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Peptidoglycan recognition is an evolutionarily conserved process. [25] The overall structure is similar between bacterial species, but various modifications can increase the diversity. These include modifications of the length of sugar polymers, modifications in the sugar structures, variations in cross-linking or substitutions of amino acids ...
It is a glycoside hydrolase that catalyzes the following process: Hydrolysis of (1→4)-β-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins. Peptidoglycan is the major component of gram-positive bacterial cell wall. [1]
The basic peptidoglycan structure of both Gram-positive and Gram-negative bacteria comprises a sheet of glycan chains connected by short cross-linking polypeptides. Biosynthesis of peptidoglycan is a multi-step (11-12 steps) process comprising three main stages: formation of UDP-N-acetylmuramic acid (UDPMurNAc) from N-acetylglucosamine (GlcNAc).
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 catalytic domain of the enzyme resides on the C-terminal region of the enzyme. OBPgp279 is also predicted to contain peptidoglycan binding domains; since OBPgp279 contains two peptidoglycan binding domain motifs in its N-terminal region (general sequence motif=D-G-(Pho)2-G-K/N-G/N-T, Pho = hydrophobic amino acid), it likely contains two peptidoglycan binding domains as shown in the ...
Many of these proteins are uncharacterised, but it has been proposed that they may function mainly in peptidoglycan hydrolysis. The CHAP domain is found in a wide range of protein architectures; it is commonly associated with bacterial type SH3 domains and with several families of amidase domains.
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Hydrolysis of peptidoglycan by PGLYRP2 diminishes peptidoglycan's pro-inflammatory activity. [ 31 ] [ 41 ] This effect is likely due to amidase activity of PGLYRP2, which separates the stem peptide from MurNAc in peptidoglycan and destroys the motif required for the peptidoglycan-induced activation of NOD2 (nucleotide-binding oligomerization ...