Leucine–tRNA ligase, cytoplasmic, also called leucyl-tRNA synthetase 1, is an enzyme that in humans is encoded by the LARS1 gene (previously LARS). Like the related enzyme, LARS2, this enzyme functions as a Leucine–tRNA ligase, which means it attaches the amino acid leucine to its corresponding transfer RNA (tRNALeu), which is needed for RNA-to-protein translation.

Function This gene encodes a cytosolic leucine-tRNA synthetase, a member of the class I aminoacyl-tRNA synthetase family. The encoded enzyme catalyzes the ATP-dependent ligation of L-leucine to tRNA(Leu). It is found in the cytoplasm as part of a multisynthetase complex and interacts with the arginyl-tRNA synthetase through its C-terminal domain. Alternatively spliced transcript variants of this gene have been found; however, their full-length nature is not known.

Interactions

Leucyl-tRNA synthetase has been shown to interact with EEF1G.

Inhibitors BC-LI-0186 Tavaborole

Medical significance Pathogenic (homozygous) mutations in LARS1 are associated with symptoms including acute liver failure in the first year of life, and called infantile liver failure syndrome-1 (ILFS1).

See also Leucine-tRNA ligase

References

Further reading