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Literature summary for 3.4.22.B69 extracted from

  • Alam, B.; Biswas, S.
    Inhibition of Plasmodium falciparum cysteine protease falcipain-2 by a human cross-class inhibitor serpinB3 A mechanistic insight (2019), Biochim. Biophys. Acta, 1867, 854-865 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Plasmodium falciparum

Crystallization (Commentary)

Crystallization (Comment) Organism
docking of serpinB3 Plasmodium falciparum

Inhibitors

Inhibitors Comment Organism Structure
SERPINB3 potent cross-class inhibitor of cysteine cathepsins L, K, S and papain, inhibits proteolytic activities as well as specific hemoglobinolytic activity of FP2 via noncovalent interaction. Disease state mutant serpin-Gly351Ala displays better anti-protease activity against FP2 Plasmodium falciparum

Organism

Organism UniProt Comment Textmining
Plasmodium falciparum Q9N6S8
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
VLK-4-nitroanilide + H2O
-
Plasmodium falciparum VLK + 4-nitronaniline
-
?

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.000338
-
SERPINB3 pH not specified in the publication, temperature not specified in the publication Plasmodium falciparum