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Literature summary for 2.5.1.58 extracted from

  • Chakrabarti, D.; Da Silva, T.; Barger, J.; Paquette, S.; Patel, H.; Patterson, S.; Allen, C.M.
    Protein Farnesyltransferase and protein prenylation in Plasmodium falciparum (2002), J. Biol. Chem., 277, 42066-42073.
    View publication on PubMed

Application

Application Comment Organism
medicine enzyme a target in developing drug therapy for malaria Plasmodium falciparum

Inhibitors

Inhibitors Comment Organism Structure
FTI-277
-
Plasmodium falciparum
GGTI-298
-
Plasmodium falciparum
additional information
-
Plasmodium falciparum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
farnesyl diphosphate + protein-cysteine Plasmodium falciparum potential role for cell cycle S-farnesyl protein + diphosphate
-
?

Organism

Organism UniProt Comment Textmining
Plasmodium falciparum
-
protozoa malaria parasite, infected erythrocytes
-

Source Tissue

Source Tissue Comment Organism Textmining
additional information appearance during specific stages of Plasmodium falciparum differentiation Plasmodium falciparum
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
farnesyl diphosphate + protein-cysteine
-
Plasmodium falciparum diphosphate + S-farnesyl protein
-
?
farnesyl diphosphate + protein-cysteine potential role for cell cycle Plasmodium falciparum S-farnesyl protein + diphosphate
-
?