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Leucine—tRNA ligase

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Leucine—tRNA ligase
Identifiers
EC no.6.1.1.4
CAS no.9031-15-6
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
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PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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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

References

Enzymes: CO CS and CN ligases (EC 6.1-6.3)
6.1: Carbon-Oxygen
6.2: Carbon-Sulfur
6.3: Carbon-Nitrogen
Enzymes
Activity
Regulation
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