Aspartate—tRNA ligase

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aspartate-tRNA ligase
Identifiers
EC number 6.1.1.12
CAS number 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 / EGO

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, 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[edit]

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[edit]

References[edit]

  • 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. PMID 13939000.