EC Number   |
General Information |
Reference |
|---|
  2.4.1.289 | malfunction |
the temperature-sensitive mc2155 strain 2-20/32 mutant shows loss of this transferase activity in 2-20/32 at elevated temperatures, complementation by expression of the enzyme encoded by genes wbbL from Escherichia coli and froms Mycobacterium tuberculosis |
-, 719822 |
| 2.4.1.289 | metabolism |
PglA is part of a general N-linked glycosylation pathway, encoded by the pgl gene cluster, which culminates in the transfer of a heptasaccharide: GalNAc-alpha1,4-GalNAc-alpha1,4-(Glcbeta1,3)-GalNAc-alpha1,4-GalNAc-alpha1,4-GalNAc-alpha1,3-Bac, where Bac is bacillosamine (2,4-diacetamido-2,4,6-trideoxyglucose), from a membrane-anchored undecaprenyldiphosphate-linked donor to the asparagine side chain of proteins at the Asn-X-Ser/Thr motif. The glycosyltransferases, PglA, PglH, PglI, and PglJ, responsible for the biosynthesis of the Und-PP-linked heptasaccharide. PglA adds the first GalNAc residue on to the isoprenoid-linked Bac carrier |
-, 720888 |
| 2.4.1.289 | metabolism |
the Pgl pathway produces the N-linked glycan heptasaccharide GalNAc-alpha1,4-GalNAc-alpha1,4-(Glcbeta1,3)-GalNAc-alpha1,4-GalNAc-alpha1,4-GalNAc-alpha1,3-Bac2,4diNAc-_1-Asn. The pathway begins with diphosphate bond formation between the Bac2,4diNAc phosphate and undecaprenylphosphate (Und-P) by Cj1124c (PglC) to form Bac2,4diNAc-alpha1-PP-Und. One N-acetylgalactosamine (GalNAc) is linked to the polyisoprenediphosphate-bound N,N'-diacetylbacillosamine by Cj1125c (PglA) to form GalNAc-alpha1,3-Bac2,4diNAc-alpha1-PP-Und. Next, four additional GalNAc and one branching glucose are added sequentially to the isoprene-linked disaccharide by PglJ, PglH, and PglI, to form the heptasaccharide, overview |
-, 714160 |
| 2.4.1.289 | physiological function |
gene RmlT is part of the rmlABCD locus encoding the biosynthetic pathway for L-rhamnose. Transferase RmlT is required for the incorporation of L-rhamnose into wall teichoic acids. Wall teichoic acids isolated from bacteria lacking RmlT display a faster migration in gel and do not contain any trace of L-rhamnose. The presence of L-rhamnosylated wall teichoic acids at the surface of Listeria monocytogenes delays the crossing of the cell wall by antimicrobial peptides and postpones their contact with the listerial membrane. Wall teichoic acids L-rhamnosylation promotes Listeri monocytogenes survival by decreasing the cell wall permeability to antimicrobial peptides, thus hindering their access and detrimental interaction with the plasma membrane |
737149 |
| 2.4.1.289 | physiological function |
the enzyme is required for the rhamnosyl-L-containing linker unit responsible for the attachment of the cell wall polymer mycolyl-arabinogalactan to the peptidoglycan in mycobacteria |
-, 719822 |
| 2.4.1.289 | physiological function |
WbbL catalyzes the transfer of an alpha-L-rhamnopyranose residue from dTDP-Rha to decaprenyldiphosphoryl-alpha-D-N-acetyl glucosamine, GlcNAc-P-PDP, to form alpha-L-Rhap-(1->3)-alpha-D-GlcNAc-P-P-DP, which is then further elongated with Galf and Araf units and finally mycolylated and attached to the peptidoglycan. The enzyme is essential for Mycobacterium tuberculosis viability and is absent in eukaryotic cells |
-, 720385 |
