426205
β-Lactamase, Bacillus cereus 569/H9
Synonym(s):
β-Lactamase, Bacillus cereus 569/H9, Penicillinase
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About This Item
CAS Number:
MDL number:
UNSPSC Code:
12352202
NACRES:
NA.54
Recommended Products
biological source
Bacillus sp. (Bacillus cereus)
Quality Level
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
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).
Warning
Toxicity: Harmful (C)
Unit Definition
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.
Reconstitution
Following reconstitution, store in the refrigerator (4°C). Stock solutions are stable for up to 1 month at 4°C.
Legal Information
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1 - Skin Sens. 1
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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Customers Also Viewed
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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