Aspartate—tRNA ligase

Aspartate—tRNA ligase
Identifiers
EC no.	6.1.1.12
CAS no.	9027-32-1
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 / QuickGO
Search PMC articles PubMed articles NCBI proteins

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

ATP + L-aspartate + tRNAAsp ${\displaystyle \rightleftharpoons }$ 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, to be specific 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.

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.

See also

• DARS (gene)

References

• 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 (1): 263–72. doi:10.1016/0005-2787(73)90298-0. 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. doi:10.1016/S0021-9258(19)83990-X. PMID 13939000.