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Literature summary extracted from

  • Andres, D.A.; Goldstein, J.L.; Ho, Y.K.; Brown, M.S.
    Mutational analysis of a-subunit of protein farnesyltransferase. Evidence for a catalytic role (1993), J. Biol. Chem., 268, 1383-1390.
    View publication on PubMed

Application

EC Number Application Comment Organism
2.5.1.58 medicine
-
 Rattus norvegicus

Protein Variants

EC Number Protein Variants Comment Organism
2.5.1.58 K164N mutation abolishes enzyme activity Rattus norvegicus
2.5.1.58 additional information deletion of 51 amino acids at the NH2 terminus of alpha subunit: activity the same as wild-type enzyme, deletion of 106 amino acids at the NH2 terminus: complete loss of activity, suggesting that residues between 51 and 106 are important for activity, deletion of 5 amino acids at the COOH terminus reduces alpha-subunit activity to about 50% of activity of wild-type enzyme, removal of 20 amino acids at the COOH terminus: complete loss of activity Rattus norvegicus
2.5.1.58 N199D mutation reduces enzyme activity Rattus norvegicus
2.5.1.58 R172E mutation reduces enzyme activity Rattus norvegicus
2.5.1.58 W203H mutation reduces enzyme activity Rattus norvegicus
2.5.1.58 Y166F mutation reduces enzyme activity Rattus norvegicus

General Stability

EC Number General Stability Organism
2.5.1.58 all activity is lost, when the subunits are dissociated chemically Rattus norvegicus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.5.1.58 Zn2+ required Rattus norvegicus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.5.1.58 46000
-
 alpha,beta, 1 * 49000 + 1 * 46000, SDS-PAGE Rattus norvegicus
2.5.1.58 49000
-
 alpha,beta, 1 * 49000 + 1 * 46000, SDS-PAGE Rattus norvegicus

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.58 Rattus norvegicus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.5.1.58
-
 Rattus norvegicus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.5.1.58 brain
-
 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 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
-
 ?

Subunits

EC Number Subunits Comment Organism
2.5.1.58 heterodimer alpha,beta, 1 * 49000 + 1 * 46000, SDS-PAGE Rattus norvegicus
2.5.1.58 More the alpha-subunit plays a direct role in the catalytic reaction in addition to its role in the stabilization of the beta-subunit Rattus norvegicus