Literature summary for 3.4.22.B69 extracted from

Ghogomu, J.; Nkungli, N.
DFT studies and topological analyses of electron density on acetophenone and propiophenone thiosemicarbazone derivatives as covalent inhibitors of falcipain-2, a major Plasmodium falciparum cysteine protease (2017), Phys. Chem. Res., 5, 795-817 .

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Inhibitors

Inhibitors	Comment	Organism	Structure
amino[(2E)-2-[1-(4-methoxyphenyl)ethylidene]hydrazinyl]methanethiol	-	Plasmodium falciparum
additional information	density functional theory calculations of binding of different derivatives of acetophenone thiosemicarbazone and propiophenone thiosemicarbazone acting as inhibitors reveal covalent interaction between the thiocarbonyl carbon of the thiosemicarbazone moiety and the thiolate sulfur of the active site cysteine residue of falcipain-2. Acetophenone thiosemicarbazone and propiophenone thiosemicarbazone derivatives are potential reversible covalent inhibitors of falcipain-2	Plasmodium falciparum

Organism

Organism	UniProt	Comment	Textmining
Plasmodium falciparum	Q9N6S8	-	-

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Release 2023.1 (January 2023)