EC Number   |
General Information |
Reference |
|---|
   1.3.1.91 | evolution |
comparison of structure and substrate recognition mechanisms of Thermus thermophilus Dus and Escherichia coli Dus enzymes, overview |
743952 |
| 1.3.1.91 | evolution |
In humans, there are four Dus enzymes. The hDus2 subfamily is proposed to specifically modify U20. The overall fold of the human Dus2 is similar to that of bacterial enzymes, but has a larger recognition domain and a unique three-stranded antiparallel beta-sheet insertion into the catalytic domain that packs next to the recognition domain, contributing to domain-domain interactions |
743940 |
| 1.3.1.91 | evolution |
while in Dus enzymes from bacteria, plants and fungi, tRNA binding is essentially achieved by the alpha-helical domain, in HsDus2 this function is carried out by the dsRNA binding domain (dsRBD) |
745924 |
| 1.3.1.91 | malfunction |
a small interfering RNA against hDUS2 transfected into NSCLC cells suppresses expression of the gene, reduces the amount of dihydrouridine in tRNA molecules, and suppresses growth |
711663 |
| 1.3.1.91 | malfunction |
increased expression of human dihydrouridine synthase 2 (hDus2) is linked to pulmonary carcinogenesis, while its knockdown decreases cancer cell line viability |
743940 |
| 1.3.1.91 | malfunction |
yeast extract from a dus1-DELTA strain is completely defective in modification of yeast pre-tRNAPhe |
713504 |
| 1.3.1.91 | more |
residues that participate in binding to the adapter molecule in EcoDusC are Asn95, Lys139, Arg141, His168 and Arg170. The catalytic cysteine residue is Cys98 |
743952 |
| 1.3.1.91 | more |
the catalytic domain binds selectively NADPH but cannot reduce uridine in the absence of the dsRNA binding domain (dsRBD). HsDus2 catalytic domain structure, overview |
745924 |
| 1.3.1.91 | more |
tRNA binding and the active site structure, overview |
743940 |
| 1.3.1.91 | physiological function |
dihydrouridine is produced by dihydrouridine synthase (Dus) by enzymatic reduction of the C5-C6 bond in uridine |
743940 |
