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Structural Insights into MltC from <i>Acinetobacter baumannii</i>: Conservation of the Catalytic Residue and Flexibility in Substrate Recognition. [PDF]
Jang H, Kim CM, Park HH.
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‘Holy’ proteins II: the soluble lytic transglycosylase
Current Opinion in Structural Biology, 1994Enzymes involved in the metabolism of the bacterial cell wall peptidoglycan are excellent targets for antibiotics. Penicillins and related beta-lactam antibiotics inhibit the enzymes that act on the peptide cross-links of the peptidoglycan. The X-ray structure of the transglycosylase revealed a two-layered ring of alpha-helices in a right-handed ...
Dijkstra, Bauke W. +1 more
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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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1996
Although cleaving the same glycosidic bond between MurNAc and GlcNAc in murein, lytic transglycosylases differ from lysozymes by catalyzing an intramolecular transglycosylation of the glycosyl-bond onto the C6 hydroxyl group of the muramic acid residue yielding 1.6-anhydromuramic acid-carrying products.
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Although cleaving the same glycosidic bond between MurNAc and GlcNAc in murein, lytic transglycosylases differ from lysozymes by catalyzing an intramolecular transglycosylation of the glycosyl-bond onto the C6 hydroxyl group of the muramic acid residue yielding 1.6-anhydromuramic acid-carrying products.
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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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