Alanine—tRNA ligase
| alanine-tRNA ligase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 6.1.1.7 | ||||||||
| CAS number | 9031-71-4 | ||||||||
| 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 alanine-tRNA ligase (EC 6.1.1.7) is an enzyme that catalyzes the chemical reaction
- ATP + L-alanine + tRNAAla AMP + diphosphate + L-alanyl-tRNAAla
The 3 substrates of this enzyme are ATP, L-alanine, and tRNA(Ala), whereas its 3 products are AMP, diphosphate, and L-alanyl-tRNA(Ala).
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-alanine:tRNAAla ligase (AMP-forming). Other names in common use include alanyl-tRNA synthetase, alanyl-transfer ribonucleate synthetase, alanyl-transfer RNA synthetase, alanyl-transfer ribonucleic acid synthetase, alanine-transfer RNA ligase, alanine transfer RNA synthetase, alanine tRNA synthetase, alanine translase, alanyl-transfer ribonucleate synthase, AlaRS, and Ala-tRNA synthetase. This enzyme participates in alanine and aspartate metabolism and aminoacyl-trna biosynthesis.
See also
- Sticky mouse - mutation in the gene
Structural studies
As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes 1RIQ, 1V4P, 1YFR, 1YFS, 1YFT, 1YGB, and 2E1B.
References
- HOLLEY RW, GOLDSTEIN J (1959). "An alanine-dependent, ribonuclease-inhibited conversion of adenosine 5'-phosphate to adenosine triphosphate. II. Reconstruction of the system from purified components". J. Biol. Chem. 234 (7): 1765–8. PMID 13672960.
- Webster GC (1961). "Isolation of an alanine-activating enzyme from pig liver". Biochim. Biophys. Acta. 49: 141–152. PMID 13783653. doi:10.1016/0006-3002(61)90877-0.