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https://soar-ir.repo.nii.ac.jp/oai
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2022-12-14T03:48:23Z
1309:1310
Identification and Characterization of a Novel Polysaccharide Deacetylase C (PdaC) from Bacillus subtilis
Kobayashi, Kaori
Sudiarta, I. Putu
Kodama, Takeko
Fukushima, Tatsuya
Ara, Katsutoshi
Ozaki, Katsuya
Sekiguchi, Junichi
Copyright© 2012 The American Society for Biochemistry and Molecular Biology, Inc.
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 (Mn2+, Mg2+, Ca2+). 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.
Article
JOURNAL OF BIOLOGICAL CHEMISTRY. 287(13):9765-9776 (2012)
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
2012-03-23
eng
journal article
AM
http://hdl.handle.net/10091/16189
https://soar-ir.repo.nii.ac.jp/records/13378
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?CMD=search&DB=pubmed&term=22277649
22277649
https://doi.org/10.1074/jbc.M111.329490
10.1074/jbc.M111.329490
0021-9258
AA00251083
JOURNAL OF BIOLOGICAL CHEMISTRY
287
13
9765
9776
https://soar-ir.repo.nii.ac.jp/record/13378/files/Identification_characterization_novel_polysaccharide_deacetylase_C.pdf
application/pdf
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2015-09-28