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EC Number Posttranslational Modification Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.207glycoprotein - 681144, 693105, 706280, 737003
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.207glycoprotein AdXET5 and AdXET6: asparagine-linked carbohydrate, N-glycosylated, glycosylation of the protein is not required for endo-transglycosylase activity 636817
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.207glycoprotein all 4 isoenzymes, TCH4, Meri-5, EXGT and XTR9, are N-glycosylated, requirement of glycosylation for activity of the isoenzymes differs 636835
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.207glycoprotein all HvXTH protein members, except HvXTH15, have a conserved N-glycosylation site. The N-glycosylation site domain (NxT/S/Y) is thought to play a role in protein stability 759806
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.207glycoprotein AtXTH13 cDNA construct is correctly expressed and posttranslationally modified with variable N-linked glycans on one site 715759
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.207glycoprotein enzyme are deglycosylated with commercial N-glycosidase F. Unglycosylated TmXET6.3 due to N-deglycosylation loses its enzyme activity, it is likely that N-glycosylation affects protein folding and/or catalytic activity 759967
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.207glycoprotein enzyme contains a conserved N-glycosylation site situated proximal to the predicted catalytic site, deglycosylation by endoglycosidase H or by site-directed mutagenesis does not influence the enzyme activity 657870
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.207glycoprotein FcXTH2 shows an N-glycosylation site that is located far to the active site and oriented on the edge of the opposite face. In the primary sequence of the protein, the N-glycosylation site is spaced by 17 residues from the catalytic triad 759371
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.207glycoprotein isozyme possesses an N-glycosylation site adjacent to the C-terminal side of the DEIDFEFLG motif 660231
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.207glycoprotein isozyme XTH1, not isozyme XTH21, possesses an N-glycosylation site adjacent to the C-terminal side of the DEIDFEFLG motif 660231
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