Name | β-LactaMase |
Synonyms | cefinase β-LactaMase beta-lactamas Lactamase, beta- Metal-β-Lactamase CENTA B-LACTAMASE SUBSTRATE lactalbumin enzymatic hydrolysate*edamin S |
CAS | 9073-60-3 |
EINECS | 232-970-8 |
Boling Point | 55 °C |
Appearance | powder |
Color | white |
Merck | 7093 |
Storage Condition | 2-8°C |
Hazard Symbols | Xn - Harmful |
Risk Codes | 42/43 - May cause sensitization by inhalation and skin contact. |
Safety Description | S22 - Do not breathe dust. S36 - Wear suitable protective clothing. |
WGK Germany | 3 |
RTECS | OD2265000 |
overview
The hydrolase that can lyse the β-lactam ring of cyanotoxin and cephalosporin antibiotics to inactivate them is called β-lactamase. Penicillin as the substrate is called penicillinase, and cephalosporin as the substrate is called cephalosporinase. According to the matrix specificity of β-lactamase, it can be roughly divided into three categories: penicillinase, cephalosporin enzyme, and oxime cephalosporin enzyme. Penicillinase is easy to decompose penicillin antibiotics, cephalosporin enzymes have higher activity in decomposing cephalosporin antibiotics, and oxime cephalosporins have a decomposition effect on penicillin and cephalosporins, especially It is easier to decompose oxime cephalosporins. The genetic factors that produce penicillinase are mainly based on the cytosomal DNA, while the genetic factors that produce cephalosporins and oxime-type cephalosporins are mostly on the host chromosome. Penicillinase can be divided into 5 types (I. e. penicillinase I, II, III, IV, V) according to its basic characteristics or biochemical characteristics of the enzyme. Cephalosporinase and oxime type cephalosporinase belong to the unique enzymes of the strain. The refined products of these enzymes and the immune test of rabbits can obtain antibodies. However, various types of β-lactamases do not cross each other in their unique immunology.
features
The effect of β-lactamase on antibiotics mainly includes hydrolysis and non-hydrolysis [4]. Most of the active sites of β-lactamases have a longitudinal groove-like structure, which is loose and easy to bend, which is conducive to the binding of substrates. The carbonyl carbon on the antibiotic β-lactam ring can irreversibly bind to the serine at the active site, unraveling the antibiotic β-lactam ring, causing antibiotic degradation and avoiding the detection of antibiotics. Other antibiotics, such as metalloenzymes, use divalent metal ions to bind to histidine or cysteine, and interact with the amide bond in the antibiotic carbonyl group to inhibit the effect of antibiotics and avoid the detection of antibiotics. At present, the international research is more active in the broader spectrum β-lactamase and cephalosporin enzyme.