『徳島大学 教育・研究者情報データベース (EDB)』---[学外] /
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EID=262426EID:262426, Map:0, LastModified:2013年9月11日(水) 18:54:34, Operator:[大家 隆弘], 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]
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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])
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2. (英) Sakuraba Haruhiko (日) (読)
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3. (英) Goda Shuichiro (日) (読)
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4. (英) Tsuge Hideaki (日) (読)
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5. (英) Ohshima Toshihisa (日) (読)
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題名 (必須): (英) Refolding, characterization and crystal structure of (S)-malate dehydrogenase from the hyperthermophilic archaeon Aeropyrum pernix.  (日)    [継承]
副題 (任意):
要約 (任意): (英) Tartrate oxidation activity was found in the crude extract of an aerobic hyperthermophilic archaeon Aeropyrum pernix, and the enzyme was identified as (S)-malate dehydrogenase (MDH), which, when produced in Escherichia coli, was mainly obtained as an inactive inclusion body. The inclusion body was dissolved in 6 M guanidine-HCl and gradually refolded to the active enzyme through dilution of the denaturant. The purified recombinant enzyme consisted of four identical subunits with a molecular mass of about 110 kDa. NADP was preferred as a coenzyme over NAD for (S)-malate oxidation and, unlike MDHs from other sources, this enzyme readily catalyzed the oxidation of (2S,3S)-tartrate and (2S,3R)-tartrate. The tartrate oxidation activity was also observed in MDHs from the hyperthermophilic archaea Methanocaldococcus jannaschii and Archaeoglobus fulgidus, suggesting these hyperthermophilic MDHs loosely bind their substrates. The refolded A. pernix MDH was also crystallized, and the structure was determined at a resolution of 2.9 A. Its overall structure was similar to those of the M. jannaschii, Chloroflexus aurantiacus, Chlorobium vibrioforme and Cryptosporidium parvum [lactate dehydrogenase-like] MDHs with root-mean-square-deviation values between 1.4 and 2.1 A. Consistent with earlier reports, Ala at position 53 was responsible for coenzyme specificity, and the next residue, Arg, was important for NADP binding. Structural comparison revealed that the hyperthermostability of the A. pernix MDH is likely attributable to its smaller cavity volume and larger numbers of ion pairs and ion-pair networks, but the molecular strategy for thermostability may be specific for each enzyme.  (日)    [継承]
キーワード (推奨): 1. (英) Aeropyrum (日) (読) [継承]
2. (英) Amino Acid Sequence (日) (読) [継承]
3. (英) Base Sequence (日) (読) [継承]
4. (英) Catalytic Domain (日) (読) [継承]
5. (英) Crystallography, X-Ray (日) (読) [継承]
6. (英) DNA Primers (日) (読) [継承]
7. (英) DNA, Archaeal (日) (読) [継承]
8. (英) Enzyme Stability (日) (読) [継承]
9. (英) Genes, Archaeal (日) (読) [継承]
10. (英) Malate Dehydrogenase (日) (読) [継承]
11. (英) Models, Molecular (日) (読) [継承]
12. (英) Molecular Sequence Data (日) (読) [継承]
13. (英) Molecular Weight (日) (読) [継承]
14. (英) Protein Folding (日) (読) [継承]
15. (英) Protein Subunits (日) (読) [継承]
16. (英) Recombinant Proteins (日) (読) [継承]
17. (英) Sequence Homology, Amino Acid (日) (読) [継承]
18. (英) Substrate Specificity (日) (読) [継承]
19. (英) Thermodynamics (日) (読) [継承]
発行所 (推奨):
誌名 (必須): Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics ([Elsevier Science])
(pISSN: 1570-9639, eISSN: 1878-1454)

ISSN (任意): 1570-9639
ISSN: 1570-9639 (pISSN: 1570-9639, eISSN: 1878-1454)
Title: Biochimica et biophysica acta. Proteins and proteomics
Title(ISO): Biochim Biophys Acta Proteins Proteom
Publisher: Elsevier BV
 (NLM Catalog  (Scopus  (CrossRef (Scopus information is found. [need login])
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(必須): 1794 [継承]
(必須): 10 [継承]
(必須): 1496 1504 [継承]
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年月日 (必須): 西暦 2009年 6月 23日 (平成 21年 6月 23日) [継承]
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DOI (任意): 10.1016/j.bbapap.2009.06.014    (→Scopusで検索) [継承]
PMID (任意): 19555779    (→Scopusで検索) [継承]
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備考 (任意): 1.(英) Article.ELocationID: 10.1016/j.bbapap.2009.06.014  (日)    [継承]
2.(英) Article.Affiliation: Analytical Research Center for Experimental Sciences, Saga University, 1 Honjo-machi, Saga 840-8502, 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 ● Ryushi Kawakami, Haruhiko Sakuraba, Shuichiro Goda, Hideaki Tsuge and Toshihisa Ohshima : Refolding, characterization and crystal structure of (S)-malate dehydrogenase from the hyperthermophilic archaeon Aeropyrum pernix., Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, Vol.1794, No.10, 1496-1504, 2009.
欧文冊子 ● Ryushi Kawakami, Haruhiko Sakuraba, Shuichiro Goda, Hideaki Tsuge and Toshihisa Ohshima : Refolding, characterization and crystal structure of (S)-malate dehydrogenase from the hyperthermophilic archaeon Aeropyrum pernix., Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, Vol.1794, No.10, 1496-1504, 2009.

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