Enzimi nelle Proteine Ricombinanti

<p>OXA-11 is a β-lactamase enzyme, which is a type of protein produced by certain bacteria. These enzymes are derived from the bacterial source and are responsible for antibiotic resistance. The primary mode of action of OXA-11 is the hydrolysis of the β-lactam ring found in various antibiotics, such as penicillins and cephalosporins, rendering them ineffective. This enzymatic activity allows bacteria to survive exposure to these antimicrobial agents, posing a significant challenge in clinical settings.</p>

<p>Enolase (phosphopyruvate hydratase, EC 4.2.1.11) is an enzyme that catalyses the following reaction:  2-phospho-D-glycerate ⇌ phosphoenolpyruvate + H2O  One unit of enolase will convert 1.0 μmole of 2-phosphoglycerate to phosphoenolpyruvate per minute.</p>

<p>LacBuster®-S 50 is a solid and Gamma-irradiated, freeze-dried, broad range beta-lactamase formulation with 50 IU beta-lactamase II and 500 IU beta-lactamase I activity per vial.</p>

<p>KPC-1 (β-Lactamase) is an enzyme that breaks down β-lactam antibiotics, rendering them ineffective. It originates from strains of bacteria, particularly Klebsiella pneumoniae, which are significant sources of hospital-acquired infections. The mode of action involves hydrolyzing the β-lactam ring found in antibiotics such as penicillins and cephalosporins, neutralizing their antibacterial effects.</p>

<p>VIM-15 (β-Lactamase) is a metallo-β-lactamase enzyme, which is derived from bacterial sources, particularly Gram-negative bacteria. Its mode of action involves the hydrolysis of β-lactam antibiotics, facilitating bacterial resistance. This enzyme employs zinc ions as cofactors to break the β-lactam ring, rendering these antibiotics ineffective against the bacteria that produce the enzyme. The hydrolysis process disrupts the antibiotic's structural integrity, crucial for its antibacterial activity, thereby nullifying its therapeutic effects.</p>

<p>Carboxypeptidase G (EC 3.4.17.11, alternative name γ-Glutamyl hydrolase) is a protease that cuts γ-glutamyl bonds with high specificity. One unit of Carboxypeptidase G will hydrolyze (+)amethopterin to generate 1.0 μmole of L-glutamic acid.</p>

<p>beta lactamase I activity - min. 600.0 IU/mg</p>

<p>VIM-15 (β-Lactamase) is an enzyme product, specifically a metallo-beta-lactamase, which is sourced from certain resistant bacterial strains. This enzyme functions by hydrolyzing the beta-lactam ring of antibiotics, rendering them ineffective. The primary mode of action involves the coordination of zinc ions at its active site, enabling the breakdown of a broad spectrum of beta-lactam antibiotics including penicillins, cephalosporins, and carbapenems. This enzymatic activity significantly contributes to antibiotic resistance, posing a challenge in the treatment of bacterial infections. Its prevalence is noted in healthcare settings, where multidrug-resistant organisms are a concern. VIM-15 is of particular interest in clinical microbiology research and antimicrobial resistance studies, where understanding its structure and function can aid in the development of new inhibitors, potentially restoring the efficacy of beta-lactam antibiotics against resistant strains. Its characterization and study are critical for developing strategies to combat antibiotic-resistant infections effectively.</p>

<p>NMCA (β-Lactamase) is an enzyme, specifically acclaimed for its role in conferring antibiotic resistance. It is derived from bacterial sources, where it naturally occurs as part of the bacterial defense mechanism against β-lactam antibiotics. NMCA (β-Lactamase) functions by hydrolyzing the β-lactam ring present in these antibiotics, effectively rendering them inactive. This mode of action disrupts the antibiotic's ability to inhibit cell wall synthesis within bacteria, thereby permitting bacterial survival and proliferation.</p>

<p>Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces. Lipases/esterases can be used as versatile tools in hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications.</p>

<p>KPC-1 (β-Lactamase) is a specialized enzyme, which is produced by certain Gram-negative bacteria, notably Klebsiella pneumoniae. It functions by hydrolyzing the β-lactam ring found in a wide range of β-lactam antibiotics, such as penicillins and cephalosporins. This enzymatic action effectively neutralizes the antibiotic's antimicrobial properties, rendering the drugs ineffective against bacteria that produce KPC-1.</p>

<p>SPM-1 (β-Lactamase) is a metallo-β-lactamase enzyme, which is derived from certain Gram-negative bacteria, such as Pseudomonas aeruginosa. This enzyme is characterized by its ability to hydrolyze a broad spectrum of β-lactam antibiotics, including penicillins, cephalosporins, and carbapenems, due to the presence of a zinc ion in its active site. The zinc ion plays a crucial role in the catalytic mechanism by facilitating the cleavage of the β-lactam ring, rendering the antibiotic ineffective against bacterial cell wall synthesis.</p>

<p>Ready to use beta-lactamase solution targeting beta-lactam antibiotics such as penicillins, carbapenems and cephalosporins. According to US Pharmacopeia (USP &lt;71&gt;) and EP, LacBusterTM-L is suitable for sterility testing methods such as membrane filtration and direct inoculation.beta lactamase I activity - min. 25.0 IU/mLbeta lactamase II activity - min. 10.0 IU/mL</p>

<p>OXA-11 (β-Lactamase) is an enzyme of the β-lactamase class, which is primarily derived from Gram-negative bacteria. This enzyme is characterized by its ability to hydrolyze β-lactam antibiotics, rendering them ineffective by breaking the β-lactam ring, a crucial component of these antibiotics. OXA-11 is a notable member of the oxacillinase group within class D β-lactamases, known for its resistance to penicillins and cephalosporins.</p>

<p>CalB 02 is a lipase enzyme, which is a biocatalyst derived from the yeast Candida antarctica. It functions primarily by catalyzing the hydrolysis of ester bonds. This enzymatic action is due to the unique structure of the active site, which allows for precise substrate specificity and stereoselectivity.</p>

<p>Glucosyltransferase211-freeze dried is an enzyme preparation which is derived from microbial fermentation. This enzyme functions by catalyzing the transfer of glucosyl groups from activated donor molecules to specific acceptor substrates. Its mechanism of action involves the formation of glycosidic bonds, facilitating the synthesis of various oligosaccharides and polysaccharides.</p>

<p>Glucosyltransferase204-freeze dried is an enzyme preparation, derived from specific strains of Streptococcus bacteria, which plays a crucial role in catalyzing the transfer of glucosyl units from donor molecules to acceptor carbohydrates, predominantly in the formation of glucans. This enzymatic activity results in complex carbohydrate structures essential for various biological processes.</p>

<p>Glucosyltransferase227-freeze dried is an enzyme-derived product, originating from microbial sources known for its role in catalyzing the transfer of glucose moieties from a donor molecule to specific acceptor molecules. The enzyme operates by facilitating covalent bond formation between glucose and target substrates, displaying specificity that can be exploited in various biochemical pathways.</p>

<p>Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces. Lipases/esterases can be used as versatile tools in hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications.</p>

<p>Carboxypeptidase P (EC 3.4.17.16, also Membrane Pro-Xaa carboxypeptidase, microsomal carboxypeptidase) is a C-terminal exopeptidase, that preferentially cuts at C-terminal amino acid next to proline: ~-Pro-X → ~-Pro + X.</p>