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  1. 080 繊維学部
  2. 0801 学術論文

Bacillus subtilis CwlP of the SP-beta Prophage Has Two Novel Peptidoglycan Hydrolase Domains, Muramidase and Cross-linkage Digesting DD-Endopeptidase

http://hdl.handle.net/10091/16188
db65bf82-cbd3-4df1-ae1d-a00121d6087f
名前 / ファイル ライセンス アクション
Bacillus_subtilis_CwlP_SP-beta_Prophage.pdf Bacillus_subtilis_CwlP_SP-beta_Prophage.pdf (1.6 MB)
Item type 学術雑誌論文 / Journal Article(1)
公開日 2013-01-18
タイトル
言語 en
タイトル Bacillus subtilis CwlP of the SP-beta Prophage Has Two Novel Peptidoglycan Hydrolase Domains, Muramidase and Cross-linkage Digesting DD-Endopeptidase
言語
言語 eng
資源タイプ
資源 http://purl.org/coar/resource_type/c_6501
タイプ journal article
著者 Sudiarta, I. Putu

× Sudiarta, I. Putu

WEKO 40646

Sudiarta, I. Putu

Search repository
Fukushima, Tatsuya

× Fukushima, Tatsuya

WEKO 40647

Fukushima, Tatsuya

Search repository
Sekiguchi, Junichi

× Sekiguchi, Junichi

WEKO 40648

Sekiguchi, Junichi

Search repository
出版者
出版者 AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
引用
内容記述タイプ Other
内容記述 JOURNAL OF BIOLOGICAL CHEMISTRY. 285(53):41232-41243 (2010)
書誌情報 JOURNAL OF BIOLOGICAL CHEMISTRY

巻 285, 号 53, p. 41232-41243, 発行日 2010-12-31
抄録
内容記述タイプ Abstract
内容記述 For bacteria and bacteriophages, cell wall digestion by hydrolases is a very important event. We investigated one of the proteins involved in cell wall digestion, the yomI gene product (renamed CwlP). The gene is located in the SP-beta prophage region of the Bacillus subtilis chromosome. Inspection of the Pfam database indicates that CwlP contains soluble lytic transglycosylase (SLT) and peptidase M23 domains, which are similar to Escherichia coli lytic transglycosylase Slt70, and the Staphylococcus aureus Gly-Gly endopeptidase LytM, respectively. The SLT domain of CwlP exhibits hydrolytic activity toward the B. subtilis cell wall; however, reverse phase (RP)HPLC and mass spectrometry revealed that the CwlP-SLT domain has only muramidase activity. In addition, the peptidase M23 domain of CwlP exhibited hydrolytic activity and could cleave D-Ala-diaminopimelic acid cross-linkage, a property associated with DD-endopeptidases. Remarkably, the M23 domain of CwlP possessed a unique Zn(2+) -independent endopeptidase activity; this contrasts with all other characterized M23 peptidases (and enzymes similar to CwlP), which are Zn(2+) dependent. Both domains of CwlP could hydrolyze the peptidoglycan and cell wall of B. subtilis. However, the M23 domain digested neither the peptidoglycans nor the cell walls of S. aureus or Streptococcus thermophilus. The effect of defined point mutations in conserved amino acid residues of CwlP is also determined.
資源タイプ(コンテンツの種類)
内容記述タイプ Other
内容記述 Article
ISSN
収録物識別子タイプ ISSN
収録物識別子 0021-9258
書誌レコードID
収録物識別子タイプ NCID
収録物識別子 AA00251083
PubMed
関連識別子
識別子タイプ PMID
関連識別子 http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?CMD=search&DB=pubmed&term=20980266
関連名称
関連名称 20980266
DOI
関連識別子
識別子タイプ DOI
関連識別子 https://doi.org/10.1074/jbc.M110.156273
関連名称
関連名称 10.1074/jbc.M110.156273
権利
権利情報 Copyright© 2010 The American Society for Biochemistry and Molecular Biology, Inc.
出版タイプ
出版タイプ AM
出版タイプResource http://purl.org/coar/version/c_ab4af688f83e57aa
WoS
表示名 Web of Science
URL http://gateway.isiknowledge.com/gateway/Gateway.cgi?&GWVersion=2&SrcAuth=ShinshuUniv&SrcApp=ShinshuUniv&DestLinkType=FullRecord&DestApp=WOS&KeyUT=000285622600009
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