426205
β-Lactamase, Bacillus cereus 569/H9
Sinônimo(s):
β-Lactamase, Bacillus cereus 569/H9, Penicillinase
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About This Item
Número CAS:
Número MDL:
Código UNSPSC:
12352202
NACRES:
NA.54
Produtos recomendados
fonte biológica
Bacillus sp. (Bacillus cereus)
Nível de qualidade
forma
lyophilized
embalagem
vial of ≥50 units β-lactamase II
vial of ≥500 units β-lactamase I
fabricante/nome comercial
Calbiochem®
condição de armazenamento
OK to freeze
solubilidade
sterile distilled water: soluble
Condições de expedição
ambient
temperatura de armazenamento
−20°C
Descrição geral
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.
Ações bioquímicas/fisiológicas
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).
Advertência
Toxicity: Harmful (C)
Definição da unidade
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.
Reconstituição
Following reconstitution, store in the refrigerator (4°C). Stock solutions are stable for up to 1 month at 4°C.
Informações legais
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
Palavra indicadora
Danger
Frases de perigo
Declarações de precaução
Classificações de perigo
Resp. Sens. 1 - Skin Sens. 1
Código de classe de armazenamento
11 - Combustible Solids
Classe de risco de água (WGK)
WGK 3
Ponto de fulgor (°F)
Not applicable
Ponto de fulgor (°C)
Not applicable
Certificados de análise (COA)
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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
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 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
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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