EC Number | Cloned (Comment) | Organism |
---|---|---|
2.7.7.52 | expressed in Escherichia coli Gold (DE3) cells | Drosophila melanogaster |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
2.7.7.52 | enzyme residues 202-560 and enzyme in complex with RNA stretches 5 -AGU-3 and 5 -AGUU-3 , sitting drop vapor diffusion method, using 0.1 M Tris-HCl, pH 8.4, 50 mM NaCl, 0.2 M lithium sulfate monohydrate and 15% (w/v) PEG3350 | Drosophila melanogaster |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
2.7.7.52 | H294A | the enzymatic activity of the mutant is reduced by about 61% as compared to the wild type enzyme | Drosophila melanogaster |
2.7.7.52 | N347A | the uridylation efficiency of the mutant is reduced dramatically to about 7% when compared with that of wild type enzyme | Drosophila melanogaster |
2.7.7.52 | R295A | the enzymatic activity of the mutant is reduced by about 84% as compared to the wild type enzyme | Drosophila melanogaster |
2.7.7.52 | R295K | the enzymatic activity of the mutant is reduced by about 80% as compared to the wild type enzyme | Drosophila melanogaster |
2.7.7.52 | R327A | the uridylation efficiency of the mutant is reduced dramatically to about 4% when compared with that of wild type enzyme | Drosophila melanogaster |
2.7.7.52 | R327K | the uridylation efficiency of the mutant is reduced dramatically to about 4% when compared with that of wild type enzyme | Drosophila melanogaster |
2.7.7.52 | V328I | the mutation barely affects the enzyme's binding with RNA substrate and also exhibits a obvious reduction in uridylation efficiency as compared to the wild type enzyme | Drosophila melanogaster |
2.7.7.52 | V328L | the mutation entirely abolishes the enzyme's catalytic activity for truncated miR-1003 bearing 3'G. The mutation barely affects the enzyme's binding with RNA substrate | Drosophila melanogaster |
2.7.7.52 | V328R | the mutation entirely abolishes the enzyme's catalytic activity for truncated miR-1003 bearing 3'G. The mutation barely affects the enzyme's binding with RNA substrate | Drosophila melanogaster |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
2.7.7.52 | Mg2+ | required | Drosophila melanogaster |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.7.7.52 | UTP + miR-1003 RNAn | Drosophila melanogaster | - |
diphosphate + miR-1003 RNAn+1 | - |
? | |
2.7.7.52 | UTP + RNAn | Drosophila melanogaster | the enzyme exhibits an intrinsic preference for RNA substrates ending in 3'G | diphosphate + RNAn+1 | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.7.7.52 | Drosophila melanogaster | Q9VI58 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.7.7.52 | Ni-NTA column chromatography, HiTrap heparin column chromatography and Superdex 200 gel filtration | Drosophila melanogaster |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.7.7.52 | UTP + 5'-Cy5-GUGGGUAUCUGGGAGAUUACAUAUUCACAG-3' | - |
Drosophila melanogaster | ? | - |
? | |
2.7.7.52 | UTP + 5-Cy5-CAUAUUCACAG-3' | - |
Drosophila melanogaster | ? | - |
? | |
2.7.7.52 | UTP + miR-1003 RNAn | - |
Drosophila melanogaster | diphosphate + miR-1003 RNAn+1 | - |
? | |
2.7.7.52 | UTP + mirtronRNAn | the enzyme preferentially catalyzes the uridylation of mirtronRNAs ending in 3'G and 3'U | Drosophila melanogaster | diphosphate + mirtronRNAn+1 | - |
? | |
2.7.7.52 | UTP + RNAn | the enzyme exhibits an intrinsic preference for RNA substrates ending in 3'G | Drosophila melanogaster | diphosphate + RNAn+1 | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.7.7.52 | Tailor | - |
Drosophila melanogaster |
2.7.7.52 | terminal uridylyl transferase | - |
Drosophila melanogaster |
2.7.7.52 | TUTase | - |
Drosophila melanogaster |
EC Number | General Information | Comment | Organism |
---|---|---|---|
2.7.7.52 | metabolism | the enzyme plays a crucial role as the repressor in the biogenesis pathway of splicing-derived mirtron pre-miRNAs | Drosophila melanogaster |