Activation of Pyrococcus furiosus alkaline phosphatase by divalent metal ions

研究成果: Contribution to journalArticle査読

4 被引用数 (Scopus)

抄録

Treatment of a hyperthermophilic enzyme, alkaline phosphatase from Pyrococcus furiosus (PfuAP), with EDTA completely deactivated PfuAP, indicating that the presence of one or more divalent metal ions is essential for its catalytic activity. Subsequent addition of various divalent metal ions to the apoprotein recovered the enzymatic activity and, in particular, the addition of Co(II) resulted in an over 50-fold increase in activity compared with PfuAP before EDTA treatment. Intriguingly, PfuAP with Co(II) exhibited weaker stability toward heat treatment, suggesting that Co2+ destabilizes the tertiary structure of PfuAP at high temperature.

本文言語英語
ページ(範囲)2055-2060
ページ数6
ジャーナルBiotechnology letters
34
11
DOI
出版ステータス出版済み - 10 2012

All Science Journal Classification (ASJC) codes

  • バイオテクノロジー
  • バイオエンジニアリング
  • 応用微生物学とバイオテクノロジー

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