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
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
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.