Biochemical characterization of the metallo-beta-lactamase CcrA from Bacteroides fragilis TAL3636.
AUTOR(ES)
Yang, Y
RESUMO
The CcrA beta-lactamase from Bacteroides fragilis TAL3636 was cloned into Escherichia coli and purified from inclusion bodies. This group 3 metalloenzyme hydrolyzed most beta-lactam antibiotics, including cephamycins and carbapenems. Following inhibition by chelators, enzyme activity was recovered with the cations Zn2+ and Co2+. Clavulanate and sulbactam were activators; tazobactam at 10 microM inactivated the enzyme.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=188856Documentos Relacionados
- Cloning and sequencing of the class B beta-lactamase gene (ccrA) from Bacteroides fragilis TAL3636.
- Biochemical properties and purification of metallo-beta-lactamase from Bacteroides fragilis.
- Dsb-insensitive expression of CcrA, a metallo-beta-lactamase from Bacteroides fragilis, in Escherichia coli after amino acid substitution at two cysteine residues within CcrA.
- Purification of metallo-B-lactamase CcrA from Bacteroides fragilis with salting-out method
- A novel integron-like element carrying the metallo-beta-lactamase gene blaIMP.