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Journal of Bacteriology, February 2005, p. 1287-1292, Vol. 187, No. 4
0021-9193/05/$08.00+0     doi:10.1128/JB.187.4.1287-1292.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

A Polysaccharide Deacetylase Homologue, PdaA, in Bacillus subtilis Acts as an N-Acetylmuramic Acid Deacetylase In Vitro

Tatsuya Fukushima, Toshihiko Kitajima, and Junichi Sekiguchi*

Department of Applied Biology, Faculty of Textile Science and Technology, Shinshu University, Ueda-shi, Nagano, Japan

Received 2 September 2004/ Accepted 5 November 2004

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.

* Corresponding author. Mailing address: Department of Applied Biology, Faculty of Textile Science and Technology, Shinshu University, Ueda-shi, Nagano 386-8567, Japan. Phone: 81-268-21-5344. Fax: 81-268-21-5345. E-mail: jsekigu{at}giptc.shinshu-u.ac.jp.

Journal of Bacteriology, February 2005, p. 1287-1292, Vol. 187, No. 4
0021-9193/05/$08.00+0     doi:10.1128/JB.187.4.1287-1292.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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