Thermostable Enzymes of Hyperthermophilic Archaea

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  • IMANAKA Tadayuki
    Dept. of Synth. Chem. and Biol. Chem., Graduate School of Engineering, Kyoto University
  • FUJIWARA Shinsuke
    Dept. of Biotechnology, Graduate School of Engineering, Osaka University

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  • 超好熱菌の耐熱性酵素
  • チョウ コウネツキン ノ タイネツセイ コウソ

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Abstract

Phylogenetic tree based on 16S rRNA or protein sequences shows that all known organisms are related suggesting a common ancestor. All organisms are divided into three groups, eukarya, bacteria, and archaea. Most proteins produced in archaea have eukaryotic features, which indicate close relationship of archaea and eukarya in the course of evolution. Especially, hyperthermophilic archaea are considered to evolve most slowly in archaea domain remaining ancestral features of higher eukaryotes. Pyrococcus sp. KOD 1 is a newly isolated hyperthermophilic archaeon from a solfatara at a wharf of Kodakara Island, Kagoshima Japan. The optimum temperature for KOD 1 cell growth is 95°C. Unusual enzyme characteristics on KOD 1 protease, amylase, DNA polymerase, glutamate synthase, Rec protein, aspartyl tRNA synthetase and molecular chaperonin are discussed. Some applications using KOD 1 enzymes are also introduced, e.g. rapid PCR by KOD 1 DNA polymerase and in vitro stabilization and in vivo solubilization of foreign proteins by KOD 1 chaperonin.

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