『徳島大学 教育・研究者情報データベース (EDB)』---[学外] /
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種別 (必須): 学術論文 (審査論文) [継承]
言語 (必須): 英語 [継承]
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カテゴリ (推奨):
共著種別 (推奨):
学究種別 (推奨):
組織 (推奨):
著者 (必須): 1. (英) Satomura Takenori (日) (読)
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2.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])
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3. (英) Sakuraba Haruhiko (日) (読)
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4. (英) Ohshima Toshihisa (日) (読)
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題名 (必須): (英) A novel flavin adenine dinucleotide (FAD) containing d-lactate dehydrogenase from the thermoacidophilic crenarchaeota Sulfolobus tokodaii strain 7: purification, characterization and expression in Escherichia coli.  (日)    [継承]
副題 (任意):
要約 (任意): (英) Dye-linked D-lactate dehydrogenase activity was found in the crude extract of a continental thermoacidophilic crenarchaeota, Sulfolobus tokodaii strain 7, and was purified 375-fold through four sequential chromatography steps. With a molecular mass of about 93 kDa, this enzyme was a homodimer comprised of identical subunits with molecular masses of about 48 kDa. The enzyme retained its full activity after incubation at 80 degrees C for 10 min and after incubation at pHs ranging from 6.5 to 10.0 for 30 min at 50 degrees C. The preferred substrate for this enzyme was D-lactate, with 2,6-dichloroindophenol serving as the electron acceptor. Using high-performance liquid chromatography (HPLC), the enzyme's prosthetic group was determined to be flavin adenine dinucleotide (FAD). Its N-terminal amino acid sequence was MLEGIEYSQGEEREDFVGFKIKPKI. Using that sequence and previously reported genome information, the gene encoding the enzyme (ST0649) was identified. It was subsequently cloned and expressed in Escherichia coli and found to encode a polypeptide of 440 amino acids with a calculated molecular weight of 49,715. The amino acid sequence of this dye-linked D-lactate dehydrogenase showed higher homology (39% identity) with that of a glycolate oxidase subunit homologue from Archaeoglobus fulgidus, but less similarity (32% identity) to D-lactate dehydrogenase from A. fulgidus. Taken together, our findings indicate that the dye-linked D-lactate dehydrogenase from S. tokodaii is a novel type of FAD containing D-lactate dehydrogenase.  (日)    [継承]
キーワード (推奨): 1. (英) Amino Acid Sequence (日) (読) [継承]
2. (英) Enzyme Activation (日) (読) [継承]
3. (英) Escherichia coli (日) (読) [継承]
4. (英) Flavin-Adenine Dinucleotide (日) (読) [継承]
5. (英) Lactate Dehydrogenases (日) (読) [継承]
6. (英) Molecular Sequence Data (日) (読) [継承]
7. (英) Protein Engineering (日) (読) [継承]
8. (英) Species Specificity (日) (読) [継承]
9. (英) Sulfolobus (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])
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年月日 (必須): 西暦 2008年 7月 初日 (平成 20年 7月 初日) [継承]
URL (任意):
DOI (任意): 10.1263/jbb.106.16    (→Scopusで検索) [継承]
PMID (任意): 18691525    (→Scopusで検索) [継承]
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備考 (任意): 1.(英) Article.ELocationID: 10.1263/jbb.106.16  (日)    [継承]
2.(英) Article.Affiliation: Department of Materials Science, Yonago National College of Technology, 4448 Hikona-cho, Yonago, Tottori 683-8506, Japan.  (日)    [継承]
3.(英) Article.PublicationTypeList.PublicationType: Journal Article  (日)    [継承]
4.(英) Article.PublicationTypeList.PublicationType: Research Support, Non-U.S. Gov't  (日)    [継承]

標準的な表示

和文冊子 ● Takenori Satomura, Ryushi Kawakami, Haruhiko Sakuraba and Toshihisa Ohshima : A novel flavin adenine dinucleotide (FAD) containing d-lactate dehydrogenase from the thermoacidophilic crenarchaeota Sulfolobus tokodaii strain 7: purification, characterization and expression in Escherichia coli., Journal of Bioscience and Bioengineering, Vol.106, No.1, 16-21, 2008.
欧文冊子 ● Takenori Satomura, Ryushi Kawakami, Haruhiko Sakuraba and Toshihisa Ohshima : A novel flavin adenine dinucleotide (FAD) containing d-lactate dehydrogenase from the thermoacidophilic crenarchaeota Sulfolobus tokodaii strain 7: purification, characterization and expression in Escherichia coli., Journal of Bioscience and Bioengineering, Vol.106, No.1, 16-21, 2008.

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