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TARS adds amino acid to tRNA by a two-step mechanism. First the enzyme binds to both <scene name='Triose_Phosphate_Isomerase/Morph/1'> Threonine </scene> 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. <ref>Lehninger, A. L., Nelson, D. L., & Cox, M. M. (2000). ''Lehninger principles of biochemistry.'' New York: Worth Publishers.</ref> Image below demonstrates the arrow pushing occuring to generate threonine bound tRNA-thr.
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TARS adds amino acid to tRNA by a two-step mechanism. First the enzyme binds to both <scene name='78/786634/Threonine_amino_acid/1'>Threonine</scene> and <scene name='78/786634/Atp/1'>ATP</scene> 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. <ref>Lehninger, A. L., Nelson, D. L., & Cox, M. M. (2000). ''Lehninger principles of biochemistry.'' New York: Worth Publishers.</ref> Image below demonstrates the arrow pushing occuring to generate threonine bound tRNA-thr.
[[Image:TARSmechanism.jpg|left|thumb|300px|'''Arrow pushing of Aminoacylation rxn.<ref>Lehninger, A. L., Nelson, D. L., & Cox, M. M. (2000). ''Lehninger principles of biochemistry.'' New York: Worth Publishers.</ref> ''']]
[[Image:TARSmechanism.jpg|left|thumb|300px|'''Arrow pushing of Aminoacylation rxn.<ref>Lehninger, A. L., Nelson, D. L., & Cox, M. M. (2000). ''Lehninger principles of biochemistry.'' New York: Worth Publishers.</ref> ''']]

Revision as of 19:39, 28 April 2018

Threonyl-tRNA Synthetase/ligase

Human Threonyl tRNA Synthetase bound to L-threoninamide

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Proteopedia Page Contributors and Editors (what is this?)

Khadar Abdi

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