Alanine–tRNA ligase
Class of enzymes
From Wikipedia, the free encyclopedia
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 tRNAAla, whereas its 3 products are AMP, diphosphate, and L-alanyl-tRNAAla.
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
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. doi:10.1016/S0021-9258(18)69922-3. PMID 13672960.
- Webster GC (1961). "Isolation of an alanine-activating enzyme from pig liver". Biochim. Biophys. Acta. 49: 141–152. doi:10.1016/0006-3002(61)90877-0. PMID 13783653.