EC Number   |
General Information |
Reference |
|---|
   2.7.7.87 | malfunction |
the loss of SUA5 causes increased leaky scanning through AUG codons, +1 frameshifting, and nonsense suppression. In addition, the loss of SUA5 amplifies the 20S RNA virus found in Saccharomyces cerevisiae, possibly through an internal ribosome entry site-mediated mechanism |
725958 |
| 2.7.7.87 | physiological function |
L-threonylcarbamoyladenylate is a modified nucleotide found in all tRNAs decoding codons starting with adenosine, its role is to facilitate codonanticodon pairing and to prevent frameshifting during protein synthesis |
726075 |
| 2.7.7.87 | physiological function |
t6A is a universally conserved tRNA modification found at position 37 in the anticodon loop of a subset of tRNA, structural studies predict an important role for t6A in translational fidelity |
725467 |
| 2.7.7.87 | physiological function |
the eukaryotic L-threonylcarbamoyladenylate biosynthesis system functions first through Sua5, which generates threonylcarbamoyl-adenylate using its adenylation function and then secondly through Qri7, which binds to threonylcarbamoyl-adenylate to conjugate the threonyl-carbamoyl moiety onto directly bound tRNA substrates |
726076 |
| 2.7.7.87 | physiological function |
the Sua5 protein is essential for normal translational regulation in yeast |
725958 |
| 2.7.7.87 | physiological function |
threonylcarbamoyladenosine is a universal modification found at position 37 of ANN decoding tRNAs, which imparts a unique structure to the anticodon loop enhancing its binding to ribosomes in vitro |
723287 |
| 2.7.7.87 | physiological function |
YrdC, with many of the properties of a putative threonylcarbamoyl transferase, most likely functions as a component of a heteromultimeric protein complex for threonylcarbamoyladenosine biosynthesis |
723758 |
