Species | Target name | Source | Bibliographic reference |
---|---|---|---|
Plasmodium berghei | dihydroorotate dehydrogenase, putative | No references | |
Saccharomyces cerevisiae | dihydroorotate dehydrogenase | Starlite/ChEMBL | No references |
Plasmodium falciparum | dihydroorotate dehydrogenase | Starlite/ChEMBL | No references |
Plasmodium vivax | dihydroorotate dehydrogenase, mitochondrial precursor, putative | No references |
Activity type | Activity value | Assay description | Source | Reference |
---|---|---|---|---|
IC50 (binding) | = 42 nM | BindingDB_Patents: Enzymatic Assays. Type 2 DHODH activity was monitored with either the direct assay measuring the formation of orotate or via a chromogen reduction assay using DCIP. Although the extinction coefficient and absorption wavelength are preferable for the chromogen reduction assay, the inorganic electron acceptor DCIP can be utilized by DHODH as the final electron acceptor in lieu of CoQn when the endogenous substrate is at a low concentration. As such, the direct assay was used to measure the binding affinity of pfDHODH to CoQD and L-DHO. The enzymatic reaction was performed by varying the L-DHO concentration (1-400 µM) or CoQD concentration (1-200 µM) while keeping the other substrate constant and in excess. Inhibition of DHODH by small molecules was evaluated using the chromogen based assay with a final substrate concentration of 200 µM L-DHO, 18 µM CoQD, and 100 µM DCIP, unless otherwise noted. | ChEMBL. | No reference |
IC50 (binding) | = 60 nM | BindingDB_Patents: Enzymatic Assays. Type 2 DHODH activity was monitored with either the direct assay measuring the formation of orotate or via a chromogen reduction assay using DCIP. Although the extinction coefficient and absorption wavelength are preferable for the chromogen reduction assay, the inorganic electron acceptor DCIP can be utilized by DHODH as the final electron acceptor in lieu of CoQn when the endogenous substrate is at a low concentration. As such, the direct assay was used to measure the binding affinity of pfDHODH to CoQD and L-DHO. The enzymatic reaction was performed by varying the L-DHO concentration (1-400 uM) or CoQD concentration (1-200 uM) while keeping the other substrate constant and in excess. Inhibition of DHODH by small molecules was evaluated using the chromogen based assay with a final substrate concentration of 200 uM L-DHO, 18 uM CoQD, and 100 uM DCIP, unless otherwise noted. | ChEMBL. | No reference |
IC50 (binding) | = 64 nM | BindingDB_Patents: Enzymatic Assays. Type 2 DHODH activity was monitored with either the direct assay measuring the formation of orotate or via a chromogen reduction assay using DCIP. Although the extinction coefficient and absorption wavelength are preferable for the chromogen reduction assay, the inorganic electron acceptor DCIP can be utilized by DHODH as the final electron acceptor in lieu of CoQn when the endogenous substrate is at a low concentration. As such, the direct assay was used to measure the binding affinity of pfDHODH to CoQD and L-DHO. The enzymatic reaction was performed by varying the L-DHO concentration (1-400 µM) or CoQD concentration (1-200 µM) while keeping the other substrate constant and in excess. Inhibition of DHODH by small molecules was evaluated using the chromogen based assay with a final substrate concentration of 200 µM L-DHO, 18 µM CoQD, and 100 µM DCIP, unless otherwise noted. | ChEMBL. | No reference |
IC50 (binding) | = 70 nM | BindingDB_Patents: Enzymatic Assays. Type 2 DHODH activity was monitored with either the direct assay measuring the formation of orotate or via a chromogen reduction assay using DCIP. Although the extinction coefficient and absorption wavelength are preferable for the chromogen reduction assay, the inorganic electron acceptor DCIP can be utilized by DHODH as the final electron acceptor in lieu of CoQn when the endogenous substrate is at a low concentration. As such, the direct assay was used to measure the binding affinity of pfDHODH to CoQD and L-DHO. The enzymatic reaction was performed by varying the L-DHO concentration (1-400 µM) or CoQD concentration (1-200 µM) while keeping the other substrate constant and in excess. Inhibition of DHODH by small molecules was evaluated using the chromogen based assay with a final substrate concentration of 200 µM L-DHO, 18 µM CoQD, and 100 µM DCIP, unless otherwise noted. | ChEMBL. | No reference |
IC50 (binding) | = 420 nM | Enzymatic Assays | BINDINGDB. | No reference |
IC50 (binding) | > 10000 nM | Enzymatic Assays | BINDINGDB. | No reference |
IC50 (binding) | > 30000 nM | Enzymatic Assays | BINDINGDB. | No reference |
IC50 (binding) | > 30000 nM | Enzymatic Assays | BINDINGDB. | No reference |
Many chemical entities in TDR Targets come from high-throughput screenings with whole cells or tissue samples, and not all assayed compounds have been tested against a single a single target protein, probably because they get ruled out during screening process. Even if these compounds may have not been of interest in the original screening, they may come as interesting leads for other screening assays. Furthermore, we may be able to propose drug-target associations using chemical similarities and network patterns.