Literature summary extracted from
Long, S.B.; Casey, P.J.; Beese, L.S.
Reaction path of protein farnesyltransferase at atomic resolution (2002), Nature, 419, 645-650.
Application
EC Number |
Application |
Comment |
Organism |
---|
2.5.1.58 |
medicine |
evidence that inhibitors of enzyme could be effective therapeutic agents in treatment of many human cancers |
Rattus norvegicus |
2.5.1.58 |
medicine |
prime target for development of anticancer therapeutics |
Rattus norvegicus |
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
2.5.1.58 |
enzyme produced using an Sf9 cell overexpression |
Rattus norvegicus |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
2.5.1.58 |
two crystal structures of enzyme complex: one containing farnesylated Ras peptide product alone and a complex that contains both the farnesylated peptide and an additional farnesyl diphosphate substrate |
Rattus norvegicus |
Inhibitors
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
2.5.1.58 |
additional information |
two primary modes of inhibition: blocking the peptide substrate site and blocking the exit groove |
Rattus norvegicus |
|
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
2.5.1.58 |
Mg2+ |
required |
Rattus norvegicus |
|
2.5.1.58 |
Zn2+ |
the zinc ion activates the cysteine thiolate for nucleophilic attack on the C1 atom of the farnesyl diphosphate substrate |
Rattus norvegicus |
|
Natural Substrates/ Products (Substrates)
EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
---|
2.5.1.58 |
farnesyl diphosphate + protein-cysteine |
Rattus norvegicus |
process required for the transforming activity of oncogenic variants of Ras, making enzyme a prime target for anticancer therapeutics |
S-farnesyl protein + diphosphate |
- |
? |
|
2.5.1.58 |
farnesyl diphosphate + protein-cysteine |
Rattus norvegicus |
process necessary for the subcellular localisation of substrate to the plasma membrane |
S-farnesyl protein + diphosphate |
- |
? |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
2.5.1.58 |
Rattus norvegicus |
- |
- |
- |
Reaction
EC Number |
Reaction |
Comment |
Organism |
Reaction ID |
---|
2.5.1.58 |
farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate |
kinetic mechanism |
Rattus norvegicus |
|
2.5.1.58 |
farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate |
enzyme constitutes the protein prenyltransferase family of enzymes |
Rattus norvegicus |
|
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
2.5.1.58 |
farnesyl diphosphate + protein-cysteine |
posttranslational lipid modification in which a 15-carbon farnesyl isoprenoid is linked via a thioether bond to specific cysteine residues of proteins, the reactive cysteine is located in the C-terminal Ca1a2X motif in which C is the modified cysteine, a1 and a2 are often an aliphatic residue, and X is Ser, Met, Ala or Gln |
Rattus norvegicus |
diphosphate + S-farnesyl protein |
- |
? |
|
2.5.1.58 |
farnesyl diphosphate + protein-cysteine |
process required for the transforming activity of oncogenic variants of Ras, making enzyme a prime target for anticancer therapeutics |
Rattus norvegicus |
S-farnesyl protein + diphosphate |
- |
? |
|
2.5.1.58 |
farnesyl diphosphate + protein-cysteine |
process necessary for the subcellular localisation of substrate to the plasma membrane |
Rattus norvegicus |
S-farnesyl protein + diphosphate |
- |
? |
|