Open AccessActivity of penicillin-binding protein 3 from Escherichia coli
Author(s) -
Antonio G. Pisabarro,
Raimon M. Prats,
D Váquez,
Alfredo RodríguezTébar
Publication year - 1986
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.168.1.199-206.1986
Subject(s) - peptidoglycan , penicillin binding proteins , tripeptide , escherichia coli , biology , biochemistry , in vivo , penicillin , enzyme , microbiology and biotechnology , antibiotics , peptide , gene
The activity of penicillin-binding protein 3 of Escherichia coli has been studied both in vivo and in ether-permeabilized cells. The peptidoglycan transpeptidase activity of penicillin-binding protein 3 appears to use either nascent or exogenously added UDP-N-acetylmuramyl tripeptide-derived substrates as acceptors. By means of a defilamentation system which elicited the activity of penicillin-binding protein 3 in vivo, the structure of peptidoglycan made by this enzyme has been elucidated. This peptidoglycan, very probably of septal location, contained increased amounts of cross-linked peptidoglycan as well as a higher ratio of tripeptide-containing cross-linked subunits.