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- W2010038324 abstract "A novel ATPase activity that was strongly activated in the presence of either cobalt or manganese ion was discovered in the chaperonin from hyperthermophilic Pyrococcus furiosus (Pfu‐cpn). Surprisingly, a significant ADPase activity was also detected under the same conditions. A more extensive search revealed similar nucleotide hydrolysis activities in other thermostable chaperonins. Chaperonin activity, i.e., thermal stabilization and refolding of malate dehydrogenase from the guanidine‐hydrochloride unfolded state were also detected for Pfu‐cpn under the same conditions. We propose that the novel cobalt/manganese‐dependent ATP/ADPase activity may be a common trait of various thermostable chaperonins." @default.
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- W2010038324 date "2005-12-06" @default.
- W2010038324 modified "2023-10-17" @default.
- W2010038324 title "A novel ATP/ADP hydrolysis activity of hyperthermostable group II chaperonin in the presence of cobalt or manganese ion" @default.
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- W2010038324 doi "https://doi.org/10.1016/j.febslet.2005.11.043" @default.
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