Neidigh, Jonathan W. published the artcileCloning and Characterization of Rhodotorula glutinis Thymine Hydroxylase, Quality Control of 608-34-4, the publication is Chemical Research in Toxicology (2009), 22(5), 885-893, database is CAplus and MEDLINE.
Thymine hydroxylase (TH) is a member of the α-ketoglutarate-dependent nonheme iron dioxygenase family that includes a series of DNA repair proteins including alkB. Substantial interest in this family of enzymes derives from their capacity to modify DNA bases and precursors by oxidation Previously, a sequence has been published for cloned Rhodotorula glutinis TH. However, the minimal reported activity of this enzyme, coupled with inconsistencies with previously published mass spectrometry data, compelled us to reexamine TH. The sequence reported here differs from the previously reported sequence at two amino acid positions and is consistent with previously reported mass spectrometry data. The cloned enzyme characterized in this report displayed substantial activity, indicating that the sequence differences are critical for activity. The substrate selectivity of TH against a series of pyrimidine analogs is consistent with that reported for the wild-type enzyme and, in part, explains the mode of selection of uracil analogs. A preliminary model of the active site has been constructed for the purposes of comparing TH with other members of this family. TH and alkB share in common the capacity to oxidize N-Me groups. However, TH has the added capacity to oxidize the 5-Me group of thymine, a property that is potentially important for enzymes that could act on DNA and modify DNA-protein interactions.
Chemical Research in Toxicology published new progress about 608-34-4. 608-34-4 belongs to pyrimidines, auxiliary class Pyrimidine,Amide, name is 3-Methylpyrimidine-2,4(1H,3H)-dione, and the molecular formula is C5H6N2O2, Quality Control of 608-34-4.
Referemce:
https://pubchem.ncbi.nlm.nih.gov/compound/Pyrimidine,
Pyrimidine – Wikipedia