『徳島大学 教育・研究者情報データベース (EDB)』---[学外] /
ID: Pass:

登録内容 (EID=324847)

EID=324847EID:324847, Map:0, LastModified:2018年8月29日(水) 15:38:34, Operator:[[ADMIN]], Avail:TRUE, Censor:0, Owner:[川上 竜巳], Read:継承, Write:継承, Delete:継承.
種別 (必須): 学術論文 (審査論文) [継承]
言語 (必須): 英語 [継承]
招待 (推奨):
審査 (推奨): Peer Review [継承]
カテゴリ (推奨): 研究 [継承]
共著種別 (推奨): 国内共著 (徳島大学内研究者と国内(学外)研究者との共同研究 (国外研究者を含まない)) [継承]
学究種別 (推奨):
組織 (推奨):
著者 (必須): 1.川上 竜巳 ([徳島大学.大学院社会産業理工学研究部.生物資源産業学域.食料科学系.食料科学分野]/[徳島大学.生物資源産業学部])
役割 (任意):
貢献度 (任意):
学籍番号 (推奨):
[継承]
2.櫻庭 春彦
役割 (任意):
貢献度 (任意):
学籍番号 (推奨):
[継承]
3. (英) Taketo Ohmori (日) 大森 勇門 (読) おおもり たけと
役割 (任意):
貢献度 (任意):
学籍番号 (推奨):
[継承]
4.大島 敏久 ([九州大学])
役割 (任意):
貢献度 (任意):
学籍番号 (推奨):
[継承]
題名 (必須): (英) First characterization of an archaeal amino acid racemase with broad substrate specificity from the hyperthermophile Pyrococcus horikoshii OT-3 induced by D-amino acids  (日)    [継承]
副題 (任意):
要約 (任意): (英) A novel amino acid racemase with broad substrate specificity (BAR) was recently isolated from the hyperthermophilic archaeon Pyrococcus horikoshii OT-3. Characterization of this enzyme has been difficult, however, because the recombinant enzyme is produced mainly as an inclusion body in Escherichia coli. In this study, expression of the recombinant protein into the soluble fraction was markedly improved by co-expression with chaperone molecules. The purified enzyme retained its full activity after incubation at 80°C for at least 2h in buffer (pH 710), making this enzyme the most thermostable amino acid racemase so far known. Besides the nine amino acids containing hydrophobic and aromatic amino acids previously reported (Kawakami etal., Amino Acids, 47, 15791587, 2015), the enzyme exhibited substantial activity toward Thr (about 42% of relative activity toward Phe) and showed no activity toward Arg, His, Gln, and Asn. The substrate specificity of this enzyme thus differs markedly from those of other known amino acid racemases. In particular, the high reaction rate with Trp and Tyr, in addition to Leu, Met and Phe as substrates is a noteworthy feature of this enzyme. The high reactivity toward Trp and Tyr, as well as extremely high thermostability, is likely a major advantage of using BAR for biochemical conversion of these aromatic amino acids.  (日)    [継承]
キーワード (推奨): 1. (英) Amino Acid Isomerases (日) (読) [継承]
2. (英) Amino Acid Sequence (日) (読) [継承]
3. (英) Hydrophobic and Hydrophilic Interactions (日) (読) [継承]
4. (英) Pyrococcus horikoshii (日) (読) [継承]
5. (英) Substrate Specificity (日) (読) [継承]
6. (英) Temperature (日) (読) [継承]
発行所 (推奨):
誌名 (必須): Journal of Bioscience and Bioengineering ([日本生物工学会])
(pISSN: 1389-1723, eISSN: 1347-4421)

ISSN (任意): 1347-4421
ISSN: 1389-1723 (pISSN: 1389-1723, eISSN: 1347-4421)
Title: Journal of bioscience and bioengineering
Title(ISO): J Biosci Bioeng
Supplier: 公益社団法人日本生物工学会
Publisher: Elsevier BV
 (NLM Catalog  (Webcat Plus  (医中誌Web  (Scopus  (CrossRef (Scopus information is found. [need login])
[継承]
[継承]
(必須): 124 [継承]
(必須): 1 [継承]
(必須): 23 27 [継承]
都市 (任意):
年月日 (必須): 西暦 2017年 7月 初日 (平成 29年 7月 初日) [継承]
URL (任意):
DOI (任意): 10.1016/j.jbiosc.2017.02.004    (→Scopusで検索) [継承]
PMID (任意): 28343923    (→Scopusで検索) [継承]
NAID (任意):
WOS (任意):
Scopus (任意): 2-s2.0-85016976917 [継承]
機関リポジトリ : 111977 [継承]
評価値 (任意):
被引用数 (任意):
指導教員 (推奨):
備考 (任意): 1.(英) Article.ELocationID: S1389-1723(16)30319-X  (日)    [継承]
2.(英) Article.ELocationID: 10.1016/j.jbiosc.2017.02.004  (日)    [継承]
3.(英) Article.PublicationTypeList.PublicationType: Journal Article  (日)    [継承]
4.(英) KeywordList.Keyword: Amino acid racemase  (日)    [継承]
5.(英) KeywordList.Keyword: Broad substrate specificity  (日)    [継承]
6.(英) KeywordList.Keyword: Hyperthermophilic archaeon  (日)    [継承]
7.(英) KeywordList.Keyword: Kinetics  (日)    [継承]
8.(英) KeywordList.Keyword: Pyrococcus horikoshii OT-3  (日)    [継承]

標準的な表示

和文冊子 ● Ryushi Kawakami, Haruhiko Sakuraba, Ohmori Taketo and Toshihisa Ohshima : First characterization of an archaeal amino acid racemase with broad substrate specificity from the hyperthermophile Pyrococcus horikoshii OT-3 induced by D-amino acids, Journal of Bioscience and Bioengineering, Vol.124, No.1, 23-27, 2017.
欧文冊子 ● Ryushi Kawakami, Haruhiko Sakuraba, Ohmori Taketo and Toshihisa Ohshima : First characterization of an archaeal amino acid racemase with broad substrate specificity from the hyperthermophile Pyrococcus horikoshii OT-3 induced by D-amino acids, Journal of Bioscience and Bioengineering, Vol.124, No.1, 23-27, 2017.

関連情報

Number of session users = 0, LA = 1.24, Max(EID) = 377826, Max(EOID) = 1011129.