"Ile tRNA Ligase" is a biological term used to refer to an enzyme that catalyzes the charging of transfer RNA (tRNA) with isoleucine amino acid. The spelling of the word "Ile tRNA Ligase" is in accordance with the International Phonetic Alphabet (IPA), which represents the sounds of spoken language. "Ile" stands for isoleucine, the amino acid, while "tRNA" is pronounced /tiː aɹ ɛn eɪ/ and "Ligase" is pronounced /laɪgeɪs/. The correct spelling of this term is important for clear communication in biological research.
Ile tRNA ligase is an enzyme that is responsible for the activation and charging of specific transfer RNA (tRNA) molecules with the amino acid isoleucine. It belongs to the class of ligases, which are enzymes involved in catalyzing the joining of two molecules through the formation of a chemical bond.
Isoleucine transfer RNA ligase ensures that the isoleucine amino acid is properly attached to its corresponding tRNA molecule, thus ensuring correct protein synthesis during translation. This enzyme plays a vital role in the process of protein synthesis by attaching the appropriate amino acid to the correct tRNA.
The activation of tRNA involves the addition of AMP (Adenosine Monophosphate) to the 3' end of the molecule, forming a high-energy bond called an aminoacyl-tRNA. This step is essential for the subsequent binding of the tRNA to the ribosome, where the amino acid will be incorporated into a growing polypeptide chain.
Ile tRNA ligase specifically recognizes the tRNA molecule that carries the anticodon sequence complementary to the mRNA codon for isoleucine. Through a series of enzymatic reactions, it catalyzes the attachment of isoleucine to the tRNA molecule, ensuring accurate translation during protein synthesis.
Overall, Ile tRNA ligase plays a crucial role in maintaining the fidelity of protein synthesis by ensuring the correct pairing of the isoleucine amino acid with its corresponding tRNA molecule.