Aspartate-tRNA ligase

Aspartate-tRNA ligase
This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "Aspartate-tRNA_ligase".

In enzymology, an aspartate-tRNA ligase (EC 6.1.1.12) is an enzyme that catalyzes the chemical reaction

ATP + L-aspartate + tRNAAsp $\rightleftharpoons$ AMP + diphosphate + L-aspartyl-tRNAAsp

The 3 substrates of this enzyme are ATP, L-aspartate, and tRNA(Asp), whereas its 3 products are AMP, diphosphate, and L-aspartyl-tRNA(Asp).

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-aspartate:tRNAAsp ligase (AMP-forming). Other names in common use include aspartyl-tRNA synthetase, aspartyl ribonucleic synthetase, aspartyl-transfer RNA synthetase, aspartic acid translase, aspartyl-transfer ribonucleic acid synthetase, and aspartyl ribonucleate synthetase. This enzyme participates in alanine and aspartate metabolism and aminoacyl-trna biosynthesis.

content

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

Structural studies

As of late 2007, 10 structures have been solved for this class of enzymes, with PDB accession codes 1ASY, 1ASZ, 1B8A, 1C0A, 1EFW, 1EOV, 1EQR, 1G51, 1IL2, and 1L0W.

References

IUBMB entry for 6.1.1.12
BRENDA references for 6.1.1.12 (Recommended.)
PubMed references for 6.1.1.12
PubMed Central references for 6.1.1.12
Google Scholar references for 6.1.1.12
Gangloff J, Dirheimer G (1973). "Studies on aspartyl-tRNA synthetase from Baker's yeast. I Purification and properties of the enzyme". Biochim. Biophys. Acta. 294: 263–72. PMID 4575961.
NORTON SJ, RAVEL JM, LEE C, SHIVE W (1963). "Purification and properties of the aspartyl ribonucleic acid synthetase of Lactobacillus arabinosus". J. Biol. Chem. 238: 269–74. PMID 13939000.