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*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

39 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)9765-9776
Number of pages12
JournalJournal of Biological Chemistry
Issue number13
Publication statusPublished - 2012 Mar 23
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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