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Determination of three amino acids causing alteration of proteolytic activities of staphylococcal glutamyl endopeptidases.
http://hdl.handle.net/10069/23192
http://hdl.handle.net/10069/231929dd5c01d-1a16-4fc7-8bbd-c064ac5b0e10
名前 / ファイル | ライセンス | アクション |
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BioChem390_277.pdf (603.6 kB)
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Item type | 学術雑誌論文 / Journal Article(1) | |||||
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公開日 | 2010-06-11 | |||||
タイトル | ||||||
タイトル | Determination of three amino acids causing alteration of proteolytic activities of staphylococcal glutamyl endopeptidases. | |||||
言語 | ||||||
言語 | eng | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | Glutamyl endopeptidase | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | Staphylococcus aureus | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | Staphylococcus epidermidis | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | Substrate-binding pocket | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | V8 protease | |||||
資源タイプ | ||||||
資源タイプ識別子 | http://purl.org/coar/resource_type/c_6501 | |||||
資源タイプ | journal article | |||||
著者 |
Nemoto, Takayuki K
× Nemoto, Takayuki K× Ono, Toshio× Shimoyama, Yu× Kimura, Shigenobu× Ohara-Nemoto, Yuko |
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抄録 | ||||||
内容記述タイプ | Abstract | |||||
内容記述 | Abstract Staphylococcus aureus, Staphylococcus epidermidis and Staphylococcus warneri secrete glutamyl endopeptidases, designated GluV8, GluSE and GluSW, respectively. The order of their protease activities was GluSE<GluSW<<GluV8. The present study investigated the mechanism that causes these differences. Expression of chimeric proteins between GluV8 and GluSE revealed that the difference was primarily attributed to amino acids at residues 170-195, which defined the intrinsic protease activity, and additionally to residues 119-169, which affected the proteolysis sensitivity. Among nine substitutions present in residues 170-195 of the three proteases, the substitutions at positions 185, 188 and 189 were responsible for the changes in their activities; and the combination of W185, V188 and P189, which naturally occurred on GluV8, exerted the highest protease activity. Among them, W185 and P189 were indispensable for the full activity; but V188 could be replaced by hydrophobic amino acids. These three amino acid residues appeared to create a substrate-binding pocket together with the catalytic triad and the N-terminal V1, and therefore, defined the K(m) values of the proteases. This study also describes the way to produce a chimeric form of GluSE and GluV8 that was resistant to proteolysis, and therefore, possessed activity 4-fold higher than that of the wild-type recombinant GluV8. | |||||
書誌情報 |
Biological chemistry 巻 390, 号 3, p. 277-285, 発行日 2009-03 |
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出版者 | ||||||
出版者 | Walter de Gruyter GmbH & Co. KG | |||||
ISSN | ||||||
収録物識別子タイプ | ISSN | |||||
収録物識別子 | 14316730 | |||||
EISSN | ||||||
収録物識別子タイプ | ISSN | |||||
収録物識別子 | 14374315 | |||||
書誌レコードID | ||||||
収録物識別子タイプ | NCID | |||||
収録物識別子 | AA11099140 | |||||
PubMed番号 | ||||||
関連タイプ | isVersionOf | |||||
識別子タイプ | PMID | |||||
関連識別子 | 19090719 | |||||
DOI | ||||||
関連タイプ | isVersionOf | |||||
識別子タイプ | DOI | |||||
関連識別子 | 10.1515/BC.2009.027 | |||||
権利 | ||||||
権利情報 | Walter de Gruyter. | |||||
著者版フラグ | ||||||
出版タイプ | AM | |||||
出版タイプResource | http://purl.org/coar/version/c_ab4af688f83e57aa | |||||
関係URI | ||||||
関連名称 | www.degruyter.com/journals/bc | |||||
引用 | ||||||
内容記述タイプ | Other | |||||
内容記述 | Biological chemistry, 390(3), pp.277-285; 2009 |