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Title: Glycosyl transferase activity of the Escherichia coli penicillin-binding protein 1b: specificity profile for the substrate
Authors: Fraipont, C ×
Sapunaric, F
Zervosen, A
Auger, G
Devreese, B
Lioux, T
Blanot, D
Mengin-Lecreulx, D
Herdewijn, Piet
Van Beeumen, J
Frère, JMe
Nguyen-Distèche, M #
Issue Date: 2006
Series Title: Biochemistry vol:45 issue:12 pages:4007-4013
Abstract: 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-A2pm-D-Ala-D-Ala units (lipid II) into linear peptidoglycan chains. These units are linked, at C1 of N-acetylmuramic acid (MurNAc), to a C55 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.
URI: 
ISSN: 0006-2960
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Medicinal Chemistry (Rega Institute)
× corresponding author
# (joint) last author

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