| Modification Notes |
The fidelity of protein synthesis requires efficient discrimination of amino acid substrates by aminoacyl-tRNA synthetases. Aminoacyl-tRNA synthetases function to catalyze the aminoacylation of tRNAs by their corresponding amino acids, thus linking amino acids with tRNA-contained nucleotide triplets. SerRSmt (seryl-tRNA synthetase, mitochondrial), also known as SARS2 or SARSM, is a 518 amino acid member of the class-II aminoacyl-tRNA synthetase family that catalyzes the tRNASer-serine aminoacylation reaction. Localized to the mitochondria, SerRSmt exists as a homodimer and contains a core catalytic domain and a tRNA-binding domain. SerRSmt catalyzes the attachment of serine to tRNA(Ser) and is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec). Via this interaction, SerRSmt is implicated in selenocysteine (Sec) biosynthesis. |