EC Number   |
General Information |
Reference |
|---|
   2.4.99.21 | malfunction |
a strain deleted of aglB, encoding the archaeal oligosaccharyltransferase, is generated. In this DELTAaglB strain, archaella are not detected and only low levels of archaellins are released into the medium, in contrast to the parent strain. Mass spectrometry analysis of the archaellins in DELTAaglB cultures did not detect N-glycosylation. DELTAaglB cells showed a slight growth defect and are impaired for motility. N-glycosylation is important for archaellum assembly and cell motility in Halobacterium salinarum, as well as for archaellin gene transcription and translation |
-, 759232 |
| 2.4.99.21 | malfunction |
AglBs from Methanococcus voltae and Methanothermococcus thermolithotrophicus functionally replace the oligosaccharyltransferase activity missing in the Methanococcus maripaludis DELTAaglB strain, both returning the apparent molecular weight of archaellin FlaB2 to wild type size and restoring archaellation. Attempts to use AglB from Methanocaldococcus jannaschii, Haloferax volcanii or Sulfolobus acidocaldarius to functionally replace the oligosaccharyltransferase activity missing in the Methanococcus maripaludis DELTAaglB strain are unsuccessful |
-, 760021 |
| 2.4.99.21 | 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 |
738680 |
| 2.4.99.21 | 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 |
732528 |
| 2.4.99.21 | metabolism |
the enzyme is involved in the transfer of the complete glycan to the flagellin and S-layer proteins |
732528 |
| 2.4.99.21 | 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) |
732558 |
| 2.4.99.21 | 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 |
-, 758885, 758886 |
| 2.4.99.21 | 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 |
-, 734470 |
| 2.4.99.21 | physiological function |
enzyme can readily replace its counterpart from Haloferax volcanii when introduced into Haloferax volcanii cells deleted of glycotransferase aglB |
-, 726749 |
| 2.4.99.21 | physiological function |
isoform AglB is essential for the viability of Sulfolobus acidocaldarius |
-, 734650 |
