Identification of BlaR, the signal transducer for beta-lactamase production in Bacillus licheniformis, as a penicillin-binding protein with strong homology to the OXA-2 beta-lactamase (class D) of Salmonella typhimurium.
AUTOR(ES)
Zhu, Y F
RESUMO
The blaR gene of Bacillus licheniformis encodes the signal transducer for induction of the class A beta-lactamase. The protein product, BlaR, has a hydrophilic carboxy region that binds beta-lactams and shows high sequence homology to the class D beta-lactamases, particularly the OXA-2 beta-lactamase of Salmonella typhimurium. The BlaR-beta-lactam complex is stable and may provide the continuing stimulus needed for the prolonged production of the enzyme.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=208548Documentos Relacionados
- Structure, function, and fate of the BlaR signal transducer involved in induction of beta-lactamase in Bacillus licheniformis.
- A second regulatory gene, blaR1, encoding a potential penicillin-binding protein required for induction of beta-lactamase in Bacillus licheniformis.
- Penem derivatives: beta-lactamase stability and affinity for penicillin-binding proteins in Escherichia coli.
- Immunological comparison between OXA-2 beta-lactamase and those mediated by other R plasmids.
- Penicillin-binding protein 2 is required for induction of the Citrobacter freundii class I chromosomal beta-lactamase in Escherichia coli.
