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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).
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 ...
Addition of a fucose alone creates the H-antigen, present in people with blood type O. [6] By adding a galactose onto this structure, the B-antigen of blood group B is created. Alternatively, adding a GalNAc sugar will create the A-antigen for blood group A. PSGL-1 has several O-glycans to extend the ligand away from the cell surface.
Lysozyme (EC 3.2.1.17, muramidase, N-acetylmuramide glycanhydrolase; systematic name peptidoglycan N-acetylmuramoylhydrolase) is an antimicrobial enzyme produced by animals that forms part of the innate immune system. It is a glycoside hydrolase that catalyzes the following process:
GLUT4 has a Km value for glucose of about 5 mM, which as stated above is the normal blood glucose level in healthy individuals. GLUT4 is the most abundant glucose transporter in skeletal muscle and is thus considered to be rate limiting for glucose uptake and metabolism in resting muscles. [ 8 ]
Lipid II is the final intermediate in peptidoglycan synthesis. It is formed when the MurG transferase catalyzes addition of N-acetylglucosamine (GlcNAc) to Lipid I, resulting in a complete disaccharide-pentapeptide monomer with a bactoprenol-pyrophosphate anchor. This occurs on the inside of the cytoplasmic membrane, where the bactoprenol chain ...
It is involved in bacterial cell wall biosynthesis, namely, the transpeptidation that crosslinks the peptide side chains of peptidoglycan strands. [ 3 ] The antibiotic penicillin irreversibly binds to and inhibits the activity of the transpeptidase enzyme by forming a highly stable penicilloyl-enzyme intermediate. [ 4 ]