A Polysaccharide Deacetylase Homologue, PdaA, in Bacillus subtilis Acts as an N-Acetylmuramic Acid Deacetylase In Vitro
2005 ◽
Vol 187
(4)
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pp. 1287-1292
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Keyword(s):
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.
2019 ◽
Vol 165
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pp. 251-260
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1996 ◽
Vol 11
(12)
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pp. 1177-1182
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2019 ◽
Vol 33
(11)
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pp. 1024-1035
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2014 ◽
Vol 89
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pp. 183-196
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2011 ◽
Vol 1218
(23)
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pp. 3711-3717
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