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- W2129239939 abstract "ABSTRACT A polysaccharide deacetylase homologue, PdaA, was determined to act as an N -acetylmuramic acid deacetylase in vitro. Histidine-tagged truncated PdaA (with the putative signal sequence removed) was overexpressed in Escherichia coli cells and purified. Measurement of deacetylase activity showed that PdaA could deacetylate peptidoglycan treated with N -acetylmuramoyl- l -alanine amidase CwlH but could not deacetylate peptidoglycan treated with or without dl -endopeptidase LytF (CwlE). Reverse-phase high-performance liquid chromatography and mass spectrometry (MS) and MS-MS analyses indicated that PdaA could deacetylate the N -acetylmuramic acid residues of purified glycan strands derived from Bacillus subtilis peptidoglycan." @default.
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- W2129239939 date "2005-02-15" @default.
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- W2129239939 title "A Polysaccharide Deacetylase Homologue, PdaA, in<i>Bacillus subtilis</i>Acts as an<i>N</i>-Acetylmuramic Acid Deacetylase In Vitro" @default.
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- W2129239939 doi "https://doi.org/10.1128/jb.187.4.1287-1292.2005" @default.
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