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In enzymology, a threonine-tRNA ligase is an enzyme that catalyzes the chemical reaction
The three substrates of this enzyme are ATP, L-threonine, and threonine-specific transfer RNA ], whereas its three products are AMP, diphosphate, and L-threonyl-tRNA.
The systematic name of this enzyme class is L-threonine:tRNAThr ligase. 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 TARS.
Threonine—tRNA ligase belongs to the family of ligases, to be specific those forming carbon-oxygen bonds in tRNA and related compounds. More precisely, it belongs to the family of the aminoacyl-tRNA synthetases. These latter enzymes link amino acids to their cognate transfer RNAs in aminoacylation reactions that establish the connection between a specific amino acid and a nucleotide triplet anticodon embedded in the tRNA. During their long evolution, some of these enzymes have acquired additional functions, including roles in RNA splicing, RNA trafficking, transcriptional regulation, translational regulation, and cell signaling.