EC Number |
Reaction |
Reference |
---|
5.4.99.25 | tRNA uridine55 = tRNA pseudouridine55 |
- |
- |
5.4.99.25 | tRNA uridine55 = tRNA pseudouridine55 |
RluA does not require thiol(ate) groups to effect catalysis |
648867 |
5.4.99.25 | tRNA uridine55 = tRNA pseudouridine55 |
the mechanism of uridine55 recognition by Cbf5 and the bacterial TruB are different |
706710 |
5.4.99.25 | tRNA uridine55 = tRNA pseudouridine55 |
the side chain of the conserved tyrosine in the four families of pseudouridine synthases (TruA, TruB, RsuA and RluA) plays a dual role within the active site, maintaining the structural integrity of the active site through its hydrophobic phenyl ring and acting as a general base through its OH group for the proton abstraction required in the last step of pseudouridine synthase-catalyzed formation of pseudouridine |
661179 |
5.4.99.25 | tRNA uridine55 = tRNA pseudouridine55 |
this enzyme recognizes the preformed three-dimensional structure of the T loop primarily through shape complementarity. It accesses its substrate uridyl residue by flipping out the nucleotide and disrupts the tertiary structure of tRNA |
650781 |
5.4.99.25 | tRNA uridine55 = tRNA pseudouridine55 |
this enzyme undergoes significant conformational changes on binding to its substrate. These conformational changes include the ordering of the thumb loop, which binds right into the RNA hairpin loop, and a 10° hinge movement of the C-terminal domain. TruB recognizes its RNA substrate through a combination of rigid docking and induced fit, with TruB first rigidly binding to its target and then maximizing the interaction by induced fit |
653587 |