title: A polysaccharide deacetylase homologue, PdaA, in Bacillus subtilis acts as an N-acetylmuramic acid deacetylase in vitro.
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.
authors.affiliation: Department of Applied Biology, Faculty of Textile Science and Technology, Shinshu University, Ueda-shi, Nagano 386-8567, Japan.
authors.forename: Tatsuya
authors.initials: T
authors.lastname: Fukushima
authors.forename: Toshihiko
authors.initials: T
authors.lastname: Kitajima
authors.forename: Junichi
authors.initials: J
authors.lastname: Sekiguchi
mesh_terms: D000581:Amidohydrolases / Q000096:biosynthesis / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D001412:Bacillus subtilis / Q000201:enzymology*; D002851:Chromatography, High Pressure Liquid; D010450:Endopeptidases / Q000378:metabolism; D013058:Mass Spectrometry; D009112:Muramic Acids / Q000378:metabolism*; D009238:N-Acetylmuramoyl-L-alanine Amidase / Q000378:metabolism; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism
chemical_list: D009112:Muramic Acids; D011994:Recombinant Proteins; C031651:N-acetylmuramic acid; D010450:Endopeptidases; D000581:Amidohydrolases; C022427:polysaccharide deacetylase; D009238:N-Acetylmuramoyl-L-alanine Amidase