Beta Lactamase E.coli Recombinant
Recombinant E.coli Beta-Lactamase produced in E.Coli is a single, non-glycosylated polypeptide chain containing 264 amino acids and having a molecular mass of approximately 28.9 kDa.
Beta Lactamase is purified by proprietary chromatographic techniques.
Beta Lactamase E.coli Recombinant, His Tag
Beta Lactamase E.Coli Recombinant, His Active
LACTB produced in E.Coli is a single, non-glycosylated polypeptide chain containing 379 amino acids (20-377 a.a) and having a molecular mass of 41.8kDa.
LACTB is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Beta-lactamases are enzymes produced by bacteria that provide resistance to beta-lactam antibiotics such as penicillins, cephalosporins, cephamycins, and carbapenems by breaking the antibiotics’ structure . These enzymes are classified based on their molecular structure and functional characteristics. The Ambler classification divides beta-lactamases into four classes (A, B, C, and D) based on their amino acid sequences . Class A, C, and D enzymes utilize serine for beta-lactam hydrolysis, while class B metalloenzymes require divalent zinc ions for substrate hydrolysis . The Bush-Jacoby-Medeiros classification groups beta-lactamases according to functional similarities, such as substrate and inhibitor profiles .
Beta-lactamases exhibit diverse biological properties. They are encoded either on chromosomes or mobile genetic elements like plasmids . These enzymes are expressed in various bacterial species, including both Gram-positive and Gram-negative bacteria . The tissue distribution of beta-lactamases is primarily within the bacterial cell wall, where they act to neutralize beta-lactam antibiotics before they reach their target sites .
The primary biological function of beta-lactamases is to confer antibiotic resistance by hydrolyzing the beta-lactam ring of antibiotics, rendering them ineffective . This enzymatic activity plays a crucial role in the survival of bacteria in the presence of beta-lactam antibiotics. Beta-lactamases also contribute to pathogen recognition and immune evasion by modifying the bacterial cell wall structure .
Beta-lactamases act by breaking the beta-lactam ring of antibiotics through hydrolysis, which deactivates the antibiotic’s antibacterial properties . The enzymes interact with beta-lactam antibiotics, treating them as substrates and deacylating the complex . This interaction involves binding to penicillin-binding proteins (PBPs) and disrupting peptidoglycan synthesis, which is essential for bacterial cell wall integrity .
The expression and activity of beta-lactamases are regulated through various mechanismsTranscriptional regulation involves the induction of beta-lactamase genes in response to the presence of beta-lactam antibiotics . This induction can be mediated by liberated murein fragments, such as muropeptides, via pathways like the AmpG–AmpR–AmpC pathway and BlrAB-like two-component regulatory system Post-translational modifications also play a role in modulating the activity of beta-lactamases .
Beta-lactamases have significant applications in biomedical research, diagnostic tools, and therapeutic strategies. In research, they are used to study antibiotic resistance mechanisms and develop new antibiotics . Diagnostic tools utilize beta-lactamases to detect the presence of beta-lactamase-producing bacteria, aiding in the selection of appropriate antibiotic treatments . Therapeutically, beta-lactamase inhibitors are developed to counteract the resistance conferred by these enzymes, enhancing the efficacy of beta-lactam antibiotics .
Throughout the bacterial life cycle, beta-lactamases play a critical role in development, aging, and disease. During bacterial growth and division, beta-lactamases ensure survival by neutralizing beta-lactam antibiotics . In aging bacterial populations, the presence of beta-lactamases can contribute to the persistence of resistant strains . In the context of disease, beta-lactamases are pivotal in the pathogenesis of infections caused by resistant bacteria .