Valine-tRNA ligase

From Wikipedia, the free encyclopedia

In enzymology, a valine-tRNA ligase (EC 6.1.1.9) is an enzyme that catalyzes the chemical reaction

ATP + L-valine + tRNAVal $\rightleftharpoons$ AMP + diphosphate + L-valyl-tRNAVal

The 3 substrates of this enzyme are ATP, L-valine, and tRNA(Val), whereas its 3 products are AMP, diphosphate, and L-valyl-tRNA(Val).

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

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes 1GAX, 1IVS, 1IYW, 1WK9, and 1WKA.

[edit] References

IUBMB entry for 6.1.1.9
BRENDA references for 6.1.1.9 (Recommended.)
PubMed references for 6.1.1.9
PubMed Central references for 6.1.1.9
Google Scholar references for 6.1.1.9
Berg P, Bergmann FH, Ofengand EJ and 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 and 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.