Beta-lactamase
From Proteopedia
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{{STRUCTURE_3bm6| PDB=3bm6 | SIZE=400| SCENE=Beta-lactamase/Beta-lactamase/1|right|CAPTION=Beta-lactamase class D dimer complex with boronic acid derivative, [[3bm6]] }} | {{STRUCTURE_3bm6| PDB=3bm6 | SIZE=400| SCENE=Beta-lactamase/Beta-lactamase/1|right|CAPTION=Beta-lactamase class D dimer complex with boronic acid derivative, [[3bm6]] }} | ||
| - | '''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. | + | == 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.<br /> | ||
| + | *Class A are broad-spectrum<br /> | ||
| + | *Class B are metalloenzymes<br /> | ||
| + | *Class C are cephalosporinases<br /> | ||
| + | *Class D are cloxacilanases<br /> | ||
| + | *Carbapenemase (Car) are Blac with wide hydrolytic capacities. Car can hydrolyze penicillins, cephalosporins, monobactams and carbapenems. <br /> | ||
| + | *Extended-spectrum Blac class A (ESBL) hydrolyze penicillins but not cephalosporins. | ||
== Relevance == | == Relevance == | ||
Revision as of 10:47, 10 November 2015
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
- Class B are metalloenzymes
- Class C are cephalosporinases
- 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.
Relevance
Blac makes some bacteria resistant to antibiotics like penicillin, cephamycin and carbapenems.
3D Structures of Beta-lactamase
Updated on 10-November-2015
Proteopedia Page Contributors and Editors (what is this?)
Michal Harel, Jaime Prilusky, Alexander Berchansky, Joel L. Sussman
