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Literature summary for 2.5.1.58 extracted from

  • Wu, Z.; Demma, M.; Strickland, C.L.; Syto, R.; Le, H.V.; Windsor, W.T.; Weber, P.C.
    High-level expression, purification, kinetic characterization and crystallization of protein farnesyltransferase b-subunit C-terminal mutants (1999), Protein Eng., 12, 341-348.
    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 Homo sapiens
medicine evidence that inhibitors of enzyme could be effective therapeutic agents in treatment of many human cancers Rattus norvegicus

Cloned(Commentary)

Cloned (Comment) Organism
enzyme produced using an Sf9 cell overexpression Homo sapiens
translationally coupled two-cistron expression system for enzyme in Escherichia coli Rattus norvegicus

Crystallization (Commentary)

Crystallization (Comment) Organism
a new crystalline form of enzyme for the mutant truncated 10 residues at the C-terminus Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
additional information
-
 Homo sapiens
additional information three beta-subunit C-terminal truncation mutants, deletion of 5, 10 and 14 residues, the overall catalytic efficiency of enzyme decreases gradually with increasing C-terminal deletion Rattus norvegicus

Inhibitors

Inhibitors Comment Organism Structure
KKSKTKCVIM
-
 Rattus norvegicus
KKTKSKCVIM
-
 Rattus norvegicus
additional information enzyme inhibited by peptides containing the C-terminal CAAX sequence Rattus norvegicus
NH2-KTKCVFM
-
 Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information comparison of Km of mutant enzymes Homo sapiens
additional information
-
 additional information comparison of Km of mutant enzymes Rattus norvegicus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
44000
-
 alpha,beta, 1 * 50000 + 1 * 44000, SDS-PAGE, 1 * 46200 + 1 * 487000, mass spectroscopy Rattus norvegicus
46200
-
 alpha,beta, 1 * 50000 + 1 * 44000, SDS-PAGE, 1 * 46200 + 1 * 487000, mass spectroscopy Rattus norvegicus
50000
-
 alpha,beta, 1 * 50000 + 1 * 44000, SDS-PAGE, 1 * 46200 + 1 * 487000, mass spectroscopy Rattus norvegicus
487000
-
 alpha,beta, 1 * 50000 + 1 * 44000, SDS-PAGE, 1 * 46200 + 1 * 487000, mass spectroscopy Rattus norvegicus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
farnesyl diphosphate + protein-cysteine Homo sapiens
-
 S-farnesyl protein + diphosphate
-
 ?
farnesyl diphosphate + protein-cysteine Rattus norvegicus
-
 S-farnesyl protein + diphosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-
Rattus norvegicus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme Rattus norvegicus

Reaction

Reaction Comment Organism Reaction ID
farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate kinetic mechanism Rattus norvegicus
a
farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate enzyme constitutes the protein prenyltransferase family of enzymes Rattus norvegicus
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
farnesyl diphosphate + protein-cysteine
-
 Homo sapiens diphosphate + S-farnesyl protein
-
 ?
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 substrate are: Ras superfamiliy and Ras-related proteins for example Rap, Rab, Rac and Ral, large G proteins, nuclear lamins, rhodopsin kinase and the retinal cGMP phosphodiesterase Rattus norvegicus diphosphate + S-farnesyl protein
-
 ?
farnesyl diphosphate + protein-cysteine
-
 Homo sapiens S-farnesyl protein + diphosphate
-
 ?
farnesyl diphosphate + protein-cysteine
-
 Rattus norvegicus S-farnesyl protein + diphosphate
-
 ?

Subunits

Subunits Comment Organism
heterodimer alpha,beta, 1 * 50000 + 1 * 44000, SDS-PAGE, 1 * 46200 + 1 * 487000, mass spectroscopy Rattus norvegicus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
 additional information comparison of kcat of mutant enzymes Homo sapiens
additional information
-
 additional information comparison of kcat of mutant enzymes Rattus norvegicus

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.00012
-
 NH2-KTKCVFM
-
 Rattus norvegicus
0.0013
-
 KKSKTKCVIM
-
 Rattus norvegicus