PROSITE documentation PDOC00606Beta-lactamases class B signatures
β-lactamases (EC 3.5.2.6) [1,2] are enzymes which catalyze the hydrolysis of an amide bond in the β-lactam ring of antibiotics belonging to the penicillin/cephalosporin family. Four kinds of β-lactamase have been identified [2]. Class-B enzymes are zinc containing proteins whilst class -A, C and D enzymes are serine hydrolases. Class-B β-lactamases have been described in several Gram-negative bacterial species; they seem to share the characteristic of being able to hydrolyze carbapenem compounds which are new β-lactam antibiotics of great therapeutic potential.
There are a number of conserved regions in the sequence of known class-B β-lactamases [3]. Most of them are centered on residues known [4] to be involved in binding the zinc ion essential for the enzyme's catalytic activity. We designed two signature patterns for this class of enzyme. The first contains three residues involved in binding zinc ions. The second pattern contains a cysteine which is also a zinc ligand.
Last update:April 2003 / Patterns and text revised.
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PROSITE methods (with tools and information) covered by this documentation:
| 1 | Authors | Ambler R.P. |
| Title | The structure of beta-lactamases. | |
| Source | Philos. Trans. R. Soc. Lond., B, Biol. Sci. 289:321-331(1980). | |
| PubMed ID | 6109327 |
| 2 | Authors | Bush K. |
| Title | Characterization of beta-lactamases. | |
| Source | Antimicrob. Agents Chemother. 33:259-263(1989). | |
| PubMed ID | 2658779 |
| 3 | Authors | Osano E. Arakawa Y. Wacharotayankun R. Ohta M. Horii T. Ito H. Yoshimura F. Kato N. |
| Title | Molecular characterization of an enterobacterial metallo beta-lactamase found in a clinical isolate of Serratia marcescens that shows imipenem resistance. | |
| Source | Antimicrob. Agents Chemother. 38:71-78(1994). | |
| PubMed ID | 8141584 |
| 4 | Authors | Concha N.O. Rasmussen B.A. Bush K. Herzberg O. |
| Title | Crystal structure of the wide-spectrum binuclear zinc beta-lactamase from Bacteroides fragilis. | |
| Source | Structure 4:823-836(1996). | |
| PubMed ID | 8805566 |
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