Identification and characterization of a novel polysaccharide deacetylase C (PdaC) from Bacillus subtilis

Kaori Kobayashi, I. Putu Sudiarta, Takeko Kodama, Tatsuya Fukushima, Katsutoshi Ara, Katsuya Ozaki, Junichi Sekiguchi*

*この研究の対応する著者

研究成果: Article査読

33 被引用数 (Scopus)

抄録

Cell wall metabolism and cell wall modification are very important processes that bacteria use to adjust to various environmental conditions. One of the main modifications is deacetylation of peptidoglycan. The polysaccharide deacetylase homologue, Bacillus subtilis YjeA (renamed PdaC), was characterized and found to be a unique deacetylase. The pdaC deletion mutant was sensitive to lysozyme treatment, indicating that PdaC acts as a deacetylase. The purified recombinant and truncated PdaC from Escherichia coli deacetylated B. subtilis peptidoglycan and its polymer, (-GlcNAc-MurNAc[-L-Ala-D-Glu]-) n. Surprisingly, RP-HPLC and ESI-MS/MS analyses showed that the enzyme deacetylates N-acetylmuramic acid (MurNAc) not GlcNAc from the polymer. Contrary to Streptococcus pneumoniae PgdA, which shows high amino acid sequence similarity with PdaC and is a zinc-dependent GlcNAc deacetylase toward peptidoglycan, there was less dependence on zinc ion for deacetylation of peptidoglycan by PdaC than other metal ions (Mn 2+, Mg 2+, Ca 2+). The kinetic values of the activity toward B. subtilis peptidoglycan were K m = 4.8 mM and k cat = 0.32 s -1. PdaC also deacetylated N-acetylglucosamine (GlcNAc) oligomers with a K m = 12.3 mM and k cat = 0.24 s -1 toward GlcNAc 4. Therefore, PdaC has GlcNAc deacetylase activity toward GlcNAc oligomers and MurNAc deacetylase activity toward B. subtilis peptidoglycan.

本文言語English
ページ(範囲)9765-9776
ページ数12
ジャーナルJournal of Biological Chemistry
287
13
DOI
出版ステータスPublished - 2012 3 23
外部発表はい

ASJC Scopus subject areas

  • 生化学
  • 分子生物学
  • 細胞生物学

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