Leucine—tRNA ligase

In enzymology, a leucine—tRNA ligase (EC 6.1.1.4) is an enzyme that catalyzes the chemical reaction

ATP + L-leucine + tRNALeu ${\displaystyle \rightleftharpoons }$ AMP + diphosphate + L-leucyl-tRNALeu

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

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 L-leucine:tRNALeu 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 1WKB, 1WZ2, 2AJG, 2AJH, and 2AJI.

See also

• Leucyl-tRNA synthetase

References

• ALLEN EH, GLASSMAN E, SCHWEET RS (1960). "Incorporation of amino acids into ribonucleic acid. I. The role of activating enzymes". J. Biol. Chem. 235: 1061–7. PMID 13792726.
• Berg P, Bergmann FH, Ofengand EJ, Dieckmann M (1961). "The enzymic synthesis of amino acyl derivatives of ribonucleic acid I. The mechanism of leucyl-, valyl-, isoleucyl- and methionyl ribonucleic acid formation". J. Biol. Chem. 236: 1726–1734.
• Bergmann FH, Berg P, Dieckmann M (1961). "The enzymic synthesis of amino acyl derivatives of ribonucleic acid II. The preparation of leucyl-, valyl-, isoleucyl- and methionyl ribonucleic acid synthetases from Escherichia coli". J. Biol. Chem. 236: 1735–1740.

This page was last edited on 26 August 2023, at 14:44