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Coordinate regulation of murein peptidase activity and AmpC β‐lactamase synthesis in Escherichia coli
Author(s) -
Bishop Russell E.,
Weiner Joel H.
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80598-b
Subject(s) - periplasmic space , escherichia coli , peptidoglycan , biochemistry , biology , peptide , serine , prolyl endopeptidase , endopeptidase , bacteria , microbiology and biotechnology , chemistry , enzyme , gene , genetics
In the periplasmic space of Escherichia coli , the ( l )‐ m ‐A 2 pm‐( d )‐ m ‐A 2 pm peptide, the lipoprotein, and the AmpC β‐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 β‐lactamase. As ld ‐peptides, dd ‐peptides and β‐lactams are structurally similar, ld ‐peptidases may belong to the larger family of dd ‐peptidases and serine β‐lactamases. In contrast to E. coli , many related bacteria possess an inducible AmpC protein. Several gene systems necessary for AmpC induction are known to affect various aspects of peptidoglycan metabolism. It is proposed that AmpC induction occurs indirectly via a recyclable cell wall peptide.