Asparagine—tRNA ligase
| asparagine-tRNA ligase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 6.1.1.22 | ||||||||
| CAS no. | 37211-76-0 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, an asparagine-tRNA ligase (EC 6.1.1.22) is an enzyme that catalyzes the chemical reaction
- ATP + L-asparagine + tRNAAsn AMP + diphosphate + L-asparaginyl-tRNAAsn
The 3 substrates of this enzyme are ATP, L-asparagine, and tRNA(Asn), whereas its 3 products are AMP, diphosphate, and L-asparaginyl-tRNA(Asn).
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-asparagine:tRNAAsn ligase (AMP-forming). Other names in common use include asparaginyl-tRNA synthetase, asparaginyl-transfer ribonucleate synthetase, asparaginyl transfer RNA synthetase, asparaginyl transfer ribonucleic acid synthetase, asparagyl-transfer RNA synthetase, and asparagine translase. This enzyme participates in alanine and aspartate metabolism and aminoacyl-trna biosynthesis.
Structural studies
[edit]As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1X54, 1X55, and 1X56.
References
[edit]- Davies MR, Marshall RD (1972). "Partial purification of L-asparaginyl-tRNA synthetase from rabbit liver". Biochem. Biophys. Res. Commun. 47 (6): 1386–95. doi:10.1016/0006-291X(72)90226-4. PMID 5040239.
