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Literature summary for 2.5.1.58 extracted from

  • Long, S.B.; Casey, P.J.; Beese, L.S.
    Cocrystal structure of protein farnesyltransferase complexed with a farnesyl diphosphate substrate (1998), Biochemistry, 37, 9612-9618.
    View publication on PubMed
Search for more literature for 2.5.1.58

Application

Application Comment Organism
medicine evidence that inhibitors of enzyme could be effective therapeutic agents in treatment of many human cancers Rattus norvegicus
medicine prime target for development of anticancer therapeutics Rattus norvegicus

Cloned(Commentary)

Cloned (Comment) Organism
enzyme produced using an Sf9 cell overexpression Rattus norvegicus

Crystallization (Commentary)

Crystallization (Comment) Organism
the isoprenoid moiety of farnsyl diphophate binds in an extended conformation in a hydrophobic cavity of the beta-subunit of the enzyme, and the diphosphate moiety binds to a positively charged cleft at the top of this cavity near the subunit interface Rattus norvegicus

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ required Rattus norvegicus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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
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 ?
farnesyl diphosphate + protein-cysteine Rattus norvegicus process necessary for the subcellular localisation of substrate to the plasma membrane S-farnesyl protein + diphosphate
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 ?
farnesyl diphosphate + protein-cysteine Rattus norvegicus enzyme responsible for catalysing isoprene lipid modifications S-farnesyl protein + diphosphate
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 ?

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
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-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
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 ?
farnesyl diphosphate + protein-cysteine substrates are cellular proteins such as Ras at a cysteine residue near their carboxy-terminus Rattus norvegicus diphosphate + S-farnesyl protein
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 ?
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
-
 ?
farnesyl diphosphate + protein-cysteine process necessary for the subcellular localisation of substrate to the plasma membrane Rattus norvegicus S-farnesyl protein + diphosphate
-
 ?
farnesyl diphosphate + protein-cysteine enzyme responsible for catalysing isoprene lipid modifications Rattus norvegicus S-farnesyl protein + diphosphate
-
 ?