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Literature summary extracted from

  • Ogasahara, K.; Nakamura, M.; Nakura, S.; Tsunasawa, S.; Kato, I.; Yoshimoto, T.; Yutani, K.
    The unusually slow unfolding rate causes the high stability of pyrrolidone carboxyl peptidase from a hyperthermophile, Pyroccoccus furiosus: equilibrium and kinetic studies of guanidine hydrochloride-induced unfolding and refolding (1998), Biochemistry, 37, 17537-17544.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
3.4.19.3 C142S/C188S the mutant enzyme is used in unfolding and refolding experiments to exclude the complexity in reaction due to oxidation of SH groups Pyrococcus furiosus

General Stability

EC Number General Stability Organism
3.4.19.3 wild-type and mutant enzyme C142S/C188S, the anomalous high stability of the hyperthermophilic enzyme originates from the unusually slow rate of unfolding reaction during treatment with guanidine-hydrochloride Pyrococcus furiosus

Organism

EC Number Organism UniProt Comment Textmining
3.4.19.3 Bacillus amyloliquefaciens
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3.4.19.3 Pyrococcus furiosus
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