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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.
    View publication on PubMed

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
a
2.5.1.58 farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate enzyme constitutes the protein prenyltransferase family of enzymes Rattus norvegicus
a

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
-
 ?