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Leucine–tRNA ligase

In enzymology, a leucine–tRNA ligase () is an enzyme that catalyzes the chemical reaction

ATP + -leucine + tRNA AMP + diphosphate + -leucyl-tRNA

The 3 substrates of this enzyme are ATP, -leucine, and tRNA, whereas its 3 products are AMP, diphosphate, and -leucyl-tRNA.

This enzyme belongs to the family of ligases, to be specific those forming carbon–oxygen bonds in aminoacyl-tRNA and related compounds. The systematic name of this enzyme class is -leucine:tRNA ligase (AMP-forming). Other names in common use include leucyl-tRNA synthetase, leucyl-transfer ribonucleate synthetase, leucyl-transfer RNA synthetase, leucyl-transfer ribonucleic acid synthetase, leucine-tRNA synthetase, and leucine translase. This enzyme participates in valine, leucine and isoleucine biosynthesis and aminoacyl-tRNA biosynthesis.

Structural studies

As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes , , , , and .

See also

References