Function/Mechanism
Threonyl t-RNA Synthetase or
Threonyl-tRNA ligase or
TARS is class II
Aminoacyl-tRNA synthetase enzymes. These enzymes primary function are to added the respective amino acid to the respective transfer Ribonucleic Acid (tRNA-AA) The main function of the enzyme is to add Threonine amino acid (Thr) to threonine specific tRNA (tRNA-thr) a necessity prep for the protein synthesis pathway. The structure to th Below displays the overview of the Aminoacylation rxn.
[1]
Overall TARS protein rxn. Substrates includes Adenosine triphosphate (ATP), Threonine (Thr) and threonine specific transfer Ribonucleic Acid (tRNA-thr).
TARS adds amino acid to tRNA by a two-step mechanism. First the enzyme binds to both and in the catalytic domain to perform an adenylation reaction in which pyrophosphate is released as a byproduct. This is then follow up by a transferring Thr from Adenosine monophosphate molecule to 3'OH site of tRNA-thr. [2] Image below demonstrates the arrow pushing occuring to generate threonine bound tRNA-thr.
Arrow pushing of Aminoacylation rxn.[3]
Structural highlights
Evolutionarily related proteins
List to available structures
References
- ↑ Rajendran V, Kalita P, Shukla H, Kumar A, Tripathi T. Aminoacyl-tRNA synthetases: Structure, function, and drug discovery. Int J Biol Macromol. 2018 May;111:400-414. doi: 10.1016/j.ijbiomac.2017.12.157., Epub 2018 Jan 3. PMID:29305884 doi:http://dx.doi.org/10.1016/j.ijbiomac.2017.12.157
- ↑ Lehninger, A. L., Nelson, D. L., & Cox, M. M. (2000). Lehninger principles of biochemistry. New York: Worth Publishers.
- ↑ Lehninger, A. L., Nelson, D. L., & Cox, M. M. (2000). Lehninger principles of biochemistry. New York: Worth Publishers.
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