Journal article
Coordinate regulation of murein peptidase activity and AmpC β‐lactamase synthesis in Escherichia coli
Abstract
In the periplasmic space of Escherichia coli, the (L)-m-A2pm-(D)-m-A2pm peptide, the lipoprotein, and the AmpC beta-lactamase are controlled by growth rate. To explain this coordinate regulation, it is proposed that the AmpC protein functions as an LD-endopeptidase in addition to its known function as a beta-lactamase. As LD-peptides, DD-peptides and beta-lactams are structurally similar, LD-peptidases may belong to the larger family of …
Authors
Bishop RE; Weiner JH
Journal
FEBS Letters, Vol. 304, No. 2-3, pp. 103–108
Publisher
Wiley
Publication Date
June 15, 1992
DOI
10.1016/0014-5793(92)80598-b
ISSN
0014-5793