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Literature summary for 2.5.1.58 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
Search for more literature for 2.5.1.58

Application

Application Comment Organism
medicine
-
 Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
K164N mutation abolishes enzyme activity Rattus norvegicus
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
N199D mutation reduces enzyme activity Rattus norvegicus
R172E mutation reduces enzyme activity Rattus norvegicus
W203H mutation reduces enzyme activity Rattus norvegicus
Y166F mutation reduces enzyme activity Rattus norvegicus

General Stability

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

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ required Rattus norvegicus

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Rattus norvegicus

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
 Rattus norvegicus
-

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
-
 ?
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

Subunits Comment Organism
heterodimer alpha,beta, 1 * 49000 + 1 * 46000, SDS-PAGE Rattus norvegicus
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