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Key Documents

426205

Sigma-Aldrich

β-Lactamase, Bacillus cereus 569/H9

Synonyma:

β-Lactamase, Bacillus cereus 569/H9, Penicillinase

Přihlásitk zobrazení cen stanovených pro organizaci a smluvních cen


About This Item

Číslo CAS:
Číslo enzymu podle klasifikace EK:
MDL number:
UNSPSC Code:
12352202
NACRES:
NA.54

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

pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1 - Skin Sens. 1

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


Osvědčení o analýze (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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