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Literature summary extracted from

  • Dunten, P.; Kammlott, U.; Crowther, R.; Weber, D.; Palermo, R.; Birktoft, J.
    Protein farnesyltransferase: Structure and implications for substrate binding (1998), Biochemistry, 37, 7907-7912.
    View publication on PubMed

Application

EC Number Application Comment Organism
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 coexpression of alpha and beta subunits of enzyme with a recombinant baculovirus Rattus norvegicus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.5.1.58 farnesyl diphosphate and peptide substrate can be accommodated in the hydrophobic active-site barrel, with the sole charged residue inside the barrel, Arg202 of the beta-subunit, forming a salt bridge with the negatively charged carboxy terminus of peptide substrate Rattus norvegicus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.5.1.58 Zn2+ zinc ion is coordinated by three residues in the beta subunit: Asp-297, Cys-299, and H-362 and a water molecule 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
-
 ?
2.5.1.58 farnesyl diphosphate + protein-cysteine Rattus norvegicus A series of steps modifies the C-terminus of Ras. Enzyme catalyses the first of these steps by transferring the farnesyl group from farnesyl diphosphates to the cysteine side chain in the CAAX sequence motif at the C-terminus of Ras 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 both subunits would appear to have a role in binding and orienting the leaving group of farnesyl diphosphate approximately for catalysis 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
-
 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
-
 ?
2.5.1.58 farnesyl diphosphate + protein-cysteine A series of steps modifies the C-terminus of Ras. Enzyme catalyses the first of these steps by transferring the farnesyl group from farnesyl diphosphates to the cysteine side chain in the CAAX sequence motif at the C-terminus of Ras Rattus norvegicus S-farnesyl protein + diphosphate
-
 ?