Abstract
Lytic proteins encoded by bacterial genomes have been implicated in cell wall biosynthesis and recycling. The Bacillus cereus E33L ampD gene encodes a putative N-acetylmuramoyl-l-alanine amidase. This gene, expressed in vitro, produced a very stable, highly active lytic protein. Very low concentrations rapidly and efficiently lyse vegetative Bacillus anthracis cells.
Publication types
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Anti-Infective Agents / chemistry
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Anti-Infective Agents / metabolism
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Bacillus anthracis / cytology
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Bacillus anthracis / drug effects*
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Bacillus anthracis / physiology*
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Bacillus cereus / enzymology*
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Bacillus cereus / genetics*
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Bacterial Proteins / chemistry
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Bacterial Proteins / genetics*
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Bacterial Proteins / metabolism*
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Bacteriolysis*
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Colony Count, Microbial
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Enzyme Stability
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Microbial Viability / drug effects
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Microscopy
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N-Acetylmuramoyl-L-alanine Amidase / chemistry
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N-Acetylmuramoyl-L-alanine Amidase / genetics*
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N-Acetylmuramoyl-L-alanine Amidase / metabolism*
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Protein Stability
Substances
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Anti-Infective Agents
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Bacterial Proteins
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AmpD protein, Bacteria
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N-Acetylmuramoyl-L-alanine Amidase