| Item type |
学術雑誌論文 / Journal Article(1) |
| 公開日 |
2012-03-27 |
| タイトル |
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|
タイトル |
Refolding, characterization and crystal structure of (S)-malate dehydrogenase from the hyperthermophilic archaeon Aeropyrum pernix |
|
言語 |
en |
| 言語 |
|
|
言語 |
eng |
| 資源タイプ |
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資源タイプ識別子 |
http://purl.org/coar/resource_type/c_6501 |
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資源タイプ |
journal article |
| アクセス権 |
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アクセス権 |
open access |
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アクセス権URI |
http://purl.org/coar/access_right/c_abf2 |
| 著者 |
川上, 竜巳
櫻庭, 春彦
郷田, 秀一郎
津下, 英明
大島, 敏久
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| 抄録 |
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内容記述タイプ |
Abstract |
|
内容記述 |
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. |
|
言語 |
en |
| 書誌情報 |
en : Biochimica et biophysica acta
巻 1794,
号 10,
p. 1496-1504,
発行日 2009-06-23
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| ISSN |
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収録物識別子タイプ |
PISSN |
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収録物識別子 |
0006-3002 |
| 書誌レコードID |
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収録物識別子タイプ |
NCID |
|
収録物識別子 |
AA00564635 |
| 権利 |
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言語 |
en |
|
権利情報 |
Copyright © 2009 Elsevier B.V. All rights reserved. |
| 論文ID（NAID） |
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関連タイプ |
isVersionOf |
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識別子タイプ |
NAID |
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関連識別子 |
120007015445 |
| PubMed番号 |
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識別子タイプ |
PMID |
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関連識別子 |
19555779 |
| 関連サイト |
|
|
関連タイプ |
isVersionOf |
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|
識別子タイプ |
DOI |
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|
関連識別子 |
https://doi.org/10.1016/j.bbapap.2009.06.014 |
| 関連サイト |
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|
関連タイプ |
isVersionOf |
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|
識別子タイプ |
NAID |
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|
関連識別子 |
80020538114 |
| 著者版フラグ |
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出版タイプ |
AM |
|
出版タイプResource |
http://purl.org/coar/version/c_ab4af688f83e57aa |
| キーワード |
|
|
言語 |
en |
|
主題Scheme |
Other |
|
主題 |
Aeropyrum pernix |
| キーワード |
|
|
言語 |
en |
|
主題Scheme |
Other |
|
主題 |
[LDH-like] MDH |
| キーワード |
|
|
言語 |
en |
|
主題Scheme |
Other |
|
主題 |
Malate dehydrogenase |
| キーワード |
|
|
言語 |
en |
|
主題Scheme |
Other |
|
主題 |
Hyperthermophilic archaea |
| キーワード |
|
|
言語 |
en |
|
主題Scheme |
Other |
|
主題 |
Refolding |
| キーワード |
|
|
言語 |
en |
|
主題Scheme |
Other |
|
主題 |
Crystal structure |
| KEID |
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|
値 |
2183 |
AA11685085_1794_10_1496 (1.3 MB)
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