Aminoacyl-tRNA synthetase

An enzyme that uses ATP to attach a specific amino acid to its corresponding transfer RNA. Its accuracy helps ensure that ribosomes incorporate the correct amino acids during protein synthesis.

Aminoacylation: The ATP-dependent attachment of an amino acid to a molecule, commonly a transfer RNA. This is the reaction catalyzed by aminoacyl-tRNA synthetases.
Transfer RNA: An RNA molecule that carries an amino acid to the ribosome and pairs its anticodon with a messenger RNA codon. Each synthetase recognizes particular tRNA identities for charging.
Ribosomal decoding: The ribosome’s selection of transfer RNAs through codon–anticodon pairing during translation. Decoding checks the tRNA anticodon, whereas synthetases determine which amino acid the tRNA carries.
Aminoacyl-tRNA synthetase-related disease: A disorder caused by altered function of an aminoacyl-tRNA synthetase or its associated protein. Mutations in these enzymes can disrupt translation or specialized cellular functions.
Paul Schimmel: An American biochemist known for research on aminoacyl-tRNA synthetases and their roles beyond translation. His work helped establish synthetases as multifunctional proteins, not merely tRNA-charging enzymes.
Aminoacyl-AMP: An activated amino acid linked to AMP, formed as an intermediate during tRNA charging. The enzyme forms this intermediate before transferring the amino acid to tRNA.
Amino acid: An organic molecule with amino and carboxyl groups; amino acids are the monomers of proteins. The synthetase selects one amino acid type for attachment to its tRNA.
Nonribosomal peptide synthetase: A modular enzyme system that assembles peptides without ribosomes or messenger RNA templates. It activates amino acids for peptide synthesis through a distinct, template-independent pathway.
FARS2 deficiency: A mitochondrial disorder caused by pathogenic variants in the gene encoding mitochondrial phenylalanyl-tRNA synthetase. It illustrates how a synthetase defect can impair mitochondrial protein synthesis.
Class I aminoacyl-tRNA synthetase: A synthetase class generally defined by a Rossmann-like fold and characteristic HIGH and KMSKS sequence motifs. This major structural class contrasts with the distinct architecture of class II enzymes.

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