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Peptidoglycan hydrolysis and synthesis are two processes that must occur in order for cells to grow and multiply, a technique carried out in three stages: clipping of current material, insertion of new material, and re-crosslinking of existing material to new material.
Peptidoglycan is the major component of gram-positive bacterial cell wall. [1] This hydrolysis in turn compromises the integrity of bacterial cell walls causing lysis of the bacteria. Lysozyme is abundant in secretions including tears , saliva , human milk , and mucus .
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 ...
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.
Pseudopeptidoglycan (also known as pseudomurein; [2] PPG hereafter) is a major cell wall component of some Archaea that differs from bacterial peptidoglycan in chemical structure, but resembles bacterial peptidoglycan in function and physical structure.
In particular, peptidoglycan synthesis is vital to cell wall production, and inhibitors of peptidoglycan synthesis have been of clinical interest for targeting bacteria for many decades. [ 24 ] [ 25 ] Furthermore, the periplasm is also relevant to clinical developments by way of its role in mediating the uptake of transforming DNA .
The U.S. Food and Drug Administration (FDA) now classifies eggs as a “healthy, nutrient-dense" food, according to a new proposed rule. Registered dietitians react to the change.
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 ...