Open AccessMajor peptidoglycan transglycosylase activity in Streptococcus pneumoniae that is not a penicillin‐binding protein
Author(s) -
Park Wan,
Seto Hiroyuki,
Hakenbeck Regine,
Matsuhashi Michio
Publication year - 1985
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.1574-6968.1985.tb01635.x
Subject(s) - peptidoglycan , penicillin binding proteins , micrococcus luteus , microbiology and biotechnology , streptococcus pneumoniae , escherichia coli , staphylococcus aureus , biology , streptococcaceae , lipid ii , penicillin , enterobacteriaceae , biochemistry , bacteria , cell wall , antibiotics , genetics , gene
As in the Gram‐positive cocci Staphylococcus aureus and Micrococcus luteus , which divide in 3 planes, Streptococcus pneumoniae , which divides on 1 fixed plane, possesses peptidoglycan transglycosylase activity that lacks penicillin‐binding activity as the sole detectable transglycosylase activity in vitro. The penicillin‐binding proteins (PBPs) in this organism did not show transglycosylase activity under the conditions in which the PBPs of Escherichia coli showed both transglycosylase and transpeptidase activities.