THE MONOFUNCTIONAL GLYCOSYLTRANSFERASE OF ESCHERICHIA-COLI IS A MEMBER OF A NEW CLASS OF PEPTIDOGLYCAN-SYNTHESIZING ENZYMES - OVEREXPRESSION AND DETERMINATION OF THE GLYCAN-POLYMERIZING ACTIVITY

Citation
M. Diberardino et al., THE MONOFUNCTIONAL GLYCOSYLTRANSFERASE OF ESCHERICHIA-COLI IS A MEMBER OF A NEW CLASS OF PEPTIDOGLYCAN-SYNTHESIZING ENZYMES - OVEREXPRESSION AND DETERMINATION OF THE GLYCAN-POLYMERIZING ACTIVITY, FEBS letters, 392(2), 1996, pp. 184-188
Citations number
23
Categorie Soggetti
Biophysics,Biology
Journal title
ISSN journal
00145793
Volume
392
Issue
2
Year of publication
1996
Pages
184 - 188
Database
ISI
SICI code
0014-5793(1996)392:2<184:TMGOEI>2.0.ZU;2-R
Abstract
Using conserved fingerprints in the glycosyltransferase (GTase) domain of high-molecular-weight penicillin-binding proteins (PBP), a gene (m gt) encoding a putative monofunctional glycosyltransferase has been id entified in Haemophilus influenzae and in other bacterial species. Her e we report the cloning of the homologous Esclterichia coli gene and s how that the solubilised membrane fraction of E. coli cells overexpres sing the mgt gene contain a significantly increased peptidoglycan synt hesis activity. In contrast to the high-molecular-weight PBPs, this ac tivity is not inhibited by Flavomycin.