A polysaccharide deacetylase homologue, PdaA, in Bacillus subtilis acts as an N-acetylmuramic acid deacetylase in vitro

被引：45

作者：

Fukushima, T ^{[1
]}

Kitajima, T ^{[1
]}

Sekiguchi, J ^{[1
]}

机构：

[1] Shinshu Univ, Fac Text Sci & Technol, Dept Appl Biol, Ueda, Nagano 3868567, Japan

来源：

JOURNAL OF BACTERIOLOGY | 2005年 / 187卷 / 04期

关键词：

D O I：

10.1128/JB.187.4.1287-1292.2005

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

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.

引用

页码：1287 / 1292

页数：6

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