論文

国際誌
2018年11月

Enzymological characteristics of a novel archaeal dye-linked D-lactate dehydrogenase showing loose binding of FAD.

Extremophiles : life under extreme conditions
  • Takenori Satomura
  • ,
  • Junji Hayashi
  • ,
  • Tatsuya Ohshida
  • ,
  • Haruhiko Sakuraba
  • ,
  • Toshihisa Ohshima
  • ,
  • Shin-Ichiro Suye

22
6
開始ページ
975
終了ページ
981
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1007/s00792-018-1054-3

A gene-encoding a dye-linked D-lactate dehydrogenase (Dye-DLDH) homolog was identified in the genome of the hyperthermophilic archaeon Thermoproteus tenax. The gene was expressed in Escherichia coli and the product was purified to homogeneity. The recombinant protein exhibited highly thermostable Dye-DLDH activity. To date, four types of Dye-DLDH have been identified in hyperthermophilic archaea (in Aeropyrum pernix, Sulfolobus tokodaii, Archaeoglobus fulgidus, and Candidatus Caldiarchaeum subterraneum). The amino acid sequence of T. tenax Dye-DLDH showed the highest similarity (45%) to A. pernix Dye-DLDH, but neither contained a known FAD-binding motif. Nonetheless, both homologs required FAD for enzymatic activity, suggesting that FAD binds loosely to the enzyme and is easily released unlike in other Dye-DLDHs. Our findings indicate that Dye-DLDHs from T. tenax and A. pernix are a novel type of Dye-DLDH characterized by loose binding of FAD.

リンク情報
DOI
https://doi.org/10.1007/s00792-018-1054-3
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/30206766

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