Reference : Glycosyl transferase activity of the Escherichia coli penicillin-binding protein 1b: Spe...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/13684
Glycosyl transferase activity of the Escherichia coli penicillin-binding protein 1b: Specificity profile for the substrate
English
Fraipont, Claudine mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Sapunaric, Frédéric mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Zervosen, Astrid mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines > >]
Auger, Geneviève [Université Paris-Sud 11 > > > > > >]
Devreese, Bart [Rijksuniversiteit Gent > > > > > >]
Lioux, Thierry [Katholieke Universiteit Leuven - KUL > > > > > >]
Blanot, Didier [Université Paris-Sud 11 > > > > > >]
Mengin-Lecreulx, Dominique [>Université Paris-Sud 11 > > > > > >]
Herdewijn, Piet [Katholieke Universiteit Leuven - KUL > > > > > >]
Van Beeumen, Jos [Rijksuniversiteit Gent > > > > > >]
Frère, Jean-Marie mailto [Université de Liège - ULg > Département des sciences de la vie > Département des sciences de la vie >]
Nguyen-Disteche, Martine [Université de Liège - ULg > > Centre d'ingénierie des protéines > >]
28-Mar-2006
Biochemistry
Amer Chemical Soc
45
12
4007-4013
Yes (verified by ORBi)
International
0006-2960
Washington
[en] glycosyl-transferase, lipid II
[en] The glycosyl transferase of the Escherichia coli bifunctional penicillin-binding protein (PBP) 1b catalyzes the assembly of lipid-transported N-acetylglucosaminyl-beta-1,4-N-acetylmuramoyl-L-Ala-gamma-D-Glu-meso-A(2)pm-D-Ala-D-Ala units (lipid II) into linear peptidoglycan chains. These units are linked, at C1 of N-acetylmuramic acid (MurNAc), to a C-55 undecaprenyl pyrophosphate. In an in vitro assay, lipid II functions both as a glycosyl donor and as a glycosyl acceptor substrate. Using substrate analogues, it is suggested that the specificity of the enzyme for the glycosyl donor substrate differs from that for the acceptor. The donor substrate requires the presence of both N-acetylglucosamine (GlcNAc) and MurNAc and a reactive group on C1 of the MurNAc and does not absolutely require the lipid chain which can be replaced by uridine. The enzyme appears to prefer an acceptor substrate containing a polyprenyl pyrophosphate on C1 of the MurNAc sugar. The problem of glycan chain elongation that presumably proceeds by the repetitive addition of disaccharide peptide units at their reducing end is discussed.
Researchers
http://hdl.handle.net/2268/13684

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