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426205

Sigma-Aldrich

β-Lactamase, Bacillus cereus 569/H9

Synonyme(s) :

β-Lactamase, Bacillus cereus 569/H9, Penicillinase

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About This Item

Numéro CAS:
9073-60-3
Numéro de classification (Commission des enzymes):
3.5.2.6 (BRENDA, IUBMB)
Numéro MDL:
MFCD00131819
Code UNSPSC :
12352202
Nomenclature NACRES :
NA.54

Source biologique

Bacillus sp. (Bacillus cereus)

Niveau de qualité

100

Forme

lyophilized

Conditionnement

vial of ≥50 units β-lactamase II
vial of ≥500 units β-lactamase I

Fabricant/nom de marque

Calbiochem®

Conditions de stockage

OK to freeze

Solubilité

sterile distilled water: soluble

Conditions d'expédition

ambient

Température de stockage

−20°C

Description générale

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.

Actions biochimiques/physiologiques

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).

Avertissement

Toxicity: Harmful (C)

Définition de l'unité

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.

Informations légales

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

Pictogrammes

Health hazard
GHS08

Mention d'avertissement

Danger

Mentions de danger

H317,H334

Classification des risques

Resp. Sens. 1 - Skin Sens. 1

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Nitrocefin A chromogenic β-lactamase substrate that undergoes distinctive color change from yellow as the amide bond in the β-lactam ring is hydrolyzed by β-lactamase.

Sigma-Aldrich

484400

Nitrocefin

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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