TABLE 2.
Activity of recombinant U. maydis DHODH-ΔN in the presence of putative inhibitors
| Compound (concn, mM) | Enzyme activitya (%) |
|---|---|
| Brequinar | 85 ± 15 |
| A77-1726 | 108 ± 8 |
| Atovaquone (0.5) | 117 ± 8 |
| Dichloroallyl lawsone | 75 ± 3 |
| Lawsone | 90 ± 4 |
| Menadione | 91 ± 7 |
| Salicylhydroxamic acid | 84 ± 7 |
| Anthranilic acid | 95 ± 7 |
| N-Phenylanthranilic acid (0.1) | 90 ± 3 |
| Coumarin (0.1) | 82 ± 3 |
| 5-Fluorocytosine | 91 ± 8 |
| 5-Fluoroorotate | 98 ± 4 |
| 5-Fluorouracil | 90 ± 3 |
| Quinoxyfen (0.1) | 94 ± 7 |
| Carboxin | 92 ± 2 |
| 3,4-DHB | 87 ± 3 |
| 3,5-DHB | 98 ± 3 |
a
Relative initial velocities were determined in chromogen reduction assays with 1 mM DHO as the substrate and 0.1 mM DCIP as the acceptor. The enzyme activity without an inhibitor was set at 100%, and values are expressed as mean percentages ± standard errors of the means. For compounds dissolved in DMSO or ethanol, the respective solvent was added to the control. If not otherwise stated, the concentration of tested compounds was 1 mM.