Open AccessPenicillin‐binding proteins in Mycobacterium smegmatis
Author(s) -
Yabu Kunihiko,
Ochiai Toshiro,
Kaneda Shunko
Publication year - 1984
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1984.tb01477.x
Subject(s) - penicillin binding proteins , mycobacterium smegmatis , mutant , cefmetazole , chemistry , antibiotics , penicillin , microbiology and biotechnology , biochemistry , cefoxitin , biology , bacteria , cephalosporin , gene , mycobacterium tuberculosis , genetics , pathology , staphylococcus aureus , medicine , tuberculosis
The penicillin‐binding proteins (PBPs) of Mycobacterium smegmatis were studied. Five PBPs ranging in M r from approx. 114000 to 25000 were detected in the cytoplasmic membrane. The affinities of the PBPs for selected β‐lactam antibiotics were determined. Most of the antibiotics bound to PBPs 3 and 4 at low concentrations. A penicillin‐susceptible mutant and a cefmetazole‐resistant mutant were isolated by selection in vitro. The PBPs of these mutants were identical to those of the parent strain. The affinity of cefmetazole for the individual PBPs was identical in each mutant.