Beta-lactamase

From Proteopedia

Jump to: navigation, search

Contents

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


Class B β-lactamase Ndm-1 complex with Zn+2 (grey) (PDB code 3spu)

Drag the structure with the mouse to rotate

References

  1. Jacoby GA. AmpC beta-lactamases. Clin Microbiol Rev. 2009 Jan;22(1):161-82, Table of Contents. PMID:19136439 doi:10.1128/CMR.00036-08
  2. King D, Strynadka N. Crystal structure of New Delhi metallo-beta-lactamase reveals molecular basis for antibiotic resistance. Protein Sci. 2011 Sep;20(9):1484-91. doi: 10.1002/pro.697. Epub 2011 Aug, 2. PMID:21774017 doi:10.1002/pro.697

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Jaime Prilusky, Alexander Berchansky, Joel L. Sussman

Personal tools