EC Number   |
Inhibitors |
Structure |
|---|
   5.4.99.12 | 5-fluorouracil tRNAPhe |
enzyme forms a covalent adduct with 5-fluorouracil-tRNA to form a putative analog of a steady-state intermediate in the normal reaction pathway. The putative Asp nucleophile is attached to the 6-position of the target 5-fluorouracil-tRNA to form a stable covalent adduct, which can undergo O-acyl hydrolytic cleavage, and the intermediate contains an intact N-glycosidic bond linking the modified base to the polynucleotide chain |
 |
| 5.4.99.12 | 5-fluorouracil tRNAPhe |
time-dependent inactivation of pseudouridine synthase I and formation of a covalent complex with the enzyme that involves the 5-fluorouracil monophosphate at position 39 |
|
| 5.4.99.12 | Calf thymus DNA |
native and denatured, about 66% residual activity |
|
| 5.4.99.12 | Dithionitrobenzoate |
irreversibly inactivates |
  |
| 5.4.99.12 | fluorouracil-substituted tRNA |
causes a time-dependent inactivation of pseudouridine synthase I and forms a covalent complex with the enzyme that involves the fluorouracil-substituted UMP at position 39. Upon incubation of 100 nM pseudouridine synthase with 0.001 mM fluorouracil-substituted tRNA at 15°C prior to addition of substrate, there is a time-dependent inactivation of the enzyme with a half-life of 35 min |
|
| 5.4.99.12 | iodoacetate |
irreversibly inactivates |
|
| 5.4.99.12 | p-chloromercuribenzoate |
irreversibly inactivates |
|
| 5.4.99.12 | poly(rA)n |
71% residual acivity |
|
| 5.4.99.12 | poly(rC)n |
93% residual acivity |
|
| 5.4.99.12 | poly(rG)n |
3.2% residual acivity |
|
