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[1] [2] Peptidoglycan serves a structural role in the bacterial cell wall, giving structural strength, as well as counteracting the osmotic pressure of the cytoplasm. This repetitive linking results in a dense peptidoglycan layer which is critical for maintaining cell form and withstanding high osmotic pressures, and it is regularly replaced by ...
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.
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:
The lysin catalytic domain digests peptidoglycan locally at a high rate, which causes holes in the cell wall. Since the cross-linked peptidoglycan cell wall is the only mechanism that prevents the spontaneous burst of bacterial cells due to the high internal pressure (3 to 5 atmospheres), enzymatic digestion by lysins irreversibly causes ...
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 ...
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 first PGRP was discovered in 1996 by Masaaki Ashida and coworkers, who purified a 19 kDa protein present in the hemolymph and cuticle of a silkworm (Bombyx mori), and named it Peptidoglycan Recognition Protein, because it specifically bound peptidoglycan and activated the prophenoloxidase cascade. [5]
PBPs normally catalyze the cross-linking of the bacterial cell wall, but they can be permanently inhibited by penicillin and other β-lactam antibiotics. (NAM = N-acetylmuramic acid; NAG = N-acetylglucosamine) [2] Penicillin-binding proteins (PBPs) are a group of proteins that are characterized by their affinity for and binding of penicillin.