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Literature summary extracted from

  • Huang, C.c.; Hightower, K.E.; Fierke, C.A.
    Mechanistic studies of rat protein farnesyltransferase indicate an associative transition state (2000), Biochemistry, 39, 2593-2602.
    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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.5.1.58 expression in Escherichia coli Rattus norvegicus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.5.1.58 Cd2+ substitution of the active site zinc with cadmium increases the affinity of the peptide substrate and decreases the rate constant for the chemical step Rattus norvegicus
2.5.1.58 Mg2+ magnesium is not required for formation of the thioether product but the presence increases the single-turnover rate constant by several orders of magnitude at saturating enzyme and substrate concentrations Rattus norvegicus
2.5.1.58 Mg2+ appears to coordinate the diphosphate moiety of farnesyl diphosphate Rattus norvegicus
2.5.1.58 additional information a metal-assisted nucleophile is involved in the catalytic mechanism of enzyme Rattus norvegicus
2.5.1.58 Zn2+ zinc metalloenzyme 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 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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.58 farnesyl diphosphate + protein-cysteine prenylation, farnesylation, substrates are Ras, nuclear lamins, transducin gamma subunit, protein substrate motif: Cys-aliphatic-aliphatic-X, X: M, S, Q, A, F Rattus norvegicus diphosphate + S-farnesyl protein
-
 ?
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
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.5.1.58 additional information
-
 additional information comparison of kcat of metal-substituted enzymes, kcat for product formation decreases for C3 fluoromethyl farnesyl diphosphate substrates, paralleling the number of fluorines at the C3 methyl position Rattus norvegicus