Results 151 to 160 of about 2,643 (172)
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Identification of Four Families of Peptidoglycan Lytic Transglycosylases
Journal of Molecular Evolution, 2001The lytic transglycosylases are a class of autolysins which cleave the bacterial cell wall heteropolymer peptidoglycan (murein) to facilitate its biosynthesis and turnover. A search of the National Center for Biotechnology Information (NCBI) databases using the primary sequences of the six characterized lytic transglycosylases of Escherichia coli, a ...
N T, Blackburn, A J, Clarke
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Assay for Lytic Transglycosylases: A Family of Peptidoglycan Lyases
Analytical Biochemistry, 2000An assay has been developed to monitor the activity of the lytic transglycosylases which does not involve the use of radiolabel. Samples of lytic transglycosylase were incubated with isolated and purified insoluble peptidoglycan as substrate for varying lengths of time.
N T, Blackburn, A J, Clarke
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Crystal structure of Escherichia coli lytic transglycosylase Slt35 reveals a lysozyme-like catalytic domain with an EF-hand [PDF]
Structure, 1999 Background: Lytic transglycosylases are bacterial muramidases that catalyse the cleavage of the β-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) in peptidoglycan with concomitant formation of a 1,6-anhydrobond ...
Kor H Kalk, W Keck, Bauke W Dijkstra
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Crystal Structure of MltA from Escherichia coli Reveals a Unique Lytic Transglycosylase Fold [PDF]
Journal of Molecular Biology, 2005 Lytic transglycosylases are bacterial enzymes involved in the maintenance and growth of the bacterial cell-wall peptidoglycan. They cleave the β-(1,4)-glycosidic bonds in peptidoglycan forming non-reducing 1,6-anhydromuropeptides.
Bauke W Dijkstra +2 more
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Binding of calcium in the EF-hand ofEscherichia colilytic transglycosylase Slt35 is important for stability [PDF]
FEBS Letters, 1999 The Escherichia coli lytic transglycosylase Slt35 contains a single metal ion-binding site that resembles EF-hand calcium-binding sites. The Slt35 EF-hand is only the second observation of such a domain in a prokaryotic protein. Two crystal structures at
Bauke W Dijkstra
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Characterization of the role of LtgB, a putative lytic transglycosylase in Neisseria gonorrhoeae
Microbiology, 2005Neisseria gonorrhoeaereleases monomeric peptidoglycan (PG) fragments during growth. These PG fragments affect pathogenesis-related phenotypes including induction of inflammatory cytokines and killing of ciliated fallopian tube cells. Although the biological activities of these molecules have been established in multiple systems, the genes and gene ...
Petra L, Kohler +4 more
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Subcellular Location of the Soluble Lytic Transglycosylase Homologue in Staphylococcus aureus
Current Microbiology, 2004The immunodominant antigen A, IsaA, of Staphylococcus aureus was found to include a putative soluble lytic transglycosylase domain in its C-terminal region. Since the presence of this distinctive domain suggested that the protein might participate in peptidoglycan turnover, as indicated in Gram-negative bacteria, its cellular location was investigated.
Noriaki, Sakata +2 more
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Lytic transglycosylases in macromolecular transport systems of Gram-negative bacteria
Cellular and Molecular Life Sciences (CMLS), 2003The cell wall of Gram-negative bacteria is essential for the integrity of the bacterial cell but also imposes a physical barrier to trans-envelope transport processes in which DNA and/or proteins are taken up or secreted by complex protein assemblies.
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Characterization of three different lytic transglycosylases in Escherichia coli
1993Two lytic transglycosylases, releasing 1,6-anhydromuropeptides from murein sacculi are present in a mutant deleted for the soluble lytic transglycosylase 70 (Slt70). Thus, there are three different lytic transglycosylases in Escherichia coli. One of the remaining enzymes is soluble and one is a membrane protein that can be solubilized by 2% Triton X ...
Romeis, T. ; https://orcid.org/0000-0002-0838-0031 +2 more
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