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KMID : 1236020190470040574
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Microbiology and Biotechnology Letters
2019 Volume.47 No. 4 p.574 ~ p.580
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Characterization of ATPase Activity of Chaperonin from the Hyperthermophilic Archaeon Pyrococcus horikoshii
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Choi Seong-Seok
Kim Se-Won
Seo Yong-Bae
Kim Kun-Do
Lee Hye-Young
Kim Yeon-Hee
Jeon Sung-Jong
Nam Soo-Wan
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Abstract
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ATP drives the conformational change of the group II chaperonin from the open lid substrate-binding conformation to the closed lid conformation to encapsulate an unfolded protein in the central cavity. It is thought that the folding activity of group II chaperonin is strongly correlated with the ATP-dependent conformational change ability. In order to confirm the dependence of the reaction temperature and ATP concentration of PhCpn, the ATPase activities were measured under different reaction temperatures and ATP concentrations. The maximal ATPase activity of PhCpn was observed at 80℃ and 3 mM ATP concentration. As a result of ATPase activity according to the type of salt ions, the highest activity was observed at 300 mM LiCl among the univalent cations and 5 mM MgCl2 among the divalent cations, respectively. The values of Km and Vmax for ATP substrate were estimated as 2.17 mM and 833.3 μM/min, respectively. This results provide the enzymatic information of PhCpn when the prolonged and high activities of pharmaceutical and industrial proteins (or enzymes), by using chaperonin molecules, are required.
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KEYWORD
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ATPase activity, chaperonin, enzymatic parameters, Pyrococcus horikoshii
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