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In enzymology, an alanine—tRNA ligase (EC 6.1.1.7) is an enzyme that catalyzes the chemical reaction

ATP + L-alanine + tRNAAla ${\displaystyle \rightleftharpoons }$ 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. 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.

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• EC 6.1.1
• Enzymes of known structure
• Ligase stubs