Threonine-tRNA ligase

In enzymology, a threonine-tRNA ligase is an enzyme that catalyzes the chemical reaction


 * ATP + L-threonine + tRNAThr $$\rightleftharpoons$$ AMP + diphosphate + L-threonyl-tRNAThr

The 3 substrates of this enzyme are ATP, L-threonine, and tRNA(Thr), whereas its 3 products are AMP, diphosphate, and L-threonyl-tRNA(Thr).

This enzyme belongs to the family of ligases, specifically those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. The systematic name of this enzyme class is L-threonine:tRNAThr ligase (AMP-forming). Other names in common use include threonyl-tRNA synthetase, threonyl-transfer ribonucleate synthetase, threonyl-transfer RNA synthetase, threonyl-transfer ribonucleic acid synthetase, threonyl ribonucleic synthetase, threonine-transfer ribonucleate synthetase, threonine translase, threonyl-tRNA synthetase, and TRS. This enzyme participates in glycine, serine and threonine metabolism and aminoacyl-trna biosynthesis.

Structural studies
As of late 2007, 17 structures have been solved for this class of enzymes, with PDB accession codes, , , , , , , , , , , , , , , , and.