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Assessment of Substrate Inhibition of Bacterial Oligopeptidase B
http://hdl.handle.net/10069/31024
http://hdl.handle.net/10069/31024895935fb-5dbb-43e1-b3b0-ab7f27035a70
名前 / ファイル | ライセンス | アクション |
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BPBul35_2010.pdf (1.2 MB)
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Item type | 学術雑誌論文 / Journal Article(1) | |||||
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公開日 | 2013-03-18 | |||||
タイトル | ||||||
タイトル | Assessment of Substrate Inhibition of Bacterial Oligopeptidase B | |||||
言語 | ||||||
言語 | eng | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | Oligopeptidase B | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | Opportunistic bacteria | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | Prolyl oligopeptidase family | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | Substrate inhibition | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | Substrate specificity | |||||
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 |
Mohamed, Mustafa Malik Suliman
× Mohamed, Mustafa Malik Suliman× Nakajima, Yoshitaka× Oyama, Hiroshi× Iwata, Nobuhisa× Ito, Kiyoshi |
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抄録 | ||||||
内容記述タイプ | Abstract | |||||
内容記述 | Oligopeptidase B (OPB; EC 3.4.21.83) from 2 Gram-negative bacteria, Stenotrophomonas maltophilia (Stm) and Serratia marcescens (Sem), and the Gram-positive bacterium Rhodococcus erythropolis (Re) were cloned and characterized to clarify their activities and substrate specificities using peptidyl-MCA substrates containing Arg or Lys. The cloned enzymes, Stm, Sem and ReOPBs, in addition to Escherichia coli OPB (EcOPB) were expressed using a pET expression system. Although the Stm and SemOPBs share 45% sequence identity to each other and up to 60% identity with respect to their catalytic domains, their activities towards MCA substrates were quite different. StmOPB is approximately 100-500 times more active than SemOPB and 3-30 times more active than EcOPB. The activity of ReOPB is comparable to that of StmOPB and it shares 40% and 36% identity to StmOPB and SemOPB, respectively. Some features of Stm, Re and EcOPBs are similar to those of previously cloned OPBs, which were also strongly inhibited by substrates, but SemOPB differs from all other OPBs in that it is not inhibited by substrates; even substrates containing double arginine at 35μM did not inhibit SemOPB. On the other hand, the same substrates at only 5μM inhibited the activity of the Stm, Re, and EcOPB. This phenomenon was not observed with substrates containing single or double lysine. | |||||
書誌情報 |
Biological and Pharmaceutical Bulletin 巻 35, 号 11, p. 2010-2016, 発行日 2012-11-01 |
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出版者 | ||||||
出版者 | 日本薬学会 | |||||
出版者別言語 | ||||||
Pharmaceutical Society of Japan | ||||||
ISSN | ||||||
収録物識別子タイプ | ISSN | |||||
収録物識別子 | 09186158 | |||||
EISSN | ||||||
収録物識別子タイプ | ISSN | |||||
収録物識別子 | 13475215 | |||||
DOI | ||||||
関連タイプ | isIdenticalTo | |||||
識別子タイプ | DOI | |||||
関連識別子 | 10.1248/bpb.b12-00544 | |||||
権利 | ||||||
権利情報 | © 2012 The Pharmaceutical Society of Japan. | |||||
著者版フラグ | ||||||
出版タイプ | VoR | |||||
出版タイプResource | http://purl.org/coar/version/c_970fb48d4fbd8a85 | |||||
引用 | ||||||
内容記述タイプ | Other | |||||
内容記述 | Biological and Pharmaceutical Bulletin, 35(11), pp.2010-2016; 2012 |