Leucine—tRNA ligase

leucine-tRNA ligase
Identifiers
EC number 6.1.1.4
CAS number 9031-15-6
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO

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

ATP + L-leucine + tRNALeu \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

References

    This article is issued from Wikipedia - version of the Thursday, March 31, 2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.