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Literature summary for 3.4.23.39 extracted from

  • Xiao, H.; Dee, D.; Yada, R.Y.
    The native conformation of plasmepsin II is kinetically trapped at neutral pH (2011), Arch. Biochem. Biophys., 513, 102-109.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Plasmodium falciparum

Organism

Organism UniProt Comment Textmining
Plasmodium falciparum
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Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification the PMII zymogen utilizes a prosegment-catalyzed folding mechanism Plasmodium falciparum

Renatured (Commentary)

Renatured (Comment) Organism
differential scanning calorimetry reveals that the native state of PMII is irreversibly unfolded, and in the pH range of 6.5-8.0, PMII refolds to a denatured state with higher thermal stability than native state. The denatured state can also be formed upon partially unfolding PMII at pH 11.0 and 37°C for 2 h, followed by adjustment to a pH in the range of 6.5-8.0. While the denatured state can be folded/unfolded reversibly, the native state exists as a kinetically trapped state. The native state is kinetically trapped by an unfolding barrier of 25.5 kcal/mol, and yet once unfolded, is prevented from folding by a comparable folding barrier Plasmodium falciparum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
EDANS-CO-CH2-CH2-CO-L-Ala-L-Leu-L-Glu-L-Arg-L-Met-L-Phe-L-Leu-L-Ser-L-Phe-L-Pro-Dap(DABCYL)-OH + H2O
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Plasmodium falciparum ?
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?