426205
β-Lactamase, Bacillus cereus 569/H9
别名:
β-Lactamase, Bacillus cereus 569/H9, Penicillinase
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关于此项目
化学文摘社编号:
UNSPSC Code:
12352202
NACRES:
NA.54
MDL number:
Biological source:
Bacillus sp. (Bacillus cereus)
biological source
Bacillus sp. (Bacillus cereus)
description
Merck USA index - 14, 7093
form
lyophilized
packaging
vial of ≥50 units β-lactamase II, vial of ≥500 units β-lactamase I
manufacturer/tradename
Calbiochem®
storage condition
OK to freeze
solubility
sterile distilled water: soluble
shipped in
ambient
storage temp.
−20°C
Quality Level
General description
β-Lactamase produced by bacteria shares sequence homology to penicillin-binding proteins. This enzyme is found in Gram-negative bacteria. β-Lactamases have four molecular classes, named A, B, C, and D. A, C, and D form an acyl-enzyme via active site serine residue. Class B β-lactamases are metalloenzymes, which have a zinc ion at their active site for β-lactam hydrolysis.
Biochem/physiol Actions
β-Lactamase hydrolyzes β-lactum antibiotics and is the chief cause of resistance to β-lactam antibiotics development by bacteria. Mutations in the β-lactamases are associated with extended-spectrum β-lactamases (ESBLs).
Preparation Note
Following reconstitution, store in the refrigerator (4°C). Stock solutions are stable for up to 1 month at 4°C.
Other Notes
One unit is defined as the amount of enzyme that will hydrolyze 1.0 µmol benzyl penicillin and 1.0 µmol of cephalosporin C, respectively, per min at 25°C.
Legal Information
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
Disclaimer
Toxicity: Harmful (C)
signalword
Danger
hcodes
Hazard Classifications
Resp. Sens. 1 - Skin Sens. 1
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
监管及禁止进口产品
此项目有
Karen Bush et al.
Antimicrobial agents and chemotherapy, 54(3), 969-976 (2009-12-10)
Two classification schemes for beta-lactamases are currently in use. The molecular classification is based on the amino acid sequence and divides beta-lactamases into class A, C, and D enzymes which utilize serine for beta-lactam hydrolysis and class B metalloenzymes which
Sibhghatulla Shaikh et al.
Saudi journal of biological sciences, 22(1), 90-101 (2015-01-07)
Antibiotic resistance is a problem of deep scientific concern both in hospital and community settings. Rapid detection in clinical laboratories is essential for the judicious recognition of antimicrobial resistant organisms. Production of extended-spectrum β-lactamases (ESBLs) is a significant resistance-mechanism that
Karen Bush
Antimicrobial agents and chemotherapy, 62(10) (2018-08-01)
β-Lactamases, the major resistance determinant for β-lactam antibiotics in Gram-negative bacteria, are ancient enzymes whose origins can be traced back millions of years ago. These well-studied enzymes, currently numbering almost 2,800 unique proteins, initially emerged from environmental sources, most likely
P A Bradford
Clinical microbiology reviews, 14(4), 933-951 (2001-10-05)
Beta-lactamases continue to be the leading cause of resistance to beta-lactam antibiotics among gram-negative bacteria. In recent years there has been an increased incidence and prevalence of extended-spectrum beta-lactamases (ESBLs), enzymes that hydrolyze and cause resistance to oxyimino-cephalosporins and aztreonam.
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