Application | Comment | Organism |
---|---|---|
drug development | the enzyme from Aspergillus fumigatus is a target for antifungal drug design | Aspergillus fumigatus |
Crystallization (Comment) | Organism |
---|---|
purified enzyme in complex with substrate farnesyl diphosphate, and inhibitors FPT-II-KCVVM, tipifarnib, andin ternary complex with farnesyl diphosphate and inhibitor ED5, X-ray diffraction structure determination and analysis at 1.45-1.90 A resolution, structure modelling | Aspergillus fumigatus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
ED5 | i.e. N-(N-tert-butoxycarbonylpiperidin-4-ylmethyl), N-(2-[((4-cyanophenyl)-3-methyl-3H-imidazol-4-ylmethyl)-amino]-ethyl) 2-methylbenzenesulfonamide, an ethylenediamine-scaffold inhibitor | Aspergillus fumigatus | |
farnesyl diphosphate inhibitor II | FPT-II | Aspergillus fumigatus | |
additional information | inhibitor structure-function analysis for antifungal drug design, comparisons of enzyme-inhibitor complex crystal structures from Aspergillus fumigatus with structures from Homo sapiens (PDB IDs 1KZO and 1TN6) and Cryptococcus neoformans (PDB ID 3Q75), Peptide-induced conformational changes, overview. Binding groove widening is consistent with variations in steady-state enzyme kinetics | Aspergillus fumigatus | |
tipifarnib | an ethylenediamine-scaffold inhibitor | Aspergillus fumigatus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | steady-state enzyme kinetics | Aspergillus fumigatus | |
0.00076 | - |
(2E,6E)-farnesyl diphosphate | pH 7.5, 25°C | Aspergillus fumigatus | |
0.00131 | - |
KGCVIM | pH 7.5, 25°C | Aspergillus fumigatus | |
0.00184 | - |
KGCVVM | pH 7.5, 25°C | Aspergillus fumigatus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Aspergillus fumigatus | |
Zn2+ | required | Aspergillus fumigatus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
(2E,6E)-farnesyl diphosphate + [protein]-L-cysteine | Aspergillus fumigatus | - |
S-(2E,6E)-farnesyl-[protein]-L-cysteine + diphosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Aspergillus fumigatus | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(2E,6E)-farnesyl diphosphate + KGCVIM | - |
Aspergillus fumigatus | S-(2E,6E)-farnesyl-KGCVIM + diphosphate | - |
? | |
(2E,6E)-farnesyl diphosphate + KGCVVM | - |
Aspergillus fumigatus | S-(2E,6E)-farnesyl-KGCVVM + diphosphate | - |
? | |
(2E,6E)-farnesyl diphosphate + [protein]-L-cysteine | - |
Aspergillus fumigatus | S-(2E,6E)-farnesyl-[protein]-L-cysteine + diphosphate | - |
? | |
(2E,6E)-farnesyl diphosphate + [protein]-L-cysteine | the reaction is catalyzed by protein farnesyltransferase on protein substrates bearing the C-terminal CaaX motif | Aspergillus fumigatus | S-(2E,6E)-farnesyl-[protein]-L-cysteine + diphosphate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
AfFTase | - |
Aspergillus fumigatus |
FTase | - |
Aspergillus fumigatus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Aspergillus fumigatus |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.12 | - |
(2E,6E)-farnesyl diphosphate | pH 7.5, 25°C | Aspergillus fumigatus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Aspergillus fumigatus |
IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|
0.000275 | - |
pH 7.5, 25°C | Aspergillus fumigatus | ED5 | |
0.0024 | - |
pH 7.5, 25°C | Aspergillus fumigatus | tipifarnib |