Application | Comment | Organism |
---|---|---|
medicine | evidence that inhibitors of enzyme could be effective therapeutic agents in treatment of many human cancers | Rattus norvegicus |
Cloned (Comment) | Organism |
---|---|
wild-type enzyme and mutant enzymes expressed in Escherichia coli | Rattus norvegicus |
Protein Variants | Comment | Organism |
---|---|---|
D297A | beta-subunit, 200fold decrease in kcat | Rattus norvegicus |
D297N | beta-subunit, 200fold decrease in kcat | Rattus norvegicus |
H362A | beta-subunit, 50fold decrease in kcat | Rattus norvegicus |
H362Q | beta-subunit, 500fold decrease in kcat | Rattus norvegicus |
H362Q | beta-subunit, 15fold decrease in kcat | Rattus norvegicus |
additional information | all five mutant enzymes bind farnesyl diphosphate with similar affinity to that of the wild-type enzyme, indicating that the targeted residues neither directly nor indirectly influence the farnesyl diphosphate binding site, only the wild-type enzyme able to bind zinc, while all five of the mutant enzymes lose this ability | Rattus norvegicus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | wild-type enzyme and the H362E mutant possess similar Km for H-Ras | Rattus norvegicus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Zn2+ | zinc metalloenzyme | Rattus norvegicus | |
Zn2+ | zinc ion is coordinated by three residues in the beta subunit: Asp-297, Cys-299, and H-362 and a water molecule | Rattus norvegicus | |
Zn2+ | zinc plays a major catalytic role in the mechanism of enzyme, zinc seems to activate the cysteine thiol of protein substrate for attack at C-1 of the isoprenoid substrate | Rattus norvegicus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rattus norvegicus | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
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 | - |
? |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | comparison of kcat of wild-type and mutant enzymes | Rattus norvegicus |