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PMID: 3531167 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Activity of penicillin-binding protein 3 from Escherichia coli.

Journal of bacteriology ·Vol. 168 ·No. 1 ·1986-10-00 ·Pages 199-206

Pisabarro AG, Prats R, Váquez D, Rodríguez-Tébar A

Abstract

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.

MeSH Terms
Acyltransferases/metabolism Aztreonam/metabolism,pharmacology Bacterial Proteins Carrier Proteins Cycloserine/pharmacology Escherichia coli/analysis,drug effects,enzymology Escherichia coli Proteins Hexosyltransferases/metabolism Multienzyme Complexes/metabolism Muramoylpentapeptide Carboxypeptidase Penicillin-Binding Proteins Peptidoglycan/analysis,biosynthesis Peptidoglycan Glycosyltransferase Peptidyl Transferases/metabolism Temperature
Chemicals
Bacterial Proteins Carrier Proteins Escherichia coli Proteins FtsI protein, E coli Multienzyme Complexes Penicillin-Binding Proteins Peptidoglycan Cycloserine Acyltransferases Peptidyl Transferases Hexosyltransferases Peptidoglycan Glycosyltransferase Muramoylpentapeptide Carboxypeptidase Aztreonam
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Pisabarro A G
Prats R
Váquez D
Rodríguez-Tébar A
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30 references, click to expand
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
DOI
10.1128/jb.168.1.199-206.1986
Published
1986-10-00
Pages
199-206
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC213438
Subset
IM
External Links
PubMed source DOI: 10.1128/jb.168.1.199-206.1986 PMC Full Text View journal details
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