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Literature summary for 2.5.1.58 extracted from
- Structure-based binding between protein farnesyl transferase and PRL-PTP of malaria parasite: an interaction study of prenylation process in Plasmodium (2016), J. Biomol. Struct. Dyn., 34, 2667-2678.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Plasmodium falciparum | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | enzyme-substrate interaction study using synthetic peptides as substrates, modelling of the enzyme interaction with substrate protein tyrosine phosphatase, protein-protein docking and molecular dynamics simulation, overview | Plasmodium falciparum | ? | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PfPFT | - |
Plasmodium falciparum |
| protein farnesyl transferase | - |
Plasmodium falciparum |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | protein prenylation is a posttranslational modification critical for many cellular processes such as DNA replication, signaling, and trafficking. Protein farnesyltransferase recognizes the CAAX motif on the protein substrate | Plasmodium falciparum |
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