Beta-lactamase

Function

Beta-lactamase (Blac) are enzymes which make bacteria resistant to β-lactam antibiotics by breaking their β-lactam ring. Blac are classified according to their resistance targets.

• Class A are broad-spectrum. See also TEM1 Class Antibiotic Resistance Proteins.
  
• Class B are metalloenzymes. See also New Delhi metallo-β-lactamase 1.
  
• Class C are cephalosporinases. See also Class C beta-lactamase.
  
• Class D are cloxacilanases
  
• Carbapenemase (Car) are Blac with wide hydrolytic capacities. Car can hydrolyze penicillins, cephalosporins, monobactams and carbapenems.
  
• Extended-spectrum Blac class A (ESBL) hydrolyze penicillins but not cephalosporins.
  
• Serine beta-lactamase (ClbP) has a serine-active site.
• AmpC beta-lactamase (ClbP) mediate resistance to cephalosphin, cefazolin,cefoxitin and most penicillins^[1].

Relevance

Blac makes some bacteria resistant to antibiotics like penicillin, cephamycin and carbapenems.

Structural highlights

The active site of class B Blac contains 2 Zn+2 ions.^[2]

See also

Journal:Structure:1

3D Structures of Beta-lactamase

Beta-lactamase 3D structures