A new beta-lactam-binding protein derived from penicillin-binding protein 3 of Escherichia coli.
AUTOR(ES)
Prats, R
RESUMO
In this paper we describe a new beta-lactam-binding protein from the cell envelope of Escherichia coli. It can be detected in cells grown at either 37 or 42 degrees C in medium containing glucose but not in cells grown at 30 degrees C. This novel component has an apparent molecular size that is 2.0 kilodaltons larger than that of penicillin-binding protein 3 and is derived from the latter through a divalent-cation-mediated process probably catalyzed by components located in the periplasmic space. The significance of this protein with regard to regulation of the amount of functional penicillin-binding protein 3 in the cell is discussed.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=210340Documentos Relacionados
- Activity of penicillin-binding protein 3 from Escherichia coli.
- Effects of furazlocillin, a beta-lactam antibiotic which binds selectively to penicillin-binding protein 3, on Escherichia coli mutants deficient in other penicillin-binding proteins.
- Purification of penicillin-binding protein 2 of Escherichia coli.
- Improved sensitivity in assays for binding of novel beta-lactam antibiotics to penicillin-binding proteins of Escherichia coli.
- Identification of the active site in penicillin-binding protein 3 of Escherichia coli.