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Literature summary for 2.5.1.58 extracted from
- Substrate characterization of the Saccharomyces cerevisiae protein farnesyltransferase and type-I protein geranylgeranyltransferase (1994), Biochim. Biophys. Acta, 1205, 39-48.
Application
| Application | Comment | Organism |
|---|---|---|
| medicine | evidence that inhibitors of enzyme could be effective therapeutic agents in treatment of many human cancers | Saccharomyces cerevisiae |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli | Saccharomyces cerevisiae |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Saccharomyces cerevisiae |  |
| Zn2+ | required | Saccharomyces cerevisiae | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| farnesyl diphosphate + protein-cysteine | Saccharomyces cerevisiae | process required for the transforming activity of oncogenic variants of Ras, making enzyme a prime target for anticancer therapeutics | S-farnesyl protein + diphosphate | - |
? | |
| farnesyl diphosphate + protein-cysteine | Saccharomyces cerevisiae | process necessary for the subcellular localisation of substrate to the plasma membrane | S-farnesyl protein + diphosphate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharomyces cerevisiae | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant enzyme | Saccharomyces cerevisiae |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate | enzyme constitutes the protein prenyltransferase family of enzymes | Saccharomyces cerevisiae | |
| farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate | The enzyme preferentially farnesylates CaaX sequences ending in methionine, cysteine or serine. Enzyme also attaches geranylgeraniol to some CaaX sequences ending in methionine, leucine and cysteine. Substrate overlap may occur between the Saccharomyces cerevisae farnesyl transferase and geranylgeranyltransferase types I in vivo | Saccharomyces cerevisiae |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| farnesyl diphosphate + protein-cysteine | preferred CaaX-substrate: CAIM | Saccharomyces cerevisiae | diphosphate + S-farnesyl protein | - |
? | |
| farnesyl diphosphate + protein-cysteine | process required for the transforming activity of oncogenic variants of Ras, making enzyme a prime target for anticancer therapeutics | Saccharomyces cerevisiae | S-farnesyl protein + diphosphate | - |
? | |
| farnesyl diphosphate + protein-cysteine | process necessary for the subcellular localisation of substrate to the plasma membrane | Saccharomyces cerevisiae | S-farnesyl protein + diphosphate | - |
? | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.9 | - |
- |
Saccharomyces cerevisiae |
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