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Results 1 - 7 of 7
EC Number
General Information
Commentary
Reference
malfunction
an aglB deletion mutant is not flagellated. The pili of the DELTAaglB strain form thick bundles containing multiple filaments, and the lack of AglB-dependent glycosylation in this strain promotes microcolony formation
malfunction
wild-type cells are motile, mutant cells (with an insertional inactivation of the aglB gene) are non-motile. The mutant cells have detectable shifts in flagellin molecular weight. Thea are non-flaggelated, since only N-terminally processed flagellins can be assembled into flagella filaments
metabolism
the enzyme is involved in the transfer of the complete glycan to the flagellin and S-layer proteins
metabolism
the enzyme participates in the N-linked glycosylation in Methanococcus voltae. It catalyzes transfer of oligosaccharides from the dolichyl phosphate donor to asparagine in the acceptor proteins. Methanococcus voltae generates N-linked glycoproteins with a unique trisaccharide (L-threonyl 2-(acetylamino)-2-deoxy-beta-D-mannuronamido-(1->4)-2,3-bis(acetylamino)-2,3-bis(acetylamino)-2,3-dideoxy-beta-D-glucuronosyl-(1->3)-2-(acetylamino)-2-deoxy-beta-D-glucosyl-[protein]-L-asparagine)
physiological function
cells lacking glycotransferase AglB are unable to N-glycosylate the S-layer glycoprotein. The absence of AglB results in enhanced release of the S-layer glycoprotein. Haloferax volcanii AglB mutant cells grow significantly less well at elevated salt levels than do cells of the background strain
physiological function
enzyme can readily replace its counterpart from Haloferax volcanii when introduced into Haloferax volcanii cells deleted of glycotransferase aglB
physiological function
isoform AglB is essential for the viability of Sulfolobus acidocaldarius
Results 1 - 7 of 7