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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 .
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.
Double-stranded DNA phage lysins tend to lie within the 25 to 40 kDa range in terms of size. A notable exception is the streptococcal PlyC endolysin, which is 114 kDa. PlyC is not only the biggest and most potent lysin, but also structurally unique since it is composed of two different gene products, PlyCA and PlyCB, with a ratio of eight PlyCB subunits for each PlyCA in its active conformation.
This degradation of the glycosidic bonds within peptidoglycan cause the sugars to separate and inhibit the structural integrity of the peptidoglycan and the bacteria. Pseudopeptidoglycan, however, is composed of a different acidic amino sugar, which is N-acetyltalosaminuronic acid.
PBPs, also known as transpeptidases, are targets for beta-lactams. These enzymes (PBPs) are involved in peptidoglycan synthesis which is a major component of the bacterial cell wall. PBPs cross-link the amino acid strands of peptidoglycan during synthesis. Normally, beta-lactams bind the PBPs and thereby inhibit the cross-linking of peptidoglycan.
Hydrolyzed protein is a solution derived from the hydrolysis of a protein into its component amino acids and peptides. While many means of achieving this process exist, the most common method is prolonged heating with hydrochloric acid, [1] sometimes with an enzyme such as pancreatic protease to simulate the naturally occurring hydrolytic process.
Peptidoglycan recognition proteins (PGRPs) are a group of highly conserved pattern recognition receptors with at least one peptidoglycan recognition domain capable of recognizing the peptidoglycan component of the cell wall of bacteria. They are present in insects, mollusks, echinoderms and chordates. The mechanism of action of PGRPs varies ...