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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] This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases.
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).
Notch is an important protein in development, with several EGF domains that are O-fucosylated. [24] Changes in the elaboration of the core fucose determine what interactions the protein can form, and therefore which genes will be transcribed during development. O-fucosylation might also play a role in protein breakdown in the liver. [1]
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 ...
O-GlcNAcylation is the process of adding a single N-acetylglucosamine sugar to the serine or threonine of a protein. [4] Comparable to phosphorylation, addition or removal of N-acetylglucosamine is a means of activating or deactivating enzymes or transcription factors. [4]
The typical prokaryotic protein-sorting transpeptidase is characterized as a protease, but does not simply hydrolyze a peptide bond. Instead, the larger, N-terminal portion of the cleaved polypeptide is transferred onto another molecule, such as a precursor of the peptidoglycan cell wall in Gram-positive bacteria .
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.
Peptidoglycan recognition protein 2 (PGLYRP2) is an enzyme (EC 3.5.1.28), N-acetylmuramoyl-L-alanine amidase (NAMLAA), that hydrolyzes bacterial cell wall peptidoglycan and is encoded by the PGLYRP2 gene.