EC Number | Application | Comment | Organism |
---|---|---|---|
2.5.1.58 | medicine | evidence that inhibitors of enzyme could be effective therapeutic agents in treatment of many human cancers | Rattus norvegicus |
2.5.1.58 | medicine | prime target for development of anticancer therapeutics | Rattus norvegicus |
EC Number | Cloned (Comment) | Organism |
---|---|---|
2.5.1.58 | enzyme produced using an Sf9 cell overexpression | Rattus norvegicus |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
2.5.1.58 | 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 |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
2.5.1.58 | Zn2+ | required | Rattus norvegicus |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.5.1.58 | 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 | - |
? | |
2.5.1.58 | farnesyl diphosphate + protein-cysteine | Rattus norvegicus | process necessary for the subcellular localisation of substrate to the plasma membrane | S-farnesyl protein + diphosphate | - |
? | |
2.5.1.58 | farnesyl diphosphate + protein-cysteine | Rattus norvegicus | enzyme responsible for catalysing isoprene lipid modifications | S-farnesyl protein + diphosphate | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.5.1.58 | Rattus norvegicus | - |
- |
- |
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 | substrates are cellular proteins such as Ras at a cysteine residue near their carboxy-terminus | Rattus norvegicus | diphosphate + S-farnesyl protein | - |
? | |
2.5.1.58 | 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 | - |
? | |
2.5.1.58 | farnesyl diphosphate + protein-cysteine | process necessary for the subcellular localisation of substrate to the plasma membrane | Rattus norvegicus | S-farnesyl protein + diphosphate | - |
? | |
2.5.1.58 | farnesyl diphosphate + protein-cysteine | enzyme responsible for catalysing isoprene lipid modifications | Rattus norvegicus | S-farnesyl protein + diphosphate | - |
? |