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. 1989 Sep;171(9):5194–5198. doi: 10.1128/jb.171.9.5194-5198.1989

A new beta-lactam-binding protein derived from penicillin-binding protein 3 of Escherichia coli.

R Prats 1, M Gomez 1, J Pla 1, B Blasco 1, J A Ayala 1
PMCID: PMC210340  PMID: 2670908

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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