Search results
Results from the WOW.Com Content Network
In the first step of peptidoglycan synthesis, glutamine, which is an amino acid, donates an amino group to a sugar, fructose 6-phosphate. [20] This reaction, catalyzed by EC 2.6.1.16 (GlmS), turns fructose 6-phosphate into glucosamine-6-phosphate .
Lipid II is a precursor molecule in the synthesis of the cell wall of bacteria. It is a peptidoglycan, which is amphipathic and named for its bactoprenol hydrocarbon chain, which acts as a lipid anchor, embedding itself in the bacterial cell membrane. Lipid II must translocate across the cell membrane to deliver and incorporate its disaccharide ...
Divisome and elongasome complexes responsible for peptidoglycan synthesis during lateral cell-wall growth and division. [1]The divisome is a protein complex in bacteria that is responsible for cell division, constriction of inner and outer membranes during division, and peptidoglycan (PG) synthesis at the division site.
Like the peptidoglycan found in bacterial cell walls, pseudopeptidoglycan consists of polymer chains of glycan cross-linked by short peptide connections. However, unlike peptidoglycan, the sugar N-acetylmuramic acid is replaced by N-acetyltalosaminuronic acid, [42] and the two sugars are bonded with a β,1-3 glycosidic linkage instead of β,1-4.
This layered structure is called peptidoglycan (formerly called murein). GlcNAc is the monomeric unit of the polymer chitin, which forms the exoskeletons of arthropods like insects and crustaceans. It is the main component of the radulas of mollusks, the beaks of cephalopods, and a major component of the cell walls of most fungi.
The bacterial cell wall differs from that of all other organisms by the presence of peptidoglycan (poly-N-acetylglucosamine and N-acetylmuramic acid), which is located immediately outside of the cytoplasmic membrane. Peptidoglycan is responsible for the rigidity of the bacterial cell wall and for the determination of cell shape. It is ...
Peptidoglycan glycosyltransferase (EC 2.4.1.129) is an enzyme used in the biosynthesis of peptidoglycan. It transfers a disaccharide-peptide from a donor substrate to synthesize a glycan chain. [1] This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases.
Peptidoglycan binding domains have a general peptidoglycan binding function and a common core structure consisting of a closed, three-helical bundle with a left-handed twist. It is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation.