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著作: [川上 竜巳]/Sakuraba Haruhiko/Goda Shuichiro/Tsuge Hideaki/Ohshima Toshihisa/Refolding, characterization and crystal structure of (S)-malate dehydrogenase from the hyperthermophilic archaeon Aeropyrum pernix./[Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics]

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EID
262426
EOID
711461
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2013年9月11日(水) 18:54:34
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大家 隆弘
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川上 竜巳
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種別 必須 学術論文(審査論文)
言語 必須 英語
招待 推奨
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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])
    役割 任意
    貢献度 任意
    学籍番号 推奨
  2. (英) Sakuraba Haruhiko
    役割 任意
    貢献度 任意
    学籍番号 推奨
  3. (英) Goda Shuichiro
    役割 任意
    貢献度 任意
    学籍番号 推奨
  4. (英) Tsuge Hideaki
    役割 任意
    貢献度 任意
    学籍番号 推奨
  5. (英) Ohshima Toshihisa
    役割 任意
    貢献度 任意
    学籍番号 推奨
題名 必須

(英) Refolding, characterization and crystal structure of (S)-malate dehydrogenase from the hyperthermophilic archaeon Aeropyrum pernix.

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(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.

キーワード 推奨
  1. (英) Aeropyrum
  2. (英) Amino Acid Sequence
  3. (英) Base Sequence
  4. (英) Catalytic Domain
  5. (英) Crystallography, X-Ray
  6. (英) DNA Primers
  7. (英) DNA, Archaeal
  8. (英) Enzyme Stability
  9. (英) Genes, Archaeal
  10. (英) Malate Dehydrogenase
  11. (英) Models, Molecular
  12. (英) Molecular Sequence Data
  13. (英) Molecular Weight
  14. (英) Protein Folding
  15. (英) Protein Subunits
  16. (英) Recombinant Proteins
  17. (英) Sequence Homology, Amino Acid
  18. (英) Substrate Specificity
  19. (英) Thermodynamics
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])
必須 1794
必須 10
必須 1496 1504
都市 任意
年月日 必須 2009年 6月 23日
URL 任意
DOI 任意 10.1016/j.bbapap.2009.06.014    (→Scopusで検索)
PMID 任意 19555779    (→Scopusで検索)
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  1. (英) Article.ELocationID: 10.1016/j.bbapap.2009.06.014

  2. (英) Article.Affiliation: Analytical Research Center for Experimental Sciences, Saga University, 1 Honjo-machi, Saga 840-8502, Japan.

  3. (英) Article.PublicationTypeList.PublicationType: Journal Article

  4. (英) Article.PublicationTypeList.PublicationType: Research Support, Non-U.S. Gov't