria Desulfovibrio sp., the PglB homologue is more closely related to eukaryotic and archaeal OTases than to its Campylobacter counterparts
evolution
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sequence analysis using 28 homologs from evolutionarily distant organisms, relationship between PglB and other Stt3 proteins, detailed overview Several inter-transmembrane loop regions of PglB/Stt3 contain strictly conserved motifs that are essential for PglB function
evolution
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bacterial PglB and archaeal AglB constitute a protein family of the catalytic subunit of OST, along with STT3 from eukaryotes, that has three types of OST catalytic centers, structure analysis and comparison, overview
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if the WWDYGY signature sequence is mutated to WAAYGY, PglB is no longer active in vivo
malfunction
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insertional knockout mutagenesis of the gene pglB2 is unsuccessful, suggesting that it is essential
malfunction
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insertional knockout mutagenesis of the gene pglB2 is unsuccessful, suggesting that it is essential
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PglB is involved in the Campylobacter jejuni general N-linked protein glycosylation pathway, overview
metabolism
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PglB is involved in the general N-linked glycosylation pathway encoded by the pgl gene cluster
metabolism
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the central enzyme in N-linked glycosylation is the oligosaccharyl transferase PglB, which catalyzes glycan transfer from a polyprenyldiphosphate-linked carrier to select asparagines within acceptor proteins
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PglB catalyzes the transfer of an oligosaccharide from a polyisoprenyl pyrophosphate carrier to the asparagine side chain of proteins within the conserved glycosylation sites D/E-X1-N-X2-S/T, where X1 and X2 can be any amino acids except proline
physiological function
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PglB catalyzes the transfer of an undecaprenyl-linked heptasaccharide to the asparagine side chain of proteins at the Asn-X-Ser/Thr motif
physiological function
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the central enzyme in N-linked glycosylation is the oligosaccharyl transferase PglB, which catalyzes glycan transfer from a polyprenyldiphosphate-linked carrier to select asparagines within acceptor proteins. Role of the intertransmembrane domain loops in OTase catalysis
physiological function
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the key enzyme involved in the coupling of glycan to asparagine residues within the acceptor sequon of the glycoprotein is the oligosaccharyltransferase PglB
physiological function
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the key enzyme involved in the coupling of glycan to asparagine residues within the acceptor sequon of the glycoprotein is the oligosaccharyltransferase PglB
physiological function
asparagine-linked glycosylation (N-linked glycosylation) is an essential and highly conserved post-translational protein modification. This modification is essential for specific molecular recognition, protein folding, sorting in the endoplasmic reticulum, cell-cell communication, and stability
physiological function
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the key enzyme involved in the coupling of glycan to asparagine residues within the acceptor sequon of the glycoprotein is the oligosaccharyltransferase PglB
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physiological function
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the key enzyme involved in the coupling of glycan to asparagine residues within the acceptor sequon of the glycoprotein is the oligosaccharyltransferase PglB
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physiological function
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asparagine-linked glycosylation (N-linked glycosylation) is an essential and highly conserved post-translational protein modification. This modification is essential for specific molecular recognition, protein folding, sorting in the endoplasmic reticulum, cell-cell communication, and stability
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several inter-transmembrane loop regions of PglB/Stt3 contain strictly conserved motifs that are essential for PglB function, these loops play a fundamental role in catalysis
additional information
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structure-function relationships for the periplasmic domain of the N-oligosaccharyltransferase PglB, overview
additional information
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the catalytic pocket is located in the right-side cavity of PglB, structure, overview. Glycosylation sequon recognition and amide nitrogen activation are prerequisites for the formation of the N-glycosidic linkage, identification of catalytically important, acidic amino acid residues, aspartates D154 and D156 belonging to a DXD motif, and metal ion interacting D56 and E319, mechanism of N-linked glycosylation, overview. A hallmark of N-linked glycosylation is the requirement of a serine or threonine at the 12 position of the acceptor sequon, enzyme structure-function relationship
additional information
the catalytic pocket is located in the right-side cavity of PglB, structure, overview. Glycosylation sequon recognition and amide nitrogen activation are prerequisites for the formation of the N-glycosidic linkage, identification of catalytically important, acidic amino acid residues, aspartates D154 and D156 belonging to a DXD motif, and metal ion interacting D56 and E319, mechanism of N-linked glycosylation, overview. A hallmark of N-linked glycosylation is the requirement of a serine or threonine at the 12 position of the acceptor sequon, enzyme structure-function relationship
additional information
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the catalytic pocket is located in the right-side cavity of PglB, structure, overview. Glycosylation sequon recognition and amide nitrogen activation are prerequisites for the formation of the N-glycosidic linkage, identification of catalytically important, acidic amino acid residues, aspartates D154 and D156 belonging to a DXD motif, and metal ion interacting D56 and E319, mechanism of N-linked glycosylation, overview. A hallmark of N-linked glycosylation is the requirement of a serine or threonine at the 12 position of the acceptor sequon, enzyme structure-function relationship
additional information
the PglB structure reveals a distinct catalytic motif in the transmembrane region that contributes to the catalytic function, structure analysis, overview
additional information
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topology mapping of PglB using the PhoA/LacZ fusion method, overview. The topological model shows that PglB possesses 11 transmembrane segments and two relatively large periplasmic regions other than the C-terminal domain, which is consistent with the proposal of the common Ncyt-Cperi topology with 11 transmembrane segments for the STT3 family proteins
additional information
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the PglB structure reveals a distinct catalytic motif in the transmembrane region that contributes to the catalytic function, structure analysis, overview
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