H
IPR012338

Beta-lactamase/transpeptidase-like

InterPro entry
Short nameBeta-lactam/transpept-like
Overlapping entries
 

Description

This superfamily represents a beta-lactamase structural motif, which contains a cluster of α-helices and an α/β sandwich. In addition to beta-lactamases, this domain is also found in D-ala carboxypeptidase/transpeptidase, esterase (EstB)
[2]
, the penicillin receptor BlaR (C-terminal domain), D-aminopeptidase (N-terminal domain)
[3]
, penicillin-biding proteins (e.g. PBP2x, PBP5), and in glutaminase (GlnA). Beta-lactamases are the most common bacterial resistance mechanism against beta-lactam antibiotics
[1]
. Beta-lactamases appear to have evolved from DD-transpeptidases, which are penicillin-binding proteins involved in cell wall biosynthesis, and as such are one of the main targets of beta-lactam antibiotics.

References

1.Understanding the acylation mechanisms of active-site serine penicillin-recognizing proteins: a molecular dynamics simulation study. Oliva M, Dideberg O, Field MJ. Proteins 53, 88-100, (2003). View articlePMID: 12945052

2.EstB from Burkholderia gladioli: a novel esterase with a beta-lactamase fold reveals steric factors to discriminate between esterolytic and beta-lactam cleaving activity. Wagner UG, Petersen EI, Schwab H, Kratky C. Protein Sci. 11, 467-78, (2002). View articlePMID: 11847270

3.Crystal structure of a D-aminopeptidase from Ochrobactrum anthropi, a new member of the 'penicillin-recognizing enzyme' family. Bompard-Gilles C, Remaut H, Villeret V, Prange T, Fanuel L, Delmarcelle M, Joris B, Frere J, Van Beeumen J. Structure 8, 971-80, (2000). View articlePMID: 10986464

Cross References

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