EC Number |
Subunits |
Reference |
---|
1.3.1.91 | ? |
x * 43000, SDS-PAGE |
712368 |
1.3.1.91 | ? |
x * 55000, about, recombinant enzyme, SDS-PAGE |
745924 |
1.3.1.91 | monomer |
1 * 32000, SDS-PAGE |
-, 765758 |
1.3.1.91 | More |
the enzyme is composed of two domains: an N-terminal catalytic domain and a C-terminal tRNA-binding domain |
743952 |
1.3.1.91 | More |
the N-terminal catalytic domain contains the flavin cofactor involved in the reduction of uridine. The second module is the conserved alpha-helical domain known as the tRNA binding domain in HsDus2 homologues. It is connected via a flexible linker to an unusual extended version of a dsRNA binding domain (dsRBD). The catalytic domain binds selectively NADPH but cannot reduce uridine in the absence of the dsRBD. Domain architecture of HsDus2, enzyme MALDI peptide mass finger printing analysis, overview |
745924 |
1.3.1.91 | More |
three-dimensional structure analysis of wild-type and selenomethionine-labeled hDus2 catalytic and tRNA-recognition domains, and modeling, overview |
743940 |