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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 ]
Peptidoglycan or murein is a unique large macromolecule, a polysaccharide, consisting of sugars and amino acids that forms a mesh-like layer (sacculus) that surrounds the bacterial cytoplasmic membrane. [1] The sugar component consists of alternating residues of β-(1,4) linked N-acetylglucosamine (NAG) and N-acetylmuramic acid (NAM).
Most glycosyltransferase enzymes form one of two folds: GT-A or GT-B. Glycosyltransferases (GTFs, Gtfs) are enzymes that establish natural glycosidic linkages.They catalyze the transfer of saccharide moieties from an activated nucleotide sugar (also known as the "glycosyl donor") to a nucleophilic glycosyl acceptor molecule, the nucleophile of which can be oxygen- carbon-, nitrogen-, or sulfur ...
Common O-GalNAc core structures; Core 1, Core 2 and poly-N-acetyllactosamine structures. Addition of N-acetylgalactosamine (GalNAc) to a serine or threonine occurs in the Golgi apparatus, after the protein has been folded. [1] [6] The process is performed by enzymes known as GalNAc transferases (GALNTs), of which there are 20 different types. [6]
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-pentapeptide "building block" into the peptidoglycan mesh.
The phosphoryl group on PEP is eventually transferred to the imported sugar via several proteins. The phosphoryl group is transferred to the Enzyme E I (EI), Histidine Protein (HPr, Heat-stable Protein) and Enzyme E II (EII) to a conserved histidine residue, whereas in the Enzyme E II B (EIIB) the phosphoryl group is usually transferred to a cysteine residue and rarely to a histidine.
Transpeptidase may refer to: DD -Transpeptidase , a bacterial enzyme that cross-links the peptidoglycan chains to form rigid cell walls Gamma-glutamyl transpeptidase , a liver enzyme
The basic components are N-acetylglucosamine and N-acetyltalosaminuronic acid (bacterial peptidoglycan containing N-acetylmuramic acid instead), which are linked by β-1,3-glycosidic bonds. [ 3 ] Lysozyme , a host defense mechanism present in human secretions (e.g. saliva and tears) breaks β-1,4-glycosidic bonds to degrade peptidoglycan.