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The AHLs are degraded by enzymes through three mechanisms: lactone hydrolysis, amide bond hydrolysis, and acyl chain modification. Lactone hydrolysis occurs when AHL Lactonase hydrolyzes homoserine lactone rings. This process was first observed in Bacillus species. AHL acylases catalyze the complete and irreversible destruction of AHLs through ...
acyl-[acyl-carrier protein] + S-adenosyl-L-methionine [acyl-carrier protein] + S-methyl-5'-thioadenosine + N-acyl-L-homoserine lactone Acyl-homoserine lactones (AHLs) are produced by a number of bacterial species and are used by them to regulate the expression of virulence genes in a process known as quorum-sensing .
Lactonase (EC 3.1.1.81, acyl-homoserine lactonase; systematic name N-acyl-L-homoserine-lactone lactonohydrolase) is a metalloenzyme, produced by certain species of bacteria, which targets and inactivates acylated homoserine lactones (AHLs). It catalyzes the reaction
Acyl halides are rather reactive compounds often synthesized to be used as intermediates in the synthesis of other organic compounds. For example, an acyl halide can react with: water, to form a carboxylic acid. This hydrolysis is the most heavily exploited reaction for acyl halides as it occurs in the industrial synthesis of acetic acid.
IAP has been considered to be associated with the emergence of resistant bacterial strains and with an increase in the incidence of early-onset infections caused by other pathogens, mainly Gram-negative bacteria such as Escherichia coli. Nevertheless, most studies have not found an increased rate of non-GBS early-onset sepsis related to the ...
The difference between the PBPs and SBLs is that the latter generates free enzyme and inactive antibiotic by the very quick hydrolysis of the acyl-enzyme intermediate. [citation needed] The MBLs use the Zn 2+ ions to activate a binding site water molecule for the hydrolysis of the β-lactam ring. Zinc chelators have recently been investigated ...
Chemical structure of lipid A as found in E. coli [1]. Lipid A is a lipid component of an endotoxin held responsible for the toxicity of gram-negative bacteria.It is the innermost of the three regions of the lipopolysaccharide (LPS), also called endotoxin molecule, and its hydrophobic nature allows it to anchor the LPS to the outer membrane. [2]
S. pyogenes is a species of beta-hemolytic Gram-positive bacteria that is responsible for a wide range of infections that are mostly common and fairly mild. If the bacteria enters the bloodstream, the infection can become severe and life-threatening, and is called an invasive GAS (iGAS). [2] [3]