Abstract
We show that in Lactococcus lactis, the gene asnH encodes the asparagine synthase involved in amidation of D-Asp present in peptidoglycan side chains and crossbridges. The level of D-Asp amidation in peptidoglycan has a strong effect on the sensitivity of bacteria to endogenous autolysins and to the cationic antimicrobials nisin and lysozyme.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Aspartate-Ammonia Ligase / genetics
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Aspartate-Ammonia Ligase / metabolism*
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism*
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Chromatography, High Pressure Liquid
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D-Aspartic Acid / metabolism*
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Drug Resistance, Bacterial / genetics
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Lactococcus lactis / drug effects
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Lactococcus lactis / enzymology*
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Muramidase / pharmacology
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N-Acetylmuramoyl-L-alanine Amidase / metabolism
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Nisin / pharmacology
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Peptidoglycan / chemistry
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Peptidoglycan / metabolism*
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Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
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Tandem Mass Spectrometry
Substances
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Bacterial Proteins
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Peptidoglycan
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Nisin
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D-Aspartic Acid
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Muramidase
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N-Acetylmuramoyl-L-alanine Amidase
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Aspartate-Ammonia Ligase