| Literature DB >> 15687192 |
Tatsuya Fukushima1, Toshihiko Kitajima, Junichi Sekiguchi.
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.Entities:
Mesh:
Substances:
Year: 2005 PMID: 15687192 PMCID: PMC545626 DOI: 10.1128/JB.187.4.1287-1292.2005
Source DB: PubMed Journal: J Bacteriol ISSN: 0021-9193 Impact factor: 3.490