EC Number   |
General Information |
Reference |
|---|
  2.4.1.B64 | evolution |
comparison of the sequence of MG1655, as the reference genome, and of parent strain ML115 reveals the presence of a 768-bp insertion sequence within lipopolysaccharide (LPS) glucosyltransferase I (WaaG). This mutation is implemented unintentionally during the development of ML115. LAR1 and LAR2 both have restored function of WaaG and a single amino acid change within the beta' subunit of RNA polymerase RpoC, and each has a unique mutation in the BasS-BasR two-component signal transduction system. The shared waaG and rpoC mutations are most likely due to the fact that these strains share a common ancestor |
759719 |
| 2.4.1.B64 | malfunction |
deletion of waaG has previously been reported to result in a truncated LPS core and loss of flagella. This is consistent with TEM imaging of our strains, in that flagella are visible for LAR1 but not for ML115. Restoration of WaaG increases membrane integrity and increases the membrane rigidity |
759719 |
| 2.4.1.B64 | malfunction |
mutation of the enzyme results in lipopolysaccharide truncated immediately after the inner core heptose residues, which serve as the sites for phosphorylation. Mutation of waaG also destabilized the outer membrane. Structural analyses of waaG mutant lipopolysaccharide shows that the cause for this phenotype is a decrease in core phosphorylation |
727735 |
| 2.4.1.B64 | more |
retaining GTs show a front-face catalytic mechanism. Glycosyltransferases GTs constitute a diverse class of enzymes that catalyze the formation of glycosidic bonds. GTs are highly versatile as they catalyze the transfer of sugar moieties from activated donor molecules to a vast amount of acceptor molecules but are at the same time highly specific for donor and acceptor molecules |
758841 |
| 2.4.1.B64 | physiological function |
glycosyltransferase WaaG is involved in the synthesis of lipopolysaccharides (LPS) in Gram-negative bacteria and is previously categorized as a monotopic glycosyltransferase (GT). Membrane-associated GTs have the peculiar property that they catalyze the formation of a glycosidic bond between a hydrophilic donor substrate and a lipid acceptor molecule. Moreover, peripheral GTs can either be membrane-bound or soluble. WaaG binds membranes via electrostatic interactions. There is no specific binding to anionic lipids. WaaG senses the anionic surface charge density of the membrane. The N- and C-terminal domains both associate to the lipid membrane with similar changes in fluorescence properties of a reporter Trp residue positioned in either the N-terminal or C-terminal domain. WaaG is a peripheral membrane protein |
758841 |
| 2.4.1.B64 | physiological function |
mutant strains lacking ADP-heptose-LPS heptosyltransferase 2, lipopolysaccharide heptosyltransferase 1 or glucosyltransferase WaaG only synthesize lipopolysaccharide with different lengths. Flagella are observed on the cell surface of the wild-type strain but not the mutant strains. 965genes in the WaaG deleltion mutant are significantly regulated compared to the control strain. Although there are significant transcriptional differences among the ADP-heptose-LPS heptosyltransferase 2, lipopolysaccharide heptosyltransferase 1 or glucosyltransferase mutant strains, genes related to flagella assembly and bacterial chemotaxis are significantly down-regulated in all three strains |
736375 |
| 2.4.1.B64 | physiological function |
the enzyme is involved in the synthesis of the core region of lipopolysaccharides in Escherichia coli |
727599 |
