EC Number   |
General Information |
Reference |
|---|
   2.5.1.58 | malfunction |
combined FTase/GGTase-I deficiency significantly reduces K-Ras-induced lung tumors and improves survival without obvious pulmonary toxicity |
738097 |
| 2.5.1.58 | malfunction |
combined FTase/GGTase-I deficiency significantly reduces K-Ras-induced lung tumors and improves survival without obvious pulmonary toxicity. Enzyme deficiency is involved in progeria, also known as Hutchinson-Gilford progeria syndrome, a fatal and rare genetic disease caused by the mutation of the LMNA gene |
738097 |
| 2.5.1.58 | more |
comparison of the substrate specificities of PFTases from three organisms, Rattus norvegicus, Saccharomyces cerevisiae, and Candida albicans, using CVa2X libraries, overview. Rattus norvegicus PFTase shares more peptide substrates with Saccharomyces cerevisiae PFTase than with Candida albicans PFTase |
737324 |
| 2.5.1.58 | more |
FTase and GGTase-I recognize the same CAAX sequence motif in a protein substrate and catalyze the attachment of farnesyl and geranygeranyl groups to the protein, respectively. The X is the key residue that determines the farnesylation or geranylgeranylation of the CAAX-containing protein. When X is serine, methionine or glutamine the protein substrate is preferentially activated by FTase, but when X is leucine or phenylalanine the protein substrate is preferentially activated by GGTase-I |
738097 |
| 2.5.1.58 | more |
ligand interaction analysis with FTase alpha subunit, mass spectrometry, overview. Modelling of dimeric FTase alpha subunits |
737611 |
| 2.5.1.58 | physiological function |
dimerization of subunits alpha and beta is required for farnesylation activity |
759946 |
| 2.5.1.58 | physiological function |
farnesyltransferase alpha subunit regulates vacuolar protein sorting-associated protein 4A (Vps4A)-dependent intracellular trafficking through recycling endosomes. The enzyme FTase alpha controls trafficking of transferrin receptor upstream of thie Vps4A protein |
737611 |
| 2.5.1.58 | physiological function |
FTase catalyzes farnesyl isoprenoid linked to the cysteine residue of the CAAX protein through a thioether linkage, which will enhance the hydrophobicity of the CAAX protein. Meanwhile, the formed CAAX-protein-isoprenoid complex is attached to the endoplasmic reticulum surface |
738097 |
| 2.5.1.58 | physiological function |
FTase catalyzes farnesyl isoprenoid linked to the cysteine residue of the CAAX protein through a thioether linkage, which will enhance the hydrophobicity of the CAAX protein. Meanwhile, the formed CAAX-protein-isoprenoid complex is attached to the endoplasmic reticulum surface. FTase is involvedin hematologic malignancies due via prenylation of Ras. The enzyme is also important in the pathological process of neurological diseases, such as neuroinflammatory disease and Parkinson's disease |
738097 |
| 2.5.1.58 | physiological function |
heat-intolerant mutant hit5 carries a mutation in the beta-subunit of the protein farnesyltransferase. The mutant is thermosensitive to prolonged heat incubation at 37°C for 4 d but thermotolerant to sudden heat shock at 44°C for 40 min. hit5/abi3 and hit5/aba3 double mutants have the same temperature-dependent phenotypes as hit5. Exogenous supplementation of neither abscisic acid nor the abscisic acid synthesis inhibitor fluridone alter the temperature-dependent phenotypes of hit5. The hit5/hsp101 double mutant is still sensitive to prolonged heat incubation, yet its ability to tolerate sudden heat shock is lost |
759854 |
