Isoleucine-tRNA ligase

Isoleucine-tRNA ligase (also known as Isoleucyl-tRNA synthetase or IleRS) is an enzyme that plays a crucial role in the protein synthesis process in living organisms. It belongs to the class of aminoacyl-tRNA synthetase enzymes, which are responsible for attaching specific amino acids to their corresponding transfer RNA (tRNA) molecules. This process is essential for the translation of genetic code into proteins.

Function

Isoleucine-tRNA ligase catalyzes the attachment of the amino acid isoleucine to its corresponding tRNA molecule (tRNA^Ile). This reaction involves two steps: the activation of the amino acid and the transfer of the activated amino acid to the tRNA. The enzyme uses adenosine triphosphate (ATP) as a source of energy for the reaction.

Structure

Like other aminoacyl-tRNA synthetases, Isoleucine-tRNA ligase is a large protein complex. It consists of multiple subunits, each of which contributes to the overall function of the enzyme. The exact structure of Isoleucine-tRNA ligase can vary between different species, but all versions of the enzyme share a common core structure that is necessary for their function.

Clinical Significance

Mutations in the gene encoding Isoleucine-tRNA ligase can lead to various health conditions. For instance, a rare genetic disorder called Charcot-Marie-Tooth disease has been associated with mutations in the IARS gene in humans. This condition affects the peripheral nerves and can cause muscle weakness and sensory loss.

See Also

• Aminoacyl-tRNA synthetase
• Protein synthesis
• Transfer RNA
• Charcot-Marie-Tooth disease

References

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